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The Effect of Hypoxia on the Expression of CXC Chemokines and CXC Chemokine Receptors—A Review of Literature

Jan Korbecki, Klaudyna Kojder, Patrycja Kapczuk and 5 more

International Journal of Molecular Sciences · 2021 · Review · CC BY

doi:10.3390/ijms22020843

Abstract

Hypoxia is an integral component of the tumor microenvironment. Either as chronic or cycling hypoxia, it exerts a similar effect on cancer processes by activating hypoxia-inducible factor-1 (HIF-1) and nuclear factor (NF-κB), with cycling hypoxia showing a stronger proinflammatory influence. One of the systems affected by hypoxia is the CXC chemokine system. This paper reviews all available information on hypoxia-induced changes in the expression of all CXC chemokines (CXCL1, CXCL2, CXCL3, CXCL4, CXCL5, CXCL6, CXCL7, CXCL8 (IL-8), CXCL9, CXCL10, CXCL11, CXCL12 (SDF-1), CXCL13, CXCL14, CXCL15, CXCL16, CXCL17) as well as CXC chemokine receptors—CXCR1, CXCR2, CXCR3, CXCR4, CXCR5, CXCR6, CXCR7 and CXCR8. First, we present basic information on the effect of these chemoattractant cytokines on cancer processes. We then discuss the effect of hypoxia-induced changes on CXC chemokine expression on the angiogenesis, lymphangiogenesis and recruitment of various cells to the tumor niche, including myeloid-derived suppressor cells (MDSCs), tumor-associated macrophages (TAMs), tumor-associated neutrophils (TANs), regulatory T cells (Tregs) and tumor-infiltrating lymphocytes (TILs). Finally, the review summarizes data on the use of drugs targeting the CXC chemokine system in cancer therapies.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 19, 2026. Paragraph numbers are ours, so an answer can point at one.

1. Introduction

1Growing standards of living and advances in medicine in many countries have resulted in increased life expectancies. This has led to the spread of other diseases, particularly “civilization diseases” which are associated with lifestyle and environmental pollution, and diseases related to old age. One of these is cancer, a major problem in developed countries and the cause of 55.9 million deaths worldwide in 2017—a 25% increase when compared to 2007. This trend has led to the intensification of efforts aimed at developing more effective therapeutic approaches.

2The last 15 years have seen an increasing interest in the tumor microenvironment—a set of factors affecting a cancer cell in a tumor. One of these are noncancer cells recruited to a tumor niche, with the recruitment process depending on factors secreted from cells already located in the tumor niche. These include factors changing the recruited cell into a tumor-associated cell—i.e., transforming the cell into an element which supports cancer processes. Both cancer and noncancer cells secrete a number of factors which shape the tumor microenvironment, including chemoattractant cytokines, also known as chemokines. Changes in the expression of chemokines affect the recruitment of cells to the tumor niche, angiogenesis and migration of cancer cells. For this reason, understanding the role of chemokines in cancer processes seems crucial for understanding the functioning of a tumor. There is a lack of research on the influence of hypoxia, i.e., tumor-specific conditions, on CXC chemokines and so the aim of this review was to collect all literature data on the influence of hypoxia on the expression of CXC chemokines in a tumor.

2. Hypoxia in a Tumor

3Tumors are associated with two kinds of hypoxia—chronic hypoxia (also known as continuous or noninterrupted hypoxia) and cycling hypoxia (intermittent or transient hypoxia). Chronic hypoxia is a persistent reduction in oxygen levels that results from an excessive distance between cells and vascular vessels whose growth cannot keep up with the rapid growth of the tumor. Cycling hypoxia has cyclic episodes of oxygen deficiency interspersed with periods of reoxygenation—a result of structural abnormalities in the vascular vessels, particularly the lack of a conventional hierarchy (Figure 1). In such vessels, the blood flow often changes route, resulting in hypoxia in some areas of the tumor. Then, when the blood flow changes its route again, some areas become reoxygenated. One such cycle of hypoxia lasts from several minutes to 4 h, depending on the selected research model.

4Both types of hypoxia change the expression of similar genes as they activate the same transcription factors—hypoxia-inducible factors (HIFs) and nuclear factor κB (NF-κB). The mechanisms of activation, however, are different. In chronic hypoxia, the main role is played by a reduction in oxygen levels which triggers a drop in the activity of oxygen-dependent enzymes. In cycling hypoxia, transcription factors are activated mainly by reactive oxygen species (ROS).

5Hypoxia-inducible factors (HIF-1, HIF-2 and HIF-3) exhibit transcriptive activity that is regulated by the proteolytic degradation of subunit α (HIF-1α and HIF-2α). This degradation occurs due to the hydroxylation of HIF-1α and HIF-2α in proline residues by prolyl hydroxylase (PHD), which leads to the ubiquitination by von Hippel-Lindau protein (pVHL) and then to proteolytic degradation of these HIF-α subunits. PHD are oxygen-dependent enzymes (Figure 2). For this reason, in chronic hypoxia, there is a decrease in PHD activity which leads to a decrease in HIF-α hydroxylation of proline residues and a decrease in proteolytic degradation of these HIF subunits. HIF-1α reaches the maximum level in a cell after 6 h of chronic hypoxia, whereas HIF-2α reaches this after 48 h. The expressions of PHD2 and PHD3 are increased by HIF-1 and HIF-2, which makes HIF-α degrade more intensely during reoxygenation. In turn, cycling hypoxia increases the level of ROS, which oxidizes the iron atoms in PHD and thus reduces the activity of these enzymes. This leads to a drop in the hydroxylation of proline residues on HIF-α, which means that HIF-α is no longer degraded but accumulated instead. The increase in HIF-1α levels during cycling hypoxia also occurs via other pathways—for example, the ROS-dependent activation of protein kinase A (PKA) phosphorizes this HIF-1 subunit thereby increasing its stability. A ROS-dependent increase in calcium ion concentration in cytoplasm, the activation of protein kinase C (PKC) and the mammalian target of rapamycin (mTOR) are also significant. In cycling hypoxia, the accumulation of HIF-1α increases with the successive cycles of oxygen deficiency. However, this protein is completely degraded during episodes of reoxygenation.

6The regulation of HIF transcriptional activity also involves factor inhibiting HIF (FIH), an enzyme which causes the hydroxylation of asparagine residue and thus disrupts the interaction of HIF-α with the CBP/p300 coactivator. In this way, FIH blocks the expression of HIF/CBP/p300-dependent genes. As FIH is an oxygen-dependent enzyme, its activity is reduced by chronic hypoxia and ROS which oxidize the iron atom—a part of the enzyme that is critical for its function. FIH requires a much lower level of oxygen for its activity than PHD (Km for FIH is 90 μM, whereas for PHD it is 230–250 μM). For this reason, in moderate hypoxia, the HIF pathway is inhibited by FIH but not by PHD.

7Both types of hypoxia also activate NF-κB. In chronic hypoxia, this activation is dependent, among other things, on a reduction in the amount of oxygen and the ensuing reduction in the activity of PHD, an enzyme that inhibits the activation of NF-κB and HIF. The activation of NF-κB in chronic hypoxia also depends on the activation of calcium/calmodulin-dependent kinase 2 (CaMK2). In contrast, in cycling hypoxia, NF-κB activation is ROS-dependent.

8In chronic hypoxia, the activation of NF-κB results in an increased expression of HIF-1α and therefore has a significant effect on the HIF activation pathway. This is related to the occurrence of the NF-κB binding site in the HIF1A gene promoter. For this reason, during chronic hypoxia, the expression of genes is directly induced by NF-κB. There is also an increase in the expression of genes directly dependent on HIF-1α but these are also indirectly dependent on NF-κB during chronic hypoxia. Therefore, in order to acquire a detailed insight into the mechanism which induces the expression of a given gene by chronic hypoxia, it is necessary to demonstrate the occurrence and investigate the functionality of the hypoxia responsive element (HRE) binding HIF or the NF-κB binding site. Importantly, chronic hypoxia and inflammation exclude each other by various mechanisms, and so chronic hypoxia reduces the inflammatory response. On the other hand, some proinflammatory genes are induced by both chronic hypoxia and inflammation. Cycling hypoxia is more proinflammatory than chronic hypoxia. This is related to the activation of NF-κB by ROS. For this reason, NF-κB plays a more important role in gene expression during cycling hypoxia than in chronic hypoxia.

9Hypoxia significantly changes the functioning of the tumor. Its proapoptotic effect on cells results in a selection of cells in terms of apoptosis resistance, a process which is important at the beginning of tumor development and results in the presence of cancer cells with a p53 dysfunction in the tumor. Hypoxia also participates in the progression of cancer at further stages of the process. In particular, hypoxia is important in the functioning of cancer stem cells (CSCs), which increase the resistance of the tumor to anticancer therapy. Hypoxia also causes cancer cell migration, invasion and metastasis, partly due to hypoxia causing the epithelial-to-mesenchymal transition (EMT). For this reason, areas of chronic hypoxia are often associated with neoplastic cell metastasis.

10Tissues respond to oxygen deficiency by developing new blood vessels. In this way, hypoxia increases the expression of proangiogenic factors such as vascular endothelial growth factor (VEGF)-A, platelet-derived growth factor subunit A (PDGF-A), transforming growth factor-β (TGF-β) and angiopoietin-like 4 (ANGPTL4). Hypoxia also participates in tumor immune evasion by polarizing macrophages to the M2 phenotype which silences the immune response. It also protects cancer cells by impairing the function of NK cells and increasing the production of immunosuppressive proteins such as indoleamine 2,3-dioxygenase (IDO), human leukocyte antigen-G (HLA-G), programmed death-ligand 1 (PD-L1) and metabolites such as adenosine. The hypoxia-induced acidosis of the cancer microenvironment, which is caused by an increased production and secretion of lactate is also important. Lactate causes tumor immune evasion and neoplastic cell migration.

11Hypoxia also affects the CXC chemokine system, which leads to changes in the level of these chemoattractant cytokines in the cancer microenvironment. CXC chemokines participate in the growth of the tumor due to a number of procancer properties.

12HIF-1α accumulation and increased HIF-1 transcriptional activity occurs in cancer cells even in normoxia. This is related to, among other things, mutations in the VHL gene which encodes pVHL, resulting in the loss of biological function of pVHL, thereby reducing the degradation of HIF-1α. Tumors also exhibit deletions of parts of the chromosome where the HIF1AN gene locus are located. This gene encodes FIH-1, the enzyme responsible for inhibiting the transcriptional activity of HIF-1. Another way of activating the HIF-1 pathway under normoxia is HIF-1α phosphorylation which leads to the increased stability of this protein and consequently, to HIF-1α accumulation in cells and increased expression of HIF-1dependent genes. Enzymes performing such phosphorylation under normoxia include PKA activated by cAMP, phosphatidylinositol-4,5-bisphosphate 3-kinase (PI3K), extracellular signal-regulated kinase (ERK) mitogen-activated protein kinase (MAPK). HIF-1α is also phosphorylated by glycogen synthase kinase 3 which reduces the stability of this protein. Apart from phosphorylation, other types of post-translational modifications also affect the activation of HIF-1 under normoxia. One of them is the deacetylation of HIF-1α by sirtuin 1 (SIRT1), which leads to a decrease in HIF-1 transcriptional activity. In addition to the post-translational modification, the activation of NF-κB in normoxia also increases the expression of HIF-1α, which is important for an increase in the activation of HIF-1 during inflammatory reactions. The elevated activation of HIF-1 via these pathways in normoxia increases the expression of genes dependent on this transcriptional factor. Although there are no studies in this area that confirm it, it is possible that this mechanism is responsible for the increase in the expression of CXC chemokines and CXC chemokine receptors in normoxia.

3. CXC Chemokines in Cancer

13CXC chemokines (also known as α-chemokines) are a subfamily of chemotactic cytokines with a CXC motif at the N-terminus. Currently, we know 17 CXC chemokines, of which CXC motif chemokine ligand (CXCL)15 is a murine CXC chemokine not found in humans. As such, it is not mentioned in Table 1 which shows the procancer and anticancer properties of CXC chemokines. The chemokines from this subfamily activate the CXC motif chemokine receptors (CXCRs)1–8 (Table 1). The receptor for CXCL14 is not clearly established. It seems that CXCL14 is a CXCR4 antagonist. However, subsequent studies have shown that CXCL14 may not directly affect CXCR4. Other studies have shown that the receptors for CXCL14 may be G-protein coupled receptor 85 (GPR85), toll-like receptor (TLR)9 after the formation of a complex of CXCL14 with CpG oligodeoxynucleotide, and insulin-like growth factor I receptor (IGF-IR).

14CXC chemokines differ in their effect on angiogenesis. Seven of them (CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL7, and CXCL8), with an additional ELR motif, mainly induce angiogenesis via CXCR2. VEGF activity also induces an increase in the expression of CXCL1 and CXCL8 in endothelial cells which enhances angiogenesis. In contrast, CXCL4, CXCL9, CXCL10 and CXCL11 exert an angiostatic effect via their CXCR3 receptor. One of them, CXCL4, has been shown to inhibit lymphangiogenesis, and so it can be inferred that the remaining CXCR3 ligands may have the same properties. Another CXC chemokine, CXCL12, has angiogenic properties, and its actions are associated with VEGF, which increases the expression of CXCR4 (receptor of CXCL12) on endothelial cells, which in turn enhances the influence of CXCL12 on these cells. CXCL12 induces an increase in VEGF expression in endothelial cells and thus indirectly enhances angiogenesis. The activation of CXCR4 on a tumor cell also causes an increase in VEGF-C expression, leading to lymphangiogenesis. Of the remaining CXC chemokines, CXCL13 interferes with the action of basic fibroblast growth factor (bFGF) which inhibits angiogenesis, CXCL14 also has angiostatic properties and CXCL16 is an angiogenic chemokine, similar to CXCL17, a chemoattractant for monocytes and macrophages in which it increases the expression of VEGF-A.

15CXC chemokines can cause a migration and invasion of tumor cells. CXCR3 ligands either induce or inhibit migration of tumor cells, depending on whether CXCR3-A or CXCR3-B is activated. CXCL14, depending on the research model, can have anticancer properties and procancer properties.

16Akin to other chemokines, CXC chemokines participate in the recruitment of cells to the tumor niche but what makes them different is their distinct ability to recruit tumor-associated neutrophils (TANs). Apart from TAN, they recruit myeloid-derived suppressor cells (MDSCs), tumor-associated macrophages (TAMs), mesenchymal stem cells (MSCs) and regulatory T cells (Tregs). CXCL14 stimulates the autocrine growth of cancer-associated fibroblasts (CAFs). On the other hand, the ligands of CXCR3, and CXCL14 and CXCL16, cause tumor infiltration by anticancer tumor-infiltrating lymphocytes (TILs) and thus show anticancer properties.

4.1. The Effect of Hypoxia on the Expressions of CXCL1 and CXCL2

17The effect of hypoxia on the expressions of CXCL1 and CXCL2 depends on the type of cancer. For example, chronic hypoxia does not affect the expression of either chemokine in lung adenocarcinoma but does increase the expression of CXCL1 in human acute myeloid leukemia cells, cervical cancer cells and hepatocarcinoma cells. The expressions of both CXCL1 and CXCL2 are increased by chronic hypoxia in PC-3 prostate cancer cells but reduced in SK-OV-3 ovarian adenocarcinoma and WM793B melanoma cells. In colitis-associated colon cancer, the source of CXCL1 in hypoxia may be tumor epithelial cells which, in a reaction mediated by HIF-2, increase the expression of this chemokine in the tumor microenvironment resulting in the recruitment of monocytes to the tumor niche.

18Cycling hypoxia increases the expression of both described chemokines (CXCL1 and CXCL2) in PC-3 prostate cancer cells and SK-OV-3 ovarian adenocarcinoma cells. In contrast, it reduces the expression of CXCL1 and CXCL2 in WM793B melanoma cells. However, in an in vivo model of Lewis lung carcinoma, cycling hypoxia increases the level of CXCL1 in a tumor.

19Another important source of CXCL1 and CXCL2 in the hypoxic microenvironment may be TAMs and MDSCs, as chronic hypoxia increases CXCL1 and CXCL2 expression in macrophages and MDSCs. The most important factor increasing the expression of CXCL2 in TAMs is HIF-2. HIF-1-dependent expression of both chemokines in MDSCs is also significant. This effect on the hypoxia-induced production of CXCL1 and CXCL2 in TAMs and MDSCs may be associated with the presence of HRE in the promoters of the CXCL1 and CXCL2 genes.

4.2. Effect of Hypoxia on the Expression of CXCL3

20The promoter of the CXCL3 gene does not contain HRE. For this reason, chronic hypoxia does not affect the expression of CXCL3 in lung adenocarcinoma cells and WM793B melanoma cells. Nevertheless, chronic hypoxia does increase the expression of CXCL3 in primary human monocytes, PC-3 prostate cancer cells and MDSCs. In MDSCs, this effect is dependent on HIF-1, although this mechanism requires further research. HIF-1 may indirectly affect the expression of CXCL3. It can increase the expression of a protein or miRNA which directly regulates the expression of this chemokine. In contrast, chronic hypoxia reduces the expression of CXCL3 in primary rat astrocytes and SK-OV-3 ovarian adenocarcinoma cells.

21Cycling hypoxia also influences the expression of CXCL3. Its effect also depends on the cell line, inducing a reduction in expression in WM793B melanoma cells and an increase in PC-3 prostate cancer cells. It may also have no effect at all, as in SK-OV-3 ovarian adenocarcinoma cells.

4.3. Effect of Hypoxia on CXCL5 Expression

22Chronic hypoxia does not increase the expression of CXCL5 in breast cancer cells, cervical squamous carcinoma cells, lung adenocarcinoma cells or MDSCs. In contrast, chronic hypoxia increases the expression of this chemokine in primary human monocytes. As well as this, the overexpression of HIF-2α in murine articular chondrocytes increases the expression of CXCL5 which is related to the presence of HRE in the CXCL5 gene promoter. The incompatibility of these results with those mentioned at the beginning of the paragraph may be due to differences between species. It is also possible that the expression of CXCL5 is dependent on HIF-2 but not on HIF-1. The indicated studies analyzed the changes in cells after 24 h of hypoxia—in such a long period of hypoxia, HIF-1 is activated, but HIF-2 is not. The maximum activation of HIF-2 only occurs after 48 h of chronic hypoxia.

4.4. Effect of Hypoxia on CXCL6 Expression

23Chronic hypoxia increases the expression of CXCL6 in hepatocellular carcinoma cells, which induces the migration of these cancer cells. Chronic hypoxia also increases the expression of CXCL6 in PC-3 prostate cancer cells. The induction of CXCL6 expression is HIF-1-dependent because the CXCL6 promoter contains HRE. However, chronic hypoxia does not always enhance the expression of CXCL6 as it can also reduce it in primary human monocytes and HeLa cervical cancer cells. Chronic hypoxia has no effect on the expression of this chemokine in breast cancer cells, the HepG2 hepatocarcinoma cell line and lung adenocarcinoma cells.

24In turn, cycling hypoxia increases the expression of CXCL6 in PC-3 prostate cancer cells.

4.5. Effect of Hypoxia on CXCL7 Expression

25Chronic hypoxia increases CXCL7 expression in cervical cancer cells and primary rat astrocytes. The overexpression of HIF-2α increases the expression of this chemokine in murine articular chondrocytes. In contrast, chronic hypoxia does not alter CXCL7 expression in HepG2 hepatocellular carcinoma cells and lung adenocarcinoma cells.

4.6. Effect of Hypoxia on CXCL8 Expression

26A tumor contains areas which are distant from blood vessels and characterized by chronic hypoxia, acidosis and cell necrosis. These areas show increased expression of CXCL8 as demonstrated by in vivo studies in human melanoma, human pancreatic cancer and ovarian carcinoma. The observed effect depends on hypoxia and the acidosis of this microenvironment. Chronic hypoxia does not alter CXCL8 expression in some cells, such as breast cancer cells, lung adenocarcinoma cells, primary hepatocytes and uveal melanoma cells.

27An increase in CXCL8 expression in melanoma cells, ovarian carcinoma, pancreatic cancer and rhabdomyosarcoma in chronic hypoxia is dependent on the activation of activating protein-1 (AP-1) and NF-κB—in particular, NF-κB p65, NF-κB p50 and c-Jun. The increase in CXCL8 expression in these tumor cells is independent of HIF-1 and nuclear factor-interleukin-6 (NF-IL-6).

28As with all the aforementioned chemokines, the mechanism of an increase in CXCL8 expression in chronic hypoxia depends on the type of tumor. In glioblastoma multiforme cells, an increase in CXCL8 expression in chronic hypoxia is AP-1-dependent but not NF-κB-dependent. In contrast, in some bladder cancer lines, it is associated with the activation of NF-κB but not AP-1. In turn, in hepatocellular carcinoma cells, an increase in the expression of CXCL8 in chronic hypoxia is dependent on the activation of HIF-1 and the effect of this transcription factor on NF-κB. In other types of cancer, the effect of HIF-1 may differ—for example, in colon cancer cells, chronic hypoxia increases the expression of CXCL8 via NF-κB. However, the activation of HIF-1 inhibits the effect of NF-κB on the expression of CXCL8.

29Hypoxia can also indirectly increase the expression of CXCL8 in glioblastoma multiforme cells by a HIF-1-dependent increase in the expression of ZNF395, a transcriptional factor that supports the increase in CXCL8 expression. In melanoma cells, chronic hypoxia degrades Tip110 by increasing the ubiquitination of this protein. The decrease in the level of Tip110 causes an increase in CXCL8 mRNA stability, which leads to an increase in CXCL8 expression. In colon cancer, chronic hypoxia intensifies the expression of dual specificity phosphatase 2 (DUSP2), a nuclear phosphatase which reduces the activation of MAPK cascades. The reduction in the expression of DUSP2 increases the activation of MAPK cascades in chronic hypoxia and thus elevates the expression of CXCL8. In turn, in lung adenocarcinoma cells, chronic hypoxia causes a change in the substrate specificity of dihydrodiol dehydrogenase which then starts to produce prostaglandin F2α (PGF2α), which increases the expression of CXCL8. However, it needs to be remembered that the mechanisms mentioned in this paragraph are not necessary for the induction of CXCL8 expression in tumor cells by chronic hypoxia and that they only enhance the influence of chronic hypoxia in terms of the expression of this chemokine.

30Cycling hypoxia also increases the expression of CXCL8, although its effect is dependent on the research model. In PC-3 prostate cancer cells, both types of hypoxia induce a similar increase in the expression of CXCL8. In SK-OV-3 ovarian adenocarcinoma cells, cycling hypoxia—unlike chronic hypoxia—increases the expression of CXCL8. In human aortic endothelial cells, cycling hypoxia increases the expression of CXCL8 more than chronic hypoxia. In neutrophils, cycling hypoxia increases the expression of CXCL8 and the receptor of this chemokine CXCR2, which reduces the spontaneous apoptosis of these cells. This may be significant in the recruitment and accumulation of TANs into the tumor niche. The effect of cycling hypoxia on CXCL8 expression is associated with increased ROS levels and greater NF-κB activation than in chronic hypoxia.

31TAMs may also be an important source of CXCL8 in the hypoxic microenvironment. However, there are no studies showing in vivo effects of hypoxia on CXCL8 expression in TAMs. The expression of this chemokine in TAMs may be increased by factors from tumor cells. Studies on monocyte-derived macrophages have shown that the expression of this chemokine in these cells may be increased by chronic hypoxia via AP-1 activation. HIF-1 and HIF-2 are no less important in this process, influencing the activation of NF-κB and thus increasing the expression of CXCL8. However, studies on (i) phorbol 12-myristate 13-acetate (PMA)–differentiated THP-1 macrophages and (ii) PMA–differentiated THP-1 macrophages, polarized by lipopolysaccharides (LPSs) and interferon-γ (IFN-γ), have shown that chronic hypoxia does not affect the expression of CXCL8 in these cells; however, cycling hypoxia increases the expression of this chemokine in these THP-1 macrophages, in a process dependent on the activation of c-Jun N-terminal kinase (JNK) MAPK and NF-κB.

32The expression of CXCL8 in endothelial cells is an important issue in cancer. VEGF secreted by cells in the tumor niche causes an increase in CXCL1 and CXCL8 expressions in endothelial cells, in a process important to angiogenesis and the migration of cancer cells. Chronic hypoxia changes the expression of CXCL8 in endothelial cells, although this effect is dependent on the research model. For example, an increase in CXCL8 expression has been observed in human umbilical vein endothelial cells (HUVECs), human pulmonary microvascular endothelial cells and human pulmonary aortic endothelial cells. This effect depends on the activation of the p38 MAPK and PI3K→PKB/Akt pathway, which in turn activates AP-1, HIF-1 and NF-κB. The activation of HIF-2 also plays a significant role in this process.

33In human microvascular endothelial HMEC-1 cells, hypoxia reduces CXCL8 expression (Figure 3) in a process mediated by HIF-1 and HIF-, which regulate the expression of CXCL8. HIF-1 increases the expression of Bach1, which in turn reduces the expression of erythroid 2-related factor (Nrf2). This reduces the expression of CXCL8. HIF-1 also decreases the expression of c-Myc. HIF-2 has the opposite effect as it increases the expression of c-Myc. HIF-2 also stabilizes the c-Myc:Max complex which increases c-Myc action, unlike HIF-1 which destabilizes the complex. As c-Myc increases the expression of CXCL8 by binding to the CXCL8 promoter, both HIFs can indirectly alter the expression of CXCL8, with a more pronounced influence of HIF-1.

34Cycling hypoxia alone does not increase the expression of CXCL8 and does not affect the activation of NF-κB, as shown in HUVECs. Nevertheless, this type of hypoxia does increase the response of these cells to proinflammatory factors such as tumor necrosis factor α (TNF-α). This results in a more intense activation of NF-κB and expression of CXCL8 and ICAM-1 in HUVECs than would occur as a result of TNF-α alone, which in turn increases the adhesion of these cells to the walls of blood vessels and thus their recruitment into the tumor niche.

4.7. Influence of Hypoxia on CXCR1 and CXCR2 Expression

35CXCR2 is a receptor of the CXCL1, CXCL2, CXCL3, CXCL5, CXCL6, CXCL7 and CXCL8 chemokines, and CXCR1 is receptor of CXCL6 and CXCL8. Changes in the expression of these receptors affect the action of these chemokines. Chronic hypoxia increases the expression of CXCR1 and CXCR2 in cervical carcinoma cells and prostate cancer cells. This effect is dependent on HIF-1 and NF-κB activation. Chronic hypoxia also increases the expression of CXCR2 on aortic endothelial cells. This may indicate the effect of hypoxia on angiogenesis by increasing the sensitivity of endothelial cells to CXCR2 ligands. However, this effect is dependent on the type of tumor—for example, chronic hypoxia reduces the expression of CXCR2 in gastric cancer cells.

36There are no data on the influence of cycling hypoxia on the expression of the described receptors on cancer cells. Screening studies did not show any influence on three cell lines: PC-3 (prostate cancer cells), SK-OV-3 (ovarian adenocarcinoma cells) and WM793B (melanoma cells). However, cycling hypoxia increases NF-κB-dependent expression of CXCR2 in neutrophil cells but decreases CXCR1 expression. Increasing the expression of CXCR2 increases the effect of CXCL1, CXCL2 and CXCL8 chemokines on these cells. In particular, there is a decrease in spontaneous apoptosis of these cells which supports TAN accumulation in the tumor niche.

5.1. The Influence of Hypoxia on CXCL4 Expression

37Chronic hypoxia increases the expression of CXCL4 in MUM2B uveal melanoma cells. This effect is mediated by HIF-1 and dependent on the type of tumor. For example, chronic hypoxia does not change the expression of CXCL4 in lung adenocarcinoma cells.

5.2. Effects of Hypoxia on CXCL9 Expression

38Chronic hypoxia does not affect the expression of CXCL9 in cervical cancer cells and lung adenocarcinoma cells. Nevertheless, chronic hypoxia increases the expression of this chemokine in primary rat brain astrocytes and hepatocarcinoma cells.

5.3. Effects of Hypoxia on the Expression of CXCL10

39The CXCL10 gene promoter contains one binding site for HIF and four binding sites for NF-κB. For this reason, the overexpression of HIF-2 increases the expression of CXCL10 in murine articular chondrocytes. Chronic hypoxia also increases the expression of CXCL10 in HepG2 cells (hepatocellular carcinoma). On the other hand, studies on cancer cells such as HeLa cells (cervical cancer), 9L glioma cells (brain tumor), breast cancer cells, ovarian cancer cells, colon cancer cells and lung cancer cells show that chronic hypoxia reduces the expression of CXCL10, as in studies on noncancer cells such as primary hepatocytes and rabbit alveolar macrophages. This effect may depend on HIF-1 or on the reduction in transcriptional NF-κB activity. However, in some types of cancer cells, such as acute myeloid leukaemia cells, chronic hypoxia does not change the expression of CXCL10.

40There are also four binding sites for NF-κB in the CXCL10 gene promoter. For this reason, by activating NF-κB and without the involvement of HIF, chronic hypoxia increases CXCL10 expression in cardiac microvascular endothelial cells. In the same way, cycling hypoxia increases the expression of CXCL10 in M1 polarized macrophages, although not in M2 macrophages.

5.4. Effect of Hypoxia on CXCL11 Expression

41The influence of chronic hypoxia on the expression of CXCL11 depends on the research model. In HeLa cervical cancer cells and primary human monocytes, chronic hypoxia reduces the expression of this chemokine. In cervical cancer, C33a cells increase. However, chronic hypoxia does not affect the expression of CXCL11 in hepatocarcinoma cells.

5.5. Effects of Hypoxia on CXCR3 Expression

42CoCl2 increases CXCR3 receptor expression in the model of renal cell carcinoma 786-O cells. CoCl2 is a substance that mimics the effects of hypoxia. For this reason, it can be assumed that chronic hypoxia increases the expression of CXCR3 on cancer cells.

6.1. Effect of Hypoxia on CXCL12 Expression

43Chronic hypoxia affects the expression of CXCL12. However, this effect depends on the adopted research model. In WM793B melanoma cells and GOT1 cells (ileal carcinoids), chronic hypoxia reduces CXCL12 expression. Chronic hypoxia also reduces the expression of CXCL12 in MDSCs, which is related to the HIF-1-dependent increase in the level of miRNA-210. Chronic hypoxia does not affect the expression of CXC12 in breast cancer cells, gastric cancer cells, lung adenocarcinoma cells, rhabdomyosarcoma cells and uveal melanoma cells. However, it does increase the expression of CXC12 in cervical cancer cells, clear cell-renal cell carcinomas cells, glioblastoma multiforme cells, multiple myeloma plasma cells, ovarian carcinomas cells and endothelial cells. This effect is dependent on HIF-1 and HIF-2. Transforming growth factor β (TGF-β) may also participate in the mechanism of increasing CXCL12 expression. On the other hand, in HUVECs, the increase in CXCL12 expression is dependent on NF-κB p65, which increases the expression of long intergenic nonprotein coding RNA 1693 (LINC01693), which functions as a miRNA-302d sponge. miRNA-302d reduces the expression of CXCL12—i.e., hypoxia increases the expression of this chemokine via NF-κB.

44Cycling hypoxia, akin to chronic hypoxia, reduces the expression of CXCL12 in WM793B melanoma cells.

6.2. Effect of Hypoxia on the Expression of CXCL12 Receptors: CXCR4 and CXCR7

45Chronic hypoxia increases the expression of CXCR4 in tumor cells such as breast cancer cells (Figure 4), chondrosarcoma cells, clear cell-renal cell carcinomas cells, chronic lymphocytic leukemia, colon cancer cells, gastric cancer cells, glioblastoma multiforme cells, GOT1 cells (ileal carcinoids), lung cancer cells, melanoma cells, multiple myeloma cells, oral squamous cell carcinoma cells, osteosarcoma cells, pancreatic ductal adenocarcinoma cells, renal cell carcinoma cells, and retinoblastoma cells. However, chronic hypoxia does not universally induce CXCR4 expression in tumor cells—for example, in hepatocellular carcinoma cells it only increases the expression of CXCR4 in some cell lines.

46The expression of CXCR7 under the influence of chronic hypoxia is upregulated in glioblastoma multiforme cells. However, its expression is not altered by chronic hypoxia in acute myeloid leukemia cells and breast cancer cells.

47Cycling hypoxia, unlike chronic hypoxia, does not affect CXCR4 expression in PC-3 prostate cancer cells and SK-OV-3 ovarian adenocarcinoma cells. However, cycling hypoxia increases CXCR7 expression in PC-3 prostate cancer cells, although this effect is not as intense as in chronic hypoxia. In contrast to chronic hypoxia, cycling hypoxia does not affect the expression of CXCR7 in SK-OV-3 ovarian adenocarcinoma cells.

48Expression of CXCR4 is increased directly by HIF-1 and HIF-2, because the promoter of the CXCR4 gene contains HRE. In particular, chronic hypoxia by HIF-2 increases the expression of CXCR4 in macrophages and endothelial progenitor cells. In breast cancer cells, chronic hypoxia increases CXCR4 expression independently of HIF-1, depending only on NF-κB. Chronic hypoxia increases the expression of CXCR4 in the pancreatic ductal adenocarcinoma cell line by reducing the level of miRNA-150. In chondrosarcoma, chronic hypoxia increases the expression of miRNA-181a, which controls the expression of the regulator of G-protein signaling 16 (RGS16). This protein reduces the expression of CXCR4. As such, miRNA-181a increases the expression of CXCR4. In breast cancer cells CoCl2 (chemical hypoxia-mimicking agent) reduces miRNA-302a expression. This miRNA regulates the expression of CXCR4—therefore, reducing the level of miRNA-302a increases the expression of CXCR4.

49Hypoxia may also alter the level of CXCR4 expression in leukemias. In multiple myeloma cells, chronic hypoxia increases CXCR4 expression in a process dependent on HIF-1. However, hypoxia can interfere with the action of CXCL12 on these cells by HIF-2-dependent upregulation of CC motif chemokine receptor 1 (CCR1). Activation of this receptor reduces the action of CXCL12 on multiple myeloma cells. In leukemic monocytic cells, mild and severe chronic hypoxias reduce the expression of CXCR4. This is related to a HIF-1- and HIF-2-dependent increase in the level of miRNA-146a, which reduces the expression of CXCR4 in these cells. Chronic hypoxia also causes a decreased migration of leukemic cells in response to CXCL12. This is related to the disturbance of Akt/PKB activation as shown by experiments on the HL-60 promyelocytic leukemia cell line. In acute myeloid leukemia, the dysfunction of CXCL12 by chronic hypoxia is dependent on cholesterol depletion, which interferes with the function of lipid rafts and thus the internalization of CXCR4. In contrast, in myeloma cell lines U266 and RPMI8226, chronic hypoxia increases the expression of CXCR4 by increasing the expression of miRNA-210.

6.3. Consequences of Hypoxia’s Influence on the CXCL12→CXCR4 Axis

50Hypoxia acts on the CXCL12→CXCR4 axis. However, the ramifications of this effect are too complex to be outlined in the section on tumor function of CXC chemokines. For this reason, consequences of the action of hypoxia on this axis are described in this part of the review.

51The CXCL12→CXCR4 pathway induced by chronic hypoxia has a significant procancer effect, especially due to the angiogenic influence of CXCL12. In a tumor cell, chronic hypoxia increases the expression of VEGF and in some types of tumor cells it increases the expression of CXCL12. CXCL12 causes an increase in VEGF expression on endothelial cells. VEGF increases expression of CXCR4 on HUVECs and human brain microvascular endothelial cells—sensitizing these cells to angiogenic CXCL12. Hypoxia also acts directly on endothelial cells by increasing the expression of VEGF and CXCR4; the latter is shown by studies on HUVECs and microvascular endothelial cells. To a lesser extent, chronic hypoxia also increases the expression of CXCR4 on microvascular endothelial cells and CXCL12 in HUVECs. Importantly, it should be remembered that chronic hypoxia does not only result in angiogenesis by inducing the expression of CXCL12 and VEGF, but via other factors as well.

52At the same time, a chronic hypoxia-induced increase in CXCR4 expression stimulates the proliferation of cancer cells and causes their migration and invasion, especially in combination with the chronic hypoxia-induced increase in CXCL12 expression in tumor cells. The upregulation of CXCR4 also aids in the transendothelial migration of cancer cells, which is followed by the invasion of cancer cells to neighboring tissues and organs. In breast cancer, the CXCL12→CXCR4 axis also participates in another stage of metastasis. After reaching the bone, breast cancer cells are retained close to osteoprogenitor cells in the hypoxic niche; the elevated expression of CXCL12 in the latter promotes the growth of breast cancer cells and thereby results in bone metastasis.

53In many types of cancer cells, chronic hypoxia does not increase the expression of CXCL12, although with an increased expression of CXCR4, the sensitivity of tumor cells to CXCL12 increases. In addition, cancer cell migration involving the CXCL12→CXCR4 axis may be caused by other cells—for example, CAFs in gastric cancer, where chronic hypoxia increases the expression of CXCL12 and thus acts on tumor cells with a hypoxia-enhanced expression of CXCR4.

54Chronic hypoxia also increases the expression of CXCR4 in monocytes and macrophages. For this reason, it can cause the accumulation of TAMs and MDSCs at sites with a high expression of CXCL12, particularly in tumors. A similar mechanism is postulated for the accumulation of Tregs in the hypoxic niche, and the recruitment of neural stem cells in glioblastoma multiforme and CD34+ endothelial progenitor cells in pituitary adenomas.

55Chronic hypoxia increases the expression of CXCR4 on multiple myelomas in a HIF-1-dependent manner. This leads to the migration of these cells and their homing to bone marrow via the CXCL12→CXCR4 pathway. Bones require physiological hypoxia for normal hematopoiesis, but are also involved in multiple myeloma. In this cancer, hypoxia increases the expression of angiogenic factors such as VEGF, CXCL8 and CXCL12. The upregulation of CXCL12 is induced by HIF-2 and to a lesser extent by HIF-1, resulting in angiogenesis and osteoclastic bone resorption. This, in turn, leads to angiogenesis and interference with the normal bone marrow microenvironment. Hypoxia in bone marrow can also cause the egress of multiple myeloma cells, as HIF-2 increases the expression of CCR1. Activation of this receptor by CC motif chemokine ligand 3 (CCL3) reduces the response of multiple myelomas to CXCL12 and the consequent egress of these cells from bone marrow.

56CXCR4 also has a function inside the tumor cell. Its activation by CXCL12 triggers its entry and internalization into the nucleus, where it interacts with HIF-1, enhancing the expression of genes dependent on this transcription factor.

7. Influence of Hypoxia on the CXCL13→CXCR5 Axis

57Chronic hypoxia does not alter CXCL13 expression in breast cancer cells, hepatocarcinoma cells and lung adenocarcinoma cells. Although the promoter of the CXCL13 gene contains HRE, no data are available on the direct chronic hypoxia-induced upregulation of CXCL13 in a tumor cell. It is only known that chronic hypoxia increases the expression of CXCL13 in adipocytes. On the other hand, chronic hypoxia may affect the expression of CXCL13 in the tumor indirectly—for example, via an increased expression of TGF-β in myofibroblasts in prostate tumors.

58There are no reports of hypoxia affecting the expression of CXCR5 (CXCL13 receptor) in cancer cells. Nevertheless, the promoter of the CXCR5 gene contains HRE. For this reason, chronic hypoxia increases the expression of CXCR5 as demonstrated in experiments on adipocytes.

8. Effect of Hypoxia on CXCL14 Expression

59Since the promoter of the CXCL14 gene contains HRE, chronic hypoxia can increase the expression of CXCL14, for example, in cervical cancer cells. The overexpression of HIF-2α in murine articular chondrocytes also increases the expression of CXCL14. Nevertheless, chronic hypoxia does not change the expression of the described chemokine in lung adenocarcinoma cells.

9. Effect of Hypoxia on CXCL15 Expression

60CXCL15 is a murine chemokine that is not found in humans and for this reason has been poorly researched. CXCL15 is mainly expressed in murine lungs, and to a much lesser extent in the murine digestive tract and urogenital organs. The expression of this chemokine can be increased by chronic hypoxia, as shown by experiments on murine articular chondrocytes, where the overexpression of HIF-2α resulted in an elevated expression of CXCL15.

10. Influence of Hypoxia on the CXCL16→CXCR6 Axis

61The effect of chronic hypoxia on the expression of CXCL16 depends on the type of cancer. In hepatocarcinoma cells and HUVECs, chronic hypoxia increases the expression of CXCL16. In HUVECs, this effect is dependent on HIF-1. In breast cancer cells, chronic hypoxia also increases the expression of CXCL16, although this is dependent on the CXCL10–CXCL16 loop. In contrast, chronic hypoxia does not alter CXCL16 expression in lung adenocarcinoma cells. Finally, it increases the expression of the CXCL16 receptor (CXCR6) in breast cancer cells in a HIF-1-dependent manner.

11. Influence of Hypoxia on the CXCL17→CXCR8 Axis

62There are no data available on the effect of hypoxia on the expression of CXCL17, or its receptor (CXCR8), in tumor cells. However, experiments on myocytes have shown that chronic hypoxia increases the expression of CXCR8 in a HIF-1-dependent process. This indicates that hypoxia increases the expression of this receptor on cancer cells and thus enhances the effect of CXCL17 on these cells.

63CXCL17 is a ligand of CXCR8, although there is currently a discussion on the existence of another, yet undiscovered, receptor. A potential discovery of a new receptor could reveal new methods of regulating the action of CXCL17, including the influence of hypoxia on the action of this chemokine.

12.1. Cancer Therapy Targeting Hypoxia

64Hypoxia and the signaling pathways activated by hypoxia are convenient therapeutic targets in cancer therapy (Figure 5). This is related to the fact that hypoxia occurs mainly in the tumor. For this reason, research focuses on inhibitors of the transcriptional activities of HIF-1 and HIF-2. On the other hand, oxygen concentration may be increased in the tumor and thus hypoxia may be prevented by using hyperbaric oxygen therapy. However, as hypoxia is also important in the functioning of hematopoietic stem cells under physiological conditions, any therapy against hypoxia may also cause side effects which affect the production of various blood cells.

65In another therapeutic approach, anticancer therapy targets certain proteins induced by hypoxia. A monoclonal anti-VEGF-A antibody known as bevacizumab is already used in therapy as an angiostatic factor. Inactivation of PD-L1 is also being studied as a way to increase the effectiveness of anticancer immunotherapy. However, targeting CXC chemokines remains a very important issue in cancer therapy, especially as hypoxia alters the expression of these chemoattractant cytokines, which promotes the growth of tumors.

12.2. Cancer Therapy Targeting CXC Chemokines

66Changes in the expression of CXC chemokines under the influence of hypoxia are an important element of cancer processes. For this reason, CXC chemokines and their receptors are a convenient therapeutic target in the treatment of cancer, with most clinical and preclinical studies focusing on CXCR2 and CXCR4 receptors and their ligands.

67The chemokines which act through CXCR1 and CXCR2 participate in numerous cancer processes, and therefore CXCR1/2 inhibitors as well as CXCR2 inhibitors, are considered as potential anticancer drugs. They reduce the proliferation and migration of cancer cells and inhibit angiogenesis, and their combination with current anticancer drugs has shown promising results. Anti-CXCL8 antibody, CXCL8 small interfering RNA, and anti-CXCL1 antibody have also been tested and such therapies have shown a reduction in tumor cell migration and angiogenesis. Another therapeutic approach involves the transduction of CXCR2 to antitumor lymphocytes which accumulate in the tumor niche and exhibit anticancer activity there.

68Drugs targeting the CXCL12→CXCR4 axis have also been investigated. Although the use of anti-CXCR4 antibodies are being tested in anticancer monotherapy, better results are obtained when drugs targeting this axis are combined with those already used in anticancer therapy. This approach involves CXCR4 antagonists, CXCR4 inhibitors, anti-CXCR4 antibodies and CXCR7 inhibitors. One of the advantages of these drugs is their ability to decrease drug resistance—e.g., to tamoxifen by CXCR4 antagonists in breast cancer. They also have the potential to increase the effectiveness of immunotherapy. An anti-CXCR4 antibody, or peptides recognizing CXCR4, have also been tested to target cytotoxic substances against cancer stem cells in acute myelogenous leukemia, breast cancer cells, colorectal cancer cells and multiple myeloma. This method can also be used to retarget an adenovirus vector against a tumor cell in gene therapy.

69Another direction of research is the use of gene therapy to increase the expression of chemokines that induce the infiltration of a tumor by anticancer TILs—for example, CXCR3 ligands such as CXCL10 and CXCL11. Promising results are also shown in the combination of current therapeutic methods, e.g., radiotherapy, with gene therapy which increases the expression of CXCL10. However, CXCL10 induces tamoxifen resistance in breast cancer and therefore any interference with the expression of the aforementioned chemokine during therapy should be performed after careful examination of its interaction with other anticancer drugs.

70Drugs that interfere with the action of other CXC chemokine receptors are also being tested, although these studies are not as advanced. An example of this is drugs which block the CXCL13→CXCR5 axis, with in vitro studies on breast cancer cells showing that anti-CXCL13 antibodies induce tumor cell apoptosis. However, to date, no advanced animal model studies or clinical trials have been conducted in this area.

71Another promising chemokine is CXCL16, which causes tumor infiltration by anticancer TILs. The expression and release of this chemokine in a tumor cell is increased by ionizing radiation, and so combining radiotherapy (increasing the expression of chemokines that result in the recruitment of anticancer lymphocytes) with immunotherapy (which consists of introducing modified anticancer lymphocytes into the patient’s body) has been postulated.

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Not in our library10.1016/j.bbrc.2017.08.169
63.
Ke X., Chen C., Song Y., Cai Q., Li J., Tang Y., Han X., Qu W., Chen A., Wang H., et al. Hypoxia modifies the polarization of macrophages and their inflammatory microenvironment, and inhibits malignant behavior in cancer cells. Oncol. Lett. 2019;18:5871-5878.
Not in our library10.3892/ol.2019.10956
64.
Balsamo M., Manzini C., Pietra G., Raggi F., Blengio F., Mingari M.C., Varesio L., Moretta L., Bosco M.C., Vitale M. Hypoxia downregulates the expression of activating receptors involved in NK-cell-mediated target cell killing without affecting ADCC. Eur. J. Immunol. 2013;43:2756-2764.
Not in our library10.1002/eji.201343448
65.
Chen C.H., Li S.X., Xiang L.X., Mu H.Q., Wang S.B., Yu K.Y. HIF-1α induces immune escape of prostate cancer by regulating NCR1/NKp46 signaling through miR-224. Biochem. Biophys. Res. Commun. 2018;503:228-234.
Not in our library10.1016/j.bbrc.2018.06.007
66.
Hypoxia-Driven Immunosuppressive Metabolites in the Tumor Microenvironment: New Approaches for Combinational Immunotherapy · 2018
No notice
67.
Song X., Zhang Y., Zhang L., Song W., Shi L. Hypoxia enhances indoleamine 2,3-dioxygenase production in dendritic cells. Oncotarget. 2018;9:11572-11580.
Not in our library10.18632/oncotarget.24098
68.
Lactate in the Tumor Microenvironment: An Essential Molecule in Cancer Progression and Treatment · 2020
No notice
69.
Miller F., Kentsis A., Osman R., Pan Z.Q. Inactivation of VHL by tumorigenic mutations that disrupt dynamic coupling of the pVHL.hypoxia-inducible transcription factor-1alpha complex. J. Biol. Chem. 2005;280:7985-7996.
Not in our library10.1074/jbc.m413160200
70.
Gossage L., Eisen T. Alterations in VHL as potential biomarkers in renal-cell carcinoma. Nat. Rev. Clin. Oncol. 2010;7:277-288.
Not in our library10.1038/nrclinonc.2010.42
71.
Wang E., Zhang C., Polavaram N., Liu F., Wu G., Schroeder M.A., Lau J.S., Mukhopadhyay D., Jiang S.W., O’Neill B.P., et al. The role of factor inhibiting HIF (FIH-1) in inhibiting HIF-1 transcriptional activity in glioblastoma multiforme. PLoS ONE. 2014;9:e86102.
Not in our library10.1371/journal.pone.0086102
72.
Bullen J.W., Tchernyshyov I., Holewinski R.J., DeVine L., Wu F., Venkatraman V., Kass D.L., Cole R.N., Van Eyk J., Semenza G.L. Protein kinase A-dependent phosphorylation stimulates the transcriptional activity of hypoxia-inducible factor 1. Sci. Signal. 2016;9:ra56.
Not in our library10.1126/scisignal.aaf0583
73.
Stiehl D.P., Jelkmann W., Wenger R.H., Hellwig-Bürgel T. Normoxic induction of the hypoxia-inducible factor 1alpha by insulin and interleukin-1beta involves the phosphatidylinositol 3-kinase pathway. FEBS Lett. 2002;512:157-162.
Not in our library10.1016/s0014-5793(02)02247-0
74.
Treins C., Giorgetti-Peraldi S., Murdaca J., Semenza G.L., Van Obberghen E. Insulin stimulates hypoxia-inducible factor 1 through a phosphatidylinositol 3-kinase/target of rapamycin-dependent signaling pathway. J. Biol. Chem. 2002;277:27975-27981.
Not in our library10.1074/jbc.m204152200
75.
Frede S., Stockmann C., Freitag P., Fandrey J. Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-kappaB. Biochem. J. 2006;396:517-527.
Not in our library10.1042/bj20051839
76.
Mylonis I., Chachami G., Samiotaki M., Panayotou G., Paraskeva E., Kalousi A., Georgatsou E., Bonanou S., Simos G. Identification of MAPK phosphorylation sites and their role in the localization and activity of hypoxia-inducible factor-1alpha. J. Biol. Chem. 2006;281:33095-33106.
Not in our library10.1074/jbc.m605058200
77.
Koyasu S., Kobayashi M., Goto Y., Hiraoka M., Harada H. Regulatory mechanisms of hypoxia-inducible factor 1 activity: Two decades of knowledge. Cancer Sci. 2018;109:560-571.
Not in our library10.1111/cas.13483
78.
Lim J.H., Lee Y.M., Chun Y.S., Chen J., Kim J.E., Park J.W. Sirtuin 1 modulates cellular responses to hypoxia by deacetylating hypoxia-inducible factor 1alpha. Mol. Cell. 2010;38:864-878.
Not in our library10.1016/j.molcel.2010.05.023
79.
Zlotnik A., Yoshie O. Chemokines: A new classification system and their role in immunity. Immunity. 2000;12:121-127.
Not in our library10.1016/s1074-7613(00)80165-x
80.
Schmitz J.M., McCracken V.J., Dimmitt R.A., Lorenz R.G. Expression of CXCL15 (Lungkine) in murine gastrointestinal, urogenital, and endocrine organs. J. HistoChem. Cytochem. 2007;55:515-524.
Not in our library10.1369/jhc.6a7121.2007
81.
Wuyts A., Proost P., Lenaerts J.P., Ben-Baruch A., Van Damme J., Wang J.M. Differential usage of the CXC chemokine receptors 1 and 2 by interleukin-8, granulocyte chemotactic protein-2 and epithelial-cell-derived neutrophil attractant-78. Eur. J. Biochem. 1998;255:67-73.
Not in our library10.1046/j.1432-1327.1998.2550067.x
82.
Jenh C.H., Cox M.A., Hipkin W., Lu T., Pugliese-Sivo C., Gonsiorek W., Chou C.C., Narula S.K., Zavodny P.J. Human B cell-attracting chemokine 1 (BCA-1; CXCL13) is an agonist for the human CXCR3 receptor. Cytokine. 2001;15:113-121.
Not in our library10.1006/cyto.2001.0923
83.
Burns J.M., Summers B.C., Wang Y., Melikian A., Berahovich R., Miao Z., Penfold M.E., Sunshine M.J., Littman D.R., Kuo C.J., et al. A novel chemokine receptor for SDF-1 and I-TAC involved in cell survival, cell adhesion, and tumor development. J. Exp. Med. 2006;203:2201-2213.
Not in our library10.1084/jem.20052144
84.
Hattermann K., Bartsch K., Gebhardt H.H., Mehdorn H.M., Synowitz M., Schmitt A.D., Mentlein R., Held-Feindt J. “Inverse signaling” of the transmembrane chemokine CXCL16 contributes to proliferative and anti-apoptotic effects in cultured human meningioma cells. Cell Commun. Signal. 2016;14:26.
Not in our library10.1186/s12964-016-0149-7
85.
Tanegashima K., Suzuki K., Nakayama Y., Tsuji K., Shigenaga A., Otaka A., Hara T. CXCL14 is a natural inhibitor of the CXCL12-CXCR4 signaling axis. FEBS Lett. 2013;587:1731-1735.
Not in our library10.1016/j.febslet.2013.04.046
86.
Otte M., Kliewer A., Schütz D., Reimann C., Schulz S., Stumm R. CXCL14 is no direct modulator of CXCR4. FEBS Lett. 2014;588:4769-4775.
Not in our library10.1016/j.febslet.2014.11.009
87.
Wang Y., Weng X., Wang L., Hao M., Li Y., Hou L., Liang Y., Wu T., Yao M., Lin G., et al. HIC1 deletion promotes breast cancer progression by activating tumor cell/fibroblast crosstalk. J. Clin. Investig. 2018;128:5235-5250.
Not in our library10.1172/jci99974
88.
Tanegashima K., Takahashi R., Nuriya H., Iwase R., Naruse N., Tsuji K., Shigenaga A., Otaka A., Hara T. CXCL14 Acts as a Specific Carrier of CpG DNA into Dendritic Cells and Activates Toll-like Receptor 9-mediated Adaptive Immunity. EBioMedicine. 2017;24:247-256.
Not in our library10.1016/j.ebiom.2017.09.012
89.
Cheng C.L., Yang S.C., Lai C.Y., Wang C.K., Chang C.F., Lin C.Y., Chen W.J., Lin P.Y., Wu H.C., Ma N., et al. CXCL14 Maintains hESC Self-Renewal through Binding to IGF-1R and Activation of the IGF-1R Pathway. Cells. 2020;9:1706.
Not in our library10.3390/cells9071706
90.
Strieter R.M., Polverini P.J., Kunkel S.L., Arenberg D.A., Burdick M.D., Kasper J., Dzuiba J., Van Damme J., Walz A., Marriott D., et al. The functional role of the ELR motif in CXC chemokine-mediated angiogenesis. J. Biol. Chem. 1995;270:27348-27357.
Not in our library10.1074/jbc.270.45.27348
91.
Salcedo R., Resau J.H., Halverson D., Hudson E.A., Dambach M., Powell D., Wasserman K., Oppenheim J.J. Differential expression and responsiveness of chemokine receptors (CXCR1-3) by human microvascular endothelial cells and umbilical vein endothelial cells. FASEB J. 2000;14:2055-2064.
Not in our library10.1096/fj.99-0963com
92.
Heidemann J., Ogawa H., Dwinell M.B., Rafiee P., Maaser C., Gockel H.R., Otterson M.F., Ota D.M., Lugering N., Domschke W., et al. Angiogenic effects of interleukin 8 (CXCL8) in human intestinal microvascular endothelial cells are mediated by CXCR2. J. Biol. Chem. 2003;278:8508-8515.
Not in our library10.1074/jbc.m208231200
93.
Nör J.E., Christensen J., Liu J., Peters M., Mooney D.J., Strieter R.M., Polverini P.J. Up-Regulation of Bcl-2 in microvascular endothelial cells enhances intratumoral angiogenesis and accelerates tumor growth. Cancer Res. 2001;61:2183-2188.
Not in our library
94.
Warner K.A., Miyazawa M., Cordeiro M.M., Love W.J., Pinsky M.S., Neiva K.G., Spalding A.C., Nör J.E. Endothelial cells enhance tumor cell invasion through a crosstalk mediated by CXC chemokine signaling. Neoplasia. 2008;10:131-139.
Not in our library10.1593/neo.07815
95.
Romagnani P., Annunziato F., Lasagni L., Lazzeri E., Beltrame C., Francalanci M., Uguccioni M., Galli G., Cosmi L., Maurenzig L., et al. Cell cycle-dependent expression of CXC chemokine receptor 3 by endothelial cells mediates angiostatic activity. J. Clin. Investig. 2001;107:53-63.
Not in our library10.1172/jci9775
96.
Parsonage G., Machado L.R., Hui J.W., McLarnon A., Schmaler T., Balasothy M., To K.F., Vlantis A.C., van Hasselt C.A., Lo K.W., et al. CXCR6 and CCR5 localize T lymphocyte subsets in nasopharyngeal carcinoma. Am. J. Pathol. 2012;180:1215-1222.
Not in our library10.1016/j.ajpath.2011.11.032
97.
Yang J., Richmond A. The angiostatic activity of interferon-inducible protein-10/CXCL10 in human melanoma depends on binding to CXCR3 but not to glycosaminoglycan. Mol. Ther. 2004;9:846-855.
Not in our library10.1016/j.ymthe.2004.01.010
98.
Van Raemdonck K., Gouwy M., Lepers S.A., Van Damme J., Struyf S. CXCL4L1 and CXCL4 signaling in human lymphatic and microvascular endothelial cells and activated lymphocytes: Involvement of mitogen-activated protein (MAP) kinases, Src and p70S6 kinase. Angiogenesis. 2014;17:631-640.
Not in our library10.1007/s10456-014-9417-6
99.
Mirshahi F., Pourtau J., Li H., Muraine M., Trochon V., Legrand E., Vannier J., Soria J., Vasse M., Soria C. SDF-1 activity on microvascular endothelial cells: Consequences on angiogenesis in in vitro and in vivo models. Thromb. Res. 2000;99:587-594.
Not in our library10.1016/s0049-3848(00)00292-9
100.
Salcedo R., Wasserman K., Young H.A., Grimm M.C., Howard O.M., Anver M.R., Kleinman H.K., Murphy W.J., Oppenheim J.J. Vascular endothelial growth factor and basic fibroblast growth factor induce expression of CXCR4 on human endothelial cells: In vivo neovascularization induced by stromal-derived factor-1alpha. Am. J. Pathol. 1999;154:1125-1135.
Not in our library10.1016/s0002-9440(10)65365-5
101.
Neuhaus T., Stier S., Totzke G., Gruenewald E., Fronhoffs S., Sachinidis A., Vetter H., Ko Y.D. Stromal cell-derived factor 1alpha (SDF-1alpha) induces gene-expression of early growth response-1 (Egr-1) and VEGF in human arterial endothelial cells and enhances VEGF induced cell proliferation. Cell Prolif. 2003;36:75-86.
Not in our library10.1046/j.1365-2184.2003.00262.x
102.
Li M., Lu Y., Xu Y., Wang J., Zhang C., Du Y., Wang L., Li L., Wang B., Shen J., et al. Horizontal transfer of exosomal CXCR4 promotes murine hepatocarcinoma cell migration, invasion and lymphangiogenesis. Gene. 2018;676:101-109.
Not in our library10.1016/j.gene.2018.07.018
103.
Spinetti G., Camarda G., Bernardini G., Romano Di Peppe S., Capogrossi M.C., Napolitano M. The chemokine CXCL13 (BCA-1) inhibits FGF-2 effects on endothelial cells. Biochem. Biophys. Res. Commun. 2001;289:19-24.
Not in our library10.1006/bbrc.2001.5924
104.
Shellenberger T.D., Wang M., Gujrati M., Jayakumar A., Strieter R.M., Burdick M.D., Ioannides C.G., Efferson C.L., El-Naggar A.K., Roberts D., et al. BRAK/CXCL14 is a potent inhibitor of angiogenesis and a chemotactic factor for immature dendritic cells. Cancer Res. 2004;64:8262-8270.
Not in our library10.1158/0008-5472.can-04-2056
105.
Liu Y., Chang Q., Wu X., Yu Y., Zhang H. Effect of chemokine CXCL14 on in vitro angiogenesis of human hepatocellular carcinoma cells. Arch. Physiol. Biochem. 2020.
Not in our library10.1080/13813455.2020.1769677
106.
Yu X., Zhao R., Lin S., Bai X., Zhang L., Yuan S., Sun L. CXCL16 induces angiogenesis in autocrine signaling pathway involving hypoxia-inducible factor 1α in human umbilical vein endothelial cells. Oncol. Rep. 2016;35:1557-1565.
Not in our library10.3892/or.2015.4520
107.
Lee W.Y., Wang C.J., Lin T.Y., Hsiao C.L., Luo C.W. CXCL17, an orphan chemokine, acts as a novel angiogenic and anti-inflammatory factor. Am. J. Physiol. Endocrinol. Metab. 2013;304:E32-E40.
Not in our library10.1152/ajpendo.00083.2012
108.
Fan L., Zhu Q., Liu L., Zhu C., Huang H., Lu S., Liu P. CXCL13 is androgen-responsive and involved in androgen induced prostate cancer cell migration and invasion. Oncotarget. 2017;8:53244-53261.
Not in our library10.18632/oncotarget.18387
109.
Guo Y.J., Zhou Y.J., Yang X.L., Shao Z.M., Ou Z.L. The role and clinical significance of the CXCL17-CXCR8 (GPR35) axis in breast cancer. Biochem. Biophys. Res. Commun. 2017;493:1159-1167.
Not in our library10.1016/j.bbrc.2017.09.113
110.
Hong L., Wang S., Li W., Wu D., Chen W. Tumor-associated macrophages promote the metastasis of ovarian carcinoma cells by enhancing CXCL16/CXCR6 expression. Pathol. Res. Pract. 2018;214:1345-1351.
Not in our library10.1016/j.prp.2018.07.009
111.
Li Y., Reader J.C., Ma X., Kundu N., Kochel T., Fulton A.M. Divergent roles of CXCR3 isoforms in promoting cancer stem-like cell survival and metastasis. Breast Cancer Res. Treat. 2015;149:403-415.
Not in our library10.1007/s10549-014-3229-7
112.
Reynders N., Abboud D., Baragli A., Noman M.Z., Rogister B., Niclou S.P., Heveker N., Janji B., Hanson J., Szpakowska M., et al. The Distinct Roles of CXCR3 Variants and Their Ligands in the Tumor Microenvironment. Cells. 2019;8:613.
Not in our library10.3390/cells8060613
113.
Lin K., Zou R., Lin F., Zheng S., Shen X., Xue X. Expression and effect of CXCL14 in colorectal carcinoma. Mol. Med. Rep. 2014;10:1561-1568.
Not in our library10.3892/mmr.2014.2343
114.
Li X., Zhao L., Meng T. Upregulated CXCL14 is associated with poor survival outcomes and promotes ovarian cancer cells proliferation. Cell Biochem. Funct. 2020;38:613-620.
Not in our library10.1002/cbf.3516
115.
Moser B., Schumacher C., von Tscharner V., Clark-Lewis I., Baggiolini M. Neutrophil-activating peptide 2 and gro/melanoma growth-stimulatory activity interact with neutrophil-activating peptide 1/interleukin 8 receptors on human neutrophils. J. Biol. Chem. 1991;266:10666-10671.
Not in our library10.1016/s0021-9258(18)99275-6
116.
Haqqani A.S., Sandhu J.K., Birnboim H.C. Expression of interleukin-8 promotes neutrophil infiltration and genetic instability in mutatect tumors. Neoplasia. 2000;2:561-568.
Not in our library10.1038/sj.neo.7900110
117.
Jablonska J., Wu C.F., Andzinski L., Leschner S., Weiss S. CXCR2-mediated tumor-associated neutrophil recruitment is regulated by IFN-β. Int. J. Cancer. 2014;134:1346-1358.
Not in our library10.1002/ijc.28551
118.
Gijsbers K., Gouwy M., Struyf S., Wuyts A., Proost P., Opdenakker G., Penninckx F., Ectors N., Geboes K., Van Damme J. GCP-2/CXCL6 synergizes with other endothelial cell-derived chemokines in neutrophil mobilization and is associated with angiogenesis in gastrointestinal tumors. Exp. Cell Res. 2005;303:331-342.
Not in our library10.1016/j.yexcr.2004.09.027
119.
Chao T., Furth E.E., Vonderheide R.H. CXCR2-Dependent Accumulation of Tumor-Associated Neutrophils Regulates T-cell Immunity in Pancreatic Ductal Adenocarcinoma. Cancer Immunol. Res. 2016;4:968-982.
Not in our library10.1158/2326-6066.cir-16-0188
120.
Ligocki A.J., Niederkorn J.Y. Natural Killer T Cells Contribute to Neutrophil Recruitment and Ocular Tissue Damage in a Model of Intraocular Tumor Rejection. Investig. Ophthalmol. Vis. Sci. 2016;57:813-823.
Not in our library10.1167/iovs.15-18786
121.
Yuan M., Zhu H., Xu J., Zheng Y., Cao X., Liu Q. Tumor-Derived CXCL1 Promotes Lung Cancer Growth via Recruitment of Tumor-Associated Neutrophils. J. Immunol. Res. 2016;2016:6530410.
Not in our library10.1155/2016/6530410
122.
Tulotta C., Stefanescu C., Chen Q., Torraca V., Meijer A.H., Snaar-Jagalska B.E. CXCR4 signaling regulates metastatic onset by controlling neutrophil motility and response to malignant cells. Sci. Rep. 2019;9:2399.
Not in our library10.1038/s41598-019-38643-2
123.
Wang S.C., Hong J.H., Hsueh C., Chiang C.S. Tumor-secreted SDF-1 promotes glioma invasiveness and TAM tropism toward hypoxia in a murine astrocytoma model. Lab. Investig. 2012;92:151-162.
Not in our library10.1038/labinvest.2011.128
124.
Oka T., Sugaya M., Takahashi N., Takahashi T., Shibata S., Miyagaki T., Asano Y., Sato S. CXCL17 Attenuates Imiquimod-Induced Psoriasis-like Skin Inflammation by Recruiting Myeloid-Derived Suppressor Cells and Regulatory T Cells. J. Immunol. 2017;198:3897-3908.
Not in our library10.4049/jimmunol.1601607
125.
Shi H., Han X., Sun Y., Shang C., Wei M., Ba X., Zeng X. Chemokine (C-X-C motif) ligand 1 and CXCL2 produced by tumor promote the generation of monocytic myeloid-derived suppressor cells. Cancer Sci. 2018;109:3826-3839.
Not in our library10.1111/cas.13809
126.
Snail promotes ovarian cancer progression by recruiting myeloid-derived suppressor cells via CXCR2 ligand upregulation · 2018
No notice
127.
Li B.H., Garstka M.A., Li Z.F. Chemokines and their receptors promoting the recruitment of myeloid-derived suppressor cells into the tumor. Mol. Immunol. 2020;117:201-215.
Not in our library10.1016/j.molimm.2019.11.014
128.
Takahashi R., Amano H., Ito Y., Eshima K., Satoh T., Iwamura M., Nakamura M., Kitasato H., Uematsu S., Raouf J., et al. Microsomal prostaglandin E synthase-1 promotes lung metastasis via SDF-1/CXCR4-mediated recruitment of CD11b+Gr1+MDSCs from bone marrow. Biomed. Pharmacother. 2020;121:109581.
Not in our library10.1016/j.biopha.2019.109581
129.
Unver N., Esendagli G., Yilmaz G., Guc D. CXCL7-induced macrophage infiltration in lung tumor is independent of CXCR2 expression: CXCL7-induced macrophage chemotaxis in LLC tumors. Cytokine. 2015;75:330-337.
Not in our library10.1016/j.cyto.2015.07.018
130.
Krawczyk K.M., Nilsson H., Allaoui R., Lindgren D., Arvidsson M., Leandersson K., Johansson M.E. Papillary renal cell carcinoma-derived chemerin, IL-8, and CXCL16 promote monocyte recruitment and differentiation into foam-cell macrophages. Lab. Investig. 2017;97:1296-1305.
Not in our library10.1038/labinvest.2017.78
131.
Cancer-associated fibroblasts enhance tumor-associated macrophages enrichment and suppress NK cells function in colorectal cancer · 2019
No notice
132.
Xu F., Shi J., Yu B., Ni W., Wu X., Gu Z. Chemokines mediate mesenchymal stem cell migration toward gliomas in vitro. Oncol. Rep. 2010;23:1561-1567.
Not in our library10.3892/or_00000796
133.
Jung Y., Kim J.K., Shiozawa Y., Wang J., Mishra A., Joseph J., Berry J.E., McGee S., Lee E., Sun H., et al. Recruitment of mesenchymal stem cells into prostate tumours promotes metastasis. Nat. Commun. 2013;4:1795.
Not in our library10.1038/ncomms2766
134.
Kasashima H., Yashiro M., Nakamae H., Kitayama K., Masuda G., Kinoshita H., Fukuoka T., Hasegawa T., Nakane T., Hino M., et al. CXCL1-Chemokine (C-X-C Motif) Receptor 2 Signaling Stimulates the Recruitment of Bone Marrow-Derived Mesenchymal Cells into Diffuse-Type Gastric Cancer Stroma. Am. J. Pathol. 2016;186:3028-3039.
Not in our library10.1016/j.ajpath.2016.07.024
135.
Zheng X.B., He X.W., Zhang L.J., Qin H.B., Lin X.T., Liu X.H., Zhou C., Liu H.S., Hu T., Cheng H.C., et al. Bone marrow-derived CXCR4-overexpressing MSCs display increased homing to intestine and ameliorate colitis-associated tumorigenesis in mice. Gastroenterol. Rep. 2019;7:127-138.
Not in our library10.1093/gastro/goy017
136.
Meng L., Zhao Y., Bu W., Li X., Liu X., Zhou D., Chen Y., Zheng S., Lin Q., Liu Q., et al. Bone mesenchymal stem cells are recruited via CXCL8-CXCR2 and promote EMT through TGF-β signal pathways in oral squamous carcinoma. Cell Prolif. 2020;53:e12859.
Not in our library10.1111/cpr.12859
137.
Recruitment of regulatory T cells is correlated with hypoxia-induced CXCR4 expression, and is associated with poor prognosis in basal-like breast cancers · 2011
No notice
138.
Yang S., Wang B., Guan C., Wu B., Cai C., Wang M., Zhang B., Liu T., Yang P. Foxp3+IL-17+ T cells promote development of cancer-initiating cells in colorectal cancer. J. Leukoc. Biol. 2011;89:85-91.
Not in our library10.1189/jlb.0910506
139.
Redjimi N., Raffin C., Raimbaud I., Pignon P., Matsuzaki J., Odunsi K., Valmori D., Ayyoub M. CXCR3+ T regulatory cells selectively accumulate in human ovarian carcinomas to limit type I immunity. Cancer Res. 2012;72:4351-4360.
Not in our library10.1158/0008-5472.can-12-0579
140.
Ye J., Ma C., Wang F., Hsueh E.C., Toth K., Huang Y., Mo W., Liu S., Han B., Varvares M.A., et al. Specific recruitment of γδ regulatory T cells in human breast cancer. Cancer Res. 2013;73:6137-6148.
Not in our library10.1158/0008-5472.can-13-0348
141.
Lv M., Xu Y., Tang R., Ren J., Shen S., Chen Y., Liu B., Hou Y., Wang T. miR141-CXCL1-CXCR2 signaling-induced Treg recruitment regulates metastases and survival of non-small cell lung cancer. Mol. Cancer Ther. 2014;13:3152-3162.
Not in our library10.1158/1535-7163.mct-14-0448
142.
Li C.X., Ling C.C., Shao Y., Xu A., Li X.C., Ng K.T., Liu X.B., Ma Y.Y., Qi X., Liu H., et al. CXCL10/CXCR3 signaling mobilized-regulatory T cells promote liver tumor recurrence after transplantation. J. Hepatol. 2016;65:944-952.
Not in our library10.1016/j.jhep.2016.05.032
143.
Chen X., Takemoto Y., Deng H., Middelhoff M., Friedman R.A., Chu T.H., Churchill M.J., Ma Y., Nagar K.K., Tailor Y.H., et al. Histidine decarboxylase (HDC)-expressing granulocytic myeloid cells induce and recruit Foxp3+ regulatory T cells in murine colon cancer. Oncoimmunology. 2017;6:e1290034.
Not in our library10.1080/2162402x.2017.1290034
144.
Santagata S., Napolitano M., D’Alterio C., Desicato S., Maro S.D., Marinelli L., Fragale A., Buoncervello M., Persico F., Gabriele L., et al. Targeting CXCR4 reverts the suppressive activity of T-regulatory cells in renal cancer. Oncotarget. 2017;8:77110-77120.
Not in our library10.18632/oncotarget.20363
145.
Deng S., Deng Q., Zhang Y., Ye H., Yu X., Zhang Y., Han G.Y., Luo P., Wu M., Yu Y., et al. Non-platelet-derived CXCL4 differentially regulates cytotoxic and regulatory T cells through CXCR3 to suppress the immune response to colon cancer. Cancer Lett. 2019;443:1-12.
Not in our library10.1016/j.canlet.2018.11.017
146.
Wang R., Feng W., Wang H., Wang L., Yang X., Yang F., Zhang Y., Liu X., Zhang D., Ren Q., et al. Blocking migration of regulatory T cells to leukemic hematopoietic microenvironment delays disease progression in mouse leukemia model. Cancer Lett. 2020;469:151-161.
Not in our library10.1016/j.canlet.2019.10.032
147.
Augsten M., Hägglöf C., Olsson E., Stolz C., Tsagozis P., Levchenko T., Frederick M.J., Borg A., Micke P., Egevad L., et al. CXCL14 is an autocrine growth factor for fibroblasts and acts as a multi-modal stimulator of prostate tumor growth. Proc. Natl. Acad. Sci. USA. 2009;106:3414-3419.
Not in our library10.1073/pnas.0813144106
148.
Starnes T., Rasila K.K., Robertson M.J., Brahmi Z., Dahl R., Christopherson K., Hromas R. The chemokine CXCL14 (BRAK) stimulates activated NK cell migration: Implications for the downregulation of CXCL14 in malignancy. Exp. Hematol. 2006;34:1101-1105.
Not in our library10.1016/j.exphem.2006.05.015
149.
Mueller A., Meiser A., McDonagh E.M., Fox J.M., Petit S.J., Xanthou G., Williams T.J., Pease J.E. CXCL4-induced migration of activated T lymphocytes is mediated by the chemokine receptor CXCR3. J. Leukoc. Biol. 2008;83:875-882.
Not in our library10.1189/jlb.1006645
150.
Kee J.Y., Ito A., Hojo S., Hashimoto I., Igarashi Y., Tsukada K., Irimura T., Shibahara N., Nakayama T., Yoshie O., et al. Chemokine CXCL16 suppresses liver metastasis of colorectal cancer via augmentation of tumor-infiltrating natural killer T cells in a murine model. Oncol. Rep. 2013;29:975-982.
Not in our library10.3892/or.2012.2185
151.
Tan K.W., Evrard M., Tham M., Hong M., Huang C., Kato M., Prevost-Blondel A., Donnadieu E., Ng L.G., Abastado J.P. Tumor stroma and chemokines control T-cell migration into melanoma following Temozolomide treatment. Oncoimmunology. 2015;4:e978709.
Not in our library10.4161/2162402x.2014.978709
152.
Cicchini L., Westrich J.A., Xu T., Vermeer D.W., Berger J.N., Clambey E.T., Lee D., Song J.I., Lambert P.F., Greer R.O., et al. Suppression of Antitumor Immune Responses by Human Papillomavirus through Epigenetic Downregulation of CXCL14. mBio. 2016;7:e00270-16.
Not in our library10.1128/mbio.00270-16
153.
Mossanen J.C., Kohlhepp M., Wehr A., Krenkel O., Liepelt A., Roeth A.A., Möckel D., Heymann F., Lammers T., Gassler N., et al. CXCR6 Inhibits Hepatocarcinogenesis by Promoting Natural Killer T- and CD4+ T-Cell-Dependent Control of Senescence. Gastroenterology. 2019;156:1877-1889.e4.
Not in our library10.1053/j.gastro.2019.01.247
154.
Huang G., Tao L., Shen S., Chen L. Hypoxia induced CCL28 promotes angiogenesis in lung adenocarcinoma by targeting CCR3 on endothelial cells. Sci. Rep. 2016;6:27152.
Not in our library10.1038/srep27152
155.
Hatfield K.J., Bedringsaas S.L., Ryningen A., Gjertsen B.T., Bruserud O. Hypoxia increases HIF-1α expression and constitutive cytokine release by primary human acute myeloid leukaemia cells. Eur. Cytokine Netw. 2010;21:154-164.
Not in our library10.1684/ecn.2010.0204
156.
Differential expression of cytokines and receptor expression during anoxic growth · 2018
Not checked
157.
Ye L.Y., Chen W., Bai X.L., Xu X.Y., Zhang Q., Xia X.F., Sun X., Li G.G., Hu Q.D., Fu Q.H., et al. Hypoxia-Induced Epithelial-to-Mesenchymal Transition in Hepatocellular Carcinoma Induces an Immunosuppressive Tumor Microenvironment to Promote Metastasis. Cancer Res. 2016;76:818-830.
Not in our library10.1158/0008-5472.can-15-0977
158.
Triner D., Xue X., Schwartz A.J., Jung I., Colacino J.A., Shah Y.M. Epithelial Hypoxia-Inducible Factor 2α Facilitates the Progression of Colon Tumors through Recruiting Neutrophils. Mol. Cell Biol. 2017;37:e00481-16.
Not in our library10.1128/mcb.00481-16
159.
Fang H.Y., Hughes R., Murdoch C., Coffelt S.B., Biswas S.K., Harris A.L., Johnson R.S., Imityaz H.Z., Simon M.C., Fredlund E., et al. Hypoxia-inducible factors 1 and 2 are important transcriptional effectors in primary macrophages experiencing hypoxia. Blood. 2009;114:844-859.
Not in our library10.1182/blood-2008-12-195941
160.
Wang J., Yu F., Jia X., Iwanowycz S., Wang Y., Huang S., Ai W., Fan D. MicroRNA-155 deficiency enhances the recruitment and functions of myeloid-derived suppressor cells in tumor microenvironment and promotes solid tumor growth. Int. J. Cancer. 2015;136:E602-E613.
Not in our library10.1002/ijc.29151
161.
Imtiyaz H.Z., Williams E.P., Hickey M.M., Patel S.A., Durham A.C., Yuan L.J., Hammond R., Gimotty P.A., Keith B., Simon M.C. Hypoxia-inducible factor 2alpha regulates macrophage function in mouse models of acute and tumor inflammation. J. Clin. Investig. 2010;120:2699-2714.
Not in our library10.1172/jci39506
162.
Blengio F., Raggi F., Pierobon D., Cappello P., Eva A., Giovarelli M., Varesio L., Bosco M.C. The hypoxic environment reprograms the cytokine/chemokine expression profile of human mature dendritic cells. Immunobiology. 2013;218:76-89.
Not in our library10.1016/j.imbio.2012.02.002
163.
Huh Y.H., Lee G., Lee K.B., Koh J.T., Chun J.S., Ryu J.H. HIF-2α-induced chemokines stimulate motility of fibroblast-like synoviocytes and chondrocytes into the cartilage-pannus interface in experimental rheumatoid arthritis mouse models. Arthritis Res. Ther. 2015;17:302.
Not in our library10.1186/s13075-015-0816-x
164.
Bosco M.C., Puppo M., Santangelo C., Anfosso L., Pfeffer U., Fardin P., Battaglia F., Varesio L. Hypoxia modifies the transcriptome of primary human monocytes: Modulation of novel immune-related genes and identification of CC-chemokine ligand 20 as a new hypoxia-inducible gene. J. Immunol. 2006;177:1941-1955.
Not in our library10.4049/jimmunol.177.3.1941
165.
Samy Z.A., Al-Abdullah L., Turcani M., Craik J., Redzic Z. Rat astrocytes during anoxia: Secretome profile of cytokines and chemokines. Brain Behav. 2018;8:e01013.
Not in our library10.1002/brb3.1013
166.
Macrophages are recruited to hypoxic tumor areas and acquire a Pro-Angiogenic M2-Polarized phenotype via hypoxic cancer cell derived cytokines Oncostatin M and Eotaxin · 2014
No notice
167.
Hypoxia-induced ZEB1 promotes cervical cancer progression via CCL8-dependent tumour-associated macrophage recruitment · 2019
Corrected
168.
Tian H., Huang P., Zhao Z., Tang W., Xia J. HIF-1α plays a role in the chemotactic migration of hepatocarcinoma cells through the modulation of CXCL6 expression. Cell Physiol. Biochem. 2014;34:1536-1546.
Not in our library10.1159/000366357
169.
Xie F., Liu L.B., Shang W.Q., Chang K.K., Meng Y.H., Mei J., Yu J.J., Li D.J., Li M.Q. The infiltration and functional regulation of eosinophils induced by TSLP promote the proliferation of cervical cancer cell. Cancer Lett. 2015;364:106-117.
Not in our library10.1016/j.canlet.2015.04.029
170.
Rofstad E.K., Halsør E.F. Hypoxia-associated spontaneous pulmonary metastasis in human melanoma xenografts: Involvement of microvascular hot spots induced in hypoxic foci by interleukin 8. Br. J. Cancer. 2002;86:301-308.
Not in our library10.1038/sj.bjc.6600052
171.
Rofstad E.K., Mathiesen B., Henriksen K., Kindem K., Galappathi K. The tumor bed effect: Increased metastatic dissemination from hypoxia-induced up-regulation of metastasis-promoting gene products. Cancer Res. 2005;65:2387-2396.
Not in our library10.1158/0008-5472.can-04-3039
172.
Shi Q., Abbruzzese J.L., Huang S., Fidler I.J., Xiong Q., Xie K. Constitutive and inducible interleukin 8 expression by hypoxia and acidosis renders human pancreatic cancer cells more tumorigenic and metastatic. Clin. Cancer Res. 1999;5:3711-3721.
Not in our library
173.
Xu L., Xie K., Mukaida N., Matsushima K., Fidler I.J. Hypoxia-induced elevation in interleukin-8 expression by human ovarian carcinoma cells. Cancer Res. 1999;59:5822-5829.
Not in our library
174.
Desbaillets I., Diserens A.C., Tribolet N., Hamou M.F., Van Meir E.G. Upregulation of interleukin 8 by oxygen-deprived cells in glioblastoma suggests a role in leukocyte activation, chemotaxis, and angiogenesis. J. Exp. Med. 1997;186:1201-1212.
Not in our library10.1084/jem.186.8.1201
175.
Heinzman J.M., Brower S.L., Bush J.E. Comparison of angiogenesis-related factor expression in primary tumor cultures under normal and hypoxic growth conditions. Cancer Cell Int. 2008;8:11.
Not in our library10.1186/1475-2867-8-11
176.
Shi Q., Le X., Wang B., Xiong Q., Abbruzzese J.L., Xie K. Regulation of interleukin-8 expression by cellular pH in human pancreatic adenocarcinoma cells. J. Interferon. Cytokine Res. 2000;20:1023-1028.
Not in our library10.1089/10799900050198471
177.
Voss M.J., Möller M.F., Powe D.G., Niggemann B., Zänker K.S., Entschladen F. Luminal and basal-like breast cancer cells show increased migration induced by hypoxia, mediated by an autocrine mechanism. BMC Cancer. 2011;11:158.
Not in our library10.1186/1471-2407-11-158
178.
Vodovotz Y., Simmons R.L., Barclay D., Yin J., Jefferson B.S., Zamora R. Decoding the secreted inflammatory response of primary human hepatocytes to hypoxic stress in vitro. Ann. Transl. Med. 2019;7:371.
Not in our library10.21037/atm.2019.07.09
179.
Bronkhorst I.H., Jehs T.M., Dijkgraaf E.M., Luyten G.P., van der Velden P.A., van der Burg S.H., Jager M.J. Effect of hypoxic stress on migration and characteristics of monocytes in uveal melanoma. JAMA Ophthalmol. 2014;132:614-621.
Not in our library10.1001/jamaophthalmol.2014.43
180.
Kunz M., Hartmann A., Flory E., Toksoy A., Koczan D., Thiesen H.J., Mukaida N., Neumann M., Rapp U.R., Bröcker E.B., et al. Anoxia-induced up-regulation of interleukin-8 in human malignant melanoma. A potential mechanism for high tumor aggressiveness. Am. J. Pathol. 1999;155:753-763.
Not in our library10.1016/s0002-9440(10)65174-7
181.
Xu L., Pathak P.S., Fukumura D. Hypoxia-induced activation of p38 mitogen-activated protein kinase and phosphatidylinositol 3′-kinase signaling pathways contributes to expression of interleukin 8 in human ovarian carcinoma cells. Clin. Cancer Res. 2004;10:701-707.
Not in our library10.1158/1078-0432.ccr-0953-03
182.
Shi Q., Le X., Abbruzzese J.L., Wang B., Mujaida N., Matsushima K., Huang S., Xiong Q., Xie K. Cooperation between transcription factor AP-1 and NF-kappaB in the induction of interleukin-8 in human pancreatic adenocarcinoma cells by hypoxia. J. Interferon. Cytokine Res. 1999;19:1363-1371.
Not in our library10.1089/107999099312821
183.
Wysoczynski M., Shin D.M., Kucia M., Ratajczak M.Z. Selective upregulation of interleukin-8 by human rhabdomyosarcomas in response to hypoxia: Therapeutic implications. Int. J. Cancer. 2010;126:371-381.
Not in our library10.1002/ijc.24732
184.
Desbaillets I., Diserens A.C., de Tribolet N., Hamou M.F., Van Meir E.G. Regulation of interleukin-8 expression by reduced oxygen pressure in human glioblastoma. Oncogene. 1999;18:1447-1456.
Not in our library10.1038/sj.onc.1202424
185.
Karashima T., Sweeney P., Kamat A., Huang S., Kim S.J., Bar-Eli M., McConkey D.J., Dinney C.P. Nuclear factor-kappaB mediates angiogenesis and metastasis of human bladder cancer through the regulation of interleukin-8. Clin. Cancer Res. 2003;9:2786-2797.
Not in our library
186.
Fei M., Guan J., Xue T., Qin L., Tang C., Cui G., Wang Y., Gong H., Feng W. Hypoxia promotes the migration and invasion of human hepatocarcinoma cells through the HIF-1α-IL-8-Akt axis. Cell Mol. Biol. Lett. 2018;23:46.
Not in our library10.1186/s11658-018-0100-6
187.
HIF-1α promotes the migration and invasion of hepatocellular carcinoma cells via the IL-8–NF-κB axis · 2018
Not checked
188.
Mizukami Y., Jo W.S., Duerr E.M., Gala M., Li J., Zhang X., Zimmer M.A., Iliopoulos O., Zukerberg L.R., Kohgo Y., et al. Induction of interleukin-8 preserves the angiogenic response in HIF-1alpha-deficient colon cancer cells. Nat. Med. 2005;11:992-997.
Not in our library10.1038/nm1294
189.
Herwartz C., Castillo-Juárez P., Schröder L., Barron B.L., Steger G. The Transcription Factor ZNF395 Is Required for the Maximal Hypoxic Induction of Proinflammatory Cytokines in U87-MG Cells. Mediat. Inflamm. 2015;2015:804264.
Not in our library10.1155/2015/804264
190.
Timani K.A., Liu Y., Fan Y., Mohammad K.S., He J.J. Tip110 Regulates the Cross Talk between p53 and Hypoxia-Inducible Factor 1α under Hypoxia and Promotes Survival of Cancer Cells. Mol. Cell Biol. 2015;35:2254-2264.
Not in our library10.1128/mcb.00001-15
191.
Timani K.A., Győrffy B., Liu Y., Mohammad K.S., He J.J. Tip110/SART3 regulates IL-8 expression and predicts the clinical outcomes in melanoma. Mol. Cancer. 2018;17:124.
Not in our library10.1186/s12943-018-0868-z
192.
Hsiao K.Y., Chang N., Lin S.C., Li Y.H., Wu M.H. Inhibition of dual specificity phosphatase-2 by hypoxia promotes interleukin-8-mediated angiogenesis in endometriosis. Hum. Reprod. 2014;29:2747-2755.
Not in our library10.1093/humrep/deu255
193.
Lin S.C., Hsiao K.Y., Chang N., Hou P.C., Tsai S.J. Loss of dual-specificity phosphatase-2 promotes angiogenesis and metastasis via up-regulation of interleukin-8 in colon cancer. J. Pathol. 2017;241:638-648.
Not in our library10.1002/path.4868
194.
Chiang Y.Y. Hepatocyte growth factor induces hypoxia-related interleukin-8 expression in lung adenocarcinoma cells. Mol. Carcinog. 2009;48:662-670.
Not in our library10.1002/mc.20521
195.
Polotsky V.Y., Savransky V., Bevans-Fonti S., Reinke C., Li J., Grigoryev D.N., Shimoda L.A. Intermittent and sustained hypoxia induce a similar gene expression profile in human aortic endothelial cells. Physiol. Genom. 2010;41:306-314.
Not in our library10.1152/physiolgenomics.00091.2009
196.
Glynn P.C., Henney E., Hall I.P. The selective CXCR2 antagonist SB272844 blocks interleukin-8 and growth-related oncogene-alpha-mediated inhibition of spontaneous neutrophil apoptosis. Pulm. Pharmacol. Ther. 2002;15:103-110.
Not in our library10.1006/pupt.2001.0323
197.
Dyugovskaya L., Polyakov A., Ginsberg D., Lavie P., Lavie L. Molecular pathways of spontaneous and TNF-{alpha}-mediated neutrophil apoptosis under intermittent hypoxia. Am. J. Respir. Cell Mol. Biol. 2011;45:154-162.
Not in our library10.1165/rcmb.2010-0025oc
198.
Galindo M., Santiago B., Alcami J., Rivero M., Martín-Serrano J., Pablos J.L. Hypoxia induces expression of the chemokines monocyte chemoattractant protein-1 (MCP-1) and IL-8 in human dermal fibroblasts. Clin. Exp. Immunol. 2001;123:36-41.
Not in our library10.1046/j.1365-2249.2001.01412.x
199.
Higashihara H., Kokura S., Imamoto E., Ueda M., Naito Y., Yoshida N., Yoshikawa T. Hypoxia-reoxygenation enhances interleukin-8 production from U937 human monocytic cells. Redox Rep. 2004;9:365-369.
Not in our library10.1179/135100004225006894
200.
Chen J.J., Yao P.L., Yuan A., Hong T.M., Shun C.T., Kuo M.L., Lee Y.C., Yang P.C. Up-regulation of tumor interleukin-8 expression by infiltrating macrophages: Its correlation with tumor angiogenesis and patient survival in non-small cell lung cancer. Clin. Cancer Res. 2003;9:729-737.
Not in our library
201.
Hirani N., Antonicelli F., Strieter R.M., Wiesener M.S., Ratcliffe P.J., Haslett C., Donnelly S.C. The regulation of interleukin-8 by hypoxia in human macrophages—a potential role in the pathogenesis of the acute respiratory distress syndrome (ARDS). Mol. Med. 2001;7:685-697.
Not in our library10.1007/bf03401959
202.
Delprat V., Tellier C., Demazy C., Raes M., Feron O., Michiels C. Cycling hypoxia promotes a pro-inflammatory phenotype in macrophages via JNK/p65 signaling pathway. Sci. Rep. 2020;10:882.
Not in our library10.1038/s41598-020-57677-5
203.
Karakurum M., Shreeniwas R., Chen J., Pinsky D., Yan S.D., Anderson M., Sunouchi K., Major J., Hamilton T., Kuwabara K., et al. Hypoxic induction of interleukin-8 gene expression in human endothelial cells. J. Clin. Investig. 1994;93:1564-1570.
Not in our library10.1172/jci117135
204.
Kim K.S., Rajagopal V., Gonsalves C., Johnson C., Kalra V.K. A novel role of hypoxia-inducible factor in cobalt chloride- and hypoxia-mediated expression of IL-8 chemokine in human endothelial cells. J. Immunol. 2006;177:7211-7224.
Not in our library10.4049/jimmunol.177.10.7211
205.
Endler A., Chen L., Li Q., Uchida K., Hashimoto T., Lu L., Xu G.T., Shibasaki F. Int6/eIF3e silenced HIF2α stabilization enhances migration and tube formation of HUVECs via IL-6 and IL-8 signaling. Cytokine. 2013;62:115-122.
Not in our library10.1016/j.cyto.2013.01.021
206.
Loboda A., Jazwa A., Jozkowicz A., Molema G., Dulak J. Angiogenic transcriptome of human microvascular endothelial cells: Effect of hypoxia, modulation by atorvastatin. Vascul. Pharmacol. 2006;44:206-214.
Not in our library10.1016/j.vph.2005.11.007
207.
Loboda A., Stachurska A., Florczyk U., Rudnicka D., Jazwa A., Wegrzyn J., Kozakowska M., Stalinska K., Poellinger L., Levonen A.L., et al. HIF-1 induction attenuates Nrf2-dependent IL-8 expression in human endothelial cells. Antioxid. Redox Signal. 2009;11:1501-1517.
Not in our library10.1089/ars.2008.2211
208.
Florczyk U., Czauderna S., Stachurska A., Tertil M., Nowak W., Kozakowska M., Poellinger L., Jozkowicz A., Loboda A., Dulak J. Opposite effects of HIF-1α and HIF-2α on the regulation of IL-8 expression in endothelial cells. Free Radic. Biol. Med. 2011;51:1882-1892.
Not in our library10.1016/j.freeradbiomed.2011.08.023
209.
Liu L.B., Xie F., Chang K.K., Li M.Q., Meng Y.H., Wang X.H., Li H., Li D.J., Yu J.J. Hypoxia promotes the proliferation of cervical carcinoma cells through stimulating the secretion of IL-8. Int. J. Clin. Exp. Pathol. 2014;7:575-583.
Not in our library
210.
Maxwell P.J., Gallagher R., Seaton A., Wilson C., Scullin P., Pettigrew J., Stratford I.J., Williams K.J., Johnston P.G., Waugh D.J. HIF-1 and NF-kappaB-mediated upregulation of CXCR1 and CXCR2 expression promotes cell survival in hypoxic prostate cancer cells. Oncogene. 2007;26:7333-7345.
Not in our library10.1038/sj.onc.1210536
211.
Moldobaeva A., Wagner E.M. Difference in proangiogenic potential of systemic and pulmonary endothelium: Role of CXCR2. Am. J. Physiol. Lung Cell Mol. Physiol. 2005;288:L1117-L1123.
Not in our library10.1152/ajplung.00370.2004
212.
Kinoshita H., Yashiro M., Fukuoka T., Hasegawa T., Morisaki T., Kasashima H., Masuda G., Noda S., Hirakawa K. Diffuse-type gastric cancer cells switch their driver pathways from FGFR2 signaling to SDF1/CXCR4 axis in hypoxic tumor microenvironments. Carcinogenesis. 2015;36:1511-1520.
Not in our library10.1093/carcin/bgv134
213.
Grutkoski P.S., Graeber C.T., D’Amico R., Keeping H., Simms H.H. Regulation of IL-8RA (CXCR1) expression in polymorphonuclear leukocytes by hypoxia/reoxygenation. J. Leukoc. Biol. 1999;65:171-178.
Not in our library10.1002/jlb.65.2.171
214.
Victor N., Ivy A., Jiang B.H., Agani F.H. Involvement of HIF-1 in invasion of Mum2B uveal melanoma cells. Clin. Exp. Metastasis. 2006;23:87-96.
Not in our library10.1007/s10585-006-9024-z
215.
Xia J.B., Liu G.H., Chen Z.Y., Mao C.Z., Zhou D.C., Wu H.Y., Park K.S., Zhao H., Kim S.K., Cai D.Q., et al. Hypoxia/ischemia promotes CXCL10 expression in cardiac microvascular endothelial cells by NFkB activation. Cytokine. 2016;81:63-70.
Not in our library10.1016/j.cyto.2016.02.007
216.
Konishi H., Shirabe K., Nakagawara H., Harimoto N., Yamashita Y., Ikegami T., Yoshizumi T., Soejima Y., Oda Y., Maehara Y. Suppression of silent information regulator 1 activity in noncancerous tissues of hepatocellular carcinoma: Possible association with non-B non-C hepatitis pathogenesis. Cancer Sci. 2015;106:542-549.
Not in our library10.1111/cas.12653
217.
Marotta D., Karar J., Jenkins W.T., Kumanova M., Jenkins K.W., Tobias J.W., Baldwin D., Hatzigeorgiou A., Alexiou P., Evans S.M., et al. In vivo profiling of hypoxic gene expression in gliomas using the hypoxia marker EF5 and laser-capture microdissection. Cancer Res. 2011;71:779-789.
Not in our library10.1158/0008-5472.can-10-3061
218.
Ullah K., Rosendahl A.H., Izzi V., Bergmann U., Pihlajaniemi T., Mäki J.M., Myllyharju J. Hypoxia-inducible factor prolyl-4-hydroxylase-1 is a convergent point in the reciprocal negative regulation of NF-κB and p53 signaling pathways. Sci. Rep. 2017;7:17220.
Not in our library10.1038/s41598-017-17376-0
219.
Utsumi T., Suyama T., Imamura Y., Fuse M., Sakamoto S., Nihei N., Ueda T., Suzuki H., Seki N., Ichikawa T. The association of CXCR3 and renal cell carcinoma metastasis. J. Urol. 2014;192:567-574.
Not in our library10.1016/j.juro.2014.01.100
220.
Muñoz-Sánchez J., Chánez-Cárdenas M.E. The use of cobalt chloride as a chemical hypoxia model. J. Appl. Toxicol. 2019;39:556-570.
Not in our library10.1002/jat.3749
221.
Arvidsson Y., Bergström A., Arvidsson L., Kristiansson E., Ahlman H., Nilsson O. Hypoxia stimulates CXCR4 signalling in ileal carcinoids. Endocr. Relat. Cancer. 2010;17:303-316.
Not in our library10.1677/erc-09-0085
222.
Noman M.Z., Janji B., Hu S., Wu J.C., Martelli F., Bronte V., Chouaib S. Tumor-Promoting Effects of Myeloid-Derived Suppressor Cells Are Potentiated by Hypoxia-Induced Expression of miR-210. Cancer Res. 2015;75:3771-3787.
Not in our library10.1158/0008-5472.can-15-0405
223.
Zagzag D., Krishnamachary B., Yee H., Okuyama H., Chiriboga L., Ali M.A., Melamed J., Semenza G.L. Stromal cell-derived factor-1alpha and CXCR4 expression in hemangioblastoma and clear cell-renal cell carcinoma: Von Hippel-Lindau loss-of-function induces expression of a ligand and its receptor. Cancer Res. 2005;65:6178-6188.
Not in our library10.1158/0008-5472.can-04-4406
224.
Tabatabai G., Frank B., Möhle R., Weller M., Wick W. Irradiation and hypoxia promote homing of haematopoietic progenitor cells towards gliomas by TGF-beta-dependent HIF-1alpha-mediated induction of CXCL12. Brain. 2006;129:2426-2435.
Not in our library10.1093/brain/awl173
225.
Zhao D., Najbauer J., Garcia E., Metz M.Z., Gutova M., Glackin C.A., Kim S.U., Aboody K.S. Neural stem cell tropism to glioma: Critical role of tumor hypoxia. Mol. Cancer Res. 2008;6:1819-1829.
Not in our library10.1158/1541-7786.mcr-08-0146
226.
Komatani H., Sugita Y., Arakawa F., Ohshima K., Shigemori M. Expression of CXCL12 on pseudopalisading cells and proliferating microvessels in glioblastomas: An accelerated growth factor in glioblastomas. Int. J. Oncol. 2009;34:665-672.
Not in our library10.3892/ijo_00000192
227.
Martin S.K., Diamond P., Williams S.A., To L.B., Peet D.J., Fujii N., Gronthos S., Harris A.L., Zannettino A.C. Hypoxia-inducible factor-2 is a novel regulator of aberrant CXCL12 expression in multiple myeloma plasma cells. Haematologica. 2010;95:776-784.
Not in our library10.3324/haematol.2009.015628
228.
Kryczek I., Lange A., Mottram P., Alvarez X., Cheng P., Hogan M., Moons L., Wei S., Zou L., Machelon V., et al. CXCL12 and vascular endothelial growth factor synergistically induce neoangiogenesis in human ovarian cancers. Cancer Res. 2005;65:465-472.
Not in our library
229.
Jin F., Brockmeier U., Otterbach F., Metzen E. New insight into the SDF-1/CXCR4 axis in a breast carcinoma model: Hypoxia-induced endothelial SDF-1 and tumor cell CXCR4 are required for tumor cell intravasation. Mol. Cancer Res. 2012;10:1021-1031.
Not in our library10.1158/1541-7786.mcr-11-0498
230.
Sun Y., Xiong X., Wang X. RELA promotes hypoxia-induced angiogenesis in human umbilical vascular endothelial cells via LINC01693/miR-302d/CXCL12 axis. J. Cell Biochem. 2019;120:12549-12558.
Not in our library10.1002/jcb.28521
231.
Ceradini D.J., Kulkarni A.R., Callaghan M.J., Tepper O.M., Bastidas N., Kleinman M.E., Capla J.M., Galiano R.D., Levine J.P., Gurtner G.C. Progenitor cell trafficking is regulated by hypoxic gradients through HIF-1 induction of SDF-1. Nat. Med. 2004;10:858-864.
Not in our library10.1038/nm1075
232.
Strickland J., Garrison D., Copple B.L. Hypoxia upregulates Cxcl12 in hepatocytes by a complex mechanism involving hypoxia-inducible factors and transforming growth factor-β. Cytokine. 2020;127:154986.
Not in our library10.1016/j.cyto.2020.154986
233.
Matteucci E., Locati M., Desiderio M.A. Hepatocyte growth factor enhances CXCR4 expression favoring breast cancer cell invasiveness. Exp. Cell Res. 2005;310:176-185.
Not in our library10.1016/j.yexcr.2005.07.008
234.
Seo Y.J., Koh S.H., Kang H.J., Shin H.Y., Jeong G., Ahn H.S. Hypoxia inhibits the SDF-1-dependent migration of human leukemic cell line HL-60 via blocking of Akt activation. Biochem. Biophys. Res. Commun. 2007;364:388-394.
Not in our library10.1016/j.bbrc.2007.10.023
235.
Hypoxia increases the metastatic ability of breast cancer cells via upregulation of CXCR4 · 2010
Not checked
236.
Tafani M., Russo A., Di Vito M., Sale P., Pellegrini L., Schito L., Gentileschi S., Bracaglia R., Marandino F., Garaci E., et al. Up-regulation of pro-inflammatory genes as adaptation to hypoxia in MCF-7 cells and in human mammary invasive carcinoma microenvironment. Cancer Sci. 2010;101:1014-1023.
Not in our library10.1111/j.1349-7006.2010.01493.x
237.
Jamaludin S.Y.N., Azimi I., Davis F.M., Peters A.A., Gonda T.J., Thompson E.W., Roberts-Thomson S.J., Monteith G.R. Assessment of CXC ligand 12-mediated calcium signalling and its regulators in basal-like breast cancer cells. Oncol. Lett. 2018;15:4289-4295.
Not in our library10.3892/ol.2018.7827
238.
Zhang M., Gao C.E., Chen W.L., Tang Y.Y., Nie J.Y., Shen L.D., Ma X., Chen D.D. Opposite response to hypoxia by breast cancer cells between cell proliferation and cell migration: A clue from microRNA expression profile. Oncol. Lett. 2018;15:2771-2780.
Not in our library10.3892/ol.2017.7636
239.
Sun X., Wei L., Chen Q., Terek R.M. CXCR4/SDF1 mediate hypoxia induced chondrosarcoma cell invasion through ERK signaling and increased MMP1 expression. Mol. Cancer. 2010;9:17.
Not in our library10.1186/1476-4598-9-17
240.
Sun X., Charbonneau C., Wei L., Chen Q., Terek R.M. miR-181a Targets RGS16 to Promote Chondrosarcoma Growth, Angiogenesis, and Metastasis. Mol. Cancer Res. 2015;13:1347-1357.
Not in our library10.1158/1541-7786.mcr-14-0697
241.
Valsecchi R., Coltella N., Belloni D., Ponente M., Ten Hacken E., Scielzo C., Scarfò L., Bertilaccio M.T., Brambilla P., Lenti E., et al. HIF-1α regulates the interaction of chronic lymphocytic leukemia cells with the tumor microenvironment. Blood. 2016;127:1987-1997.
Not in our library10.1182/blood-2015-07-657056
242.
Hongo K., Tsuno N.H., Kawai K., Sasaki K., Kaneko M., Hiyoshi M., Murono K., Tada N., Nirei T., Sunami E., et al. Hypoxia enhances colon cancer migration and invasion through promotion of epithelial-mesenchymal transition. J. Surg. Res. 2013;182:75-84.
Not in our library10.1016/j.jss.2012.08.034
243.
Romain B., Hachet-Haas M., Rohr S., Brigand C., Galzi J.L., Gaub M.P., Pencreach E., Guenot D. Hypoxia differentially regulated CXCR4 and CXCR7 signaling in colon cancer. Mol. Cancer. 2014;13:58.
Not in our library10.1186/1476-4598-13-58
244.
Oh Y.S., Kim H.Y., Song I.C., Yun H.J., Jo D.Y., Kim S., Lee H.J. Hypoxia induces CXCR4 expression and biological activity in gastric cancer cells through activation of hypoxia-inducible factor-1α. Oncol. Rep. 2012;28:2239-2246.
Not in our library10.3892/or.2012.2063
245.
Zagzag D., Lukyanov Y., Lan L., Ali M.A., Esencay M., Mendez O., Yee H., Voura E.B., Newcomb E.W. Hypoxia-inducible factor 1 and VEGF upregulate CXCR4 in glioblastoma: Implications for angiogenesis and glioma cell invasion. Lab. Investig. 2006;86:1221-1232.
Not in our library10.1038/labinvest.3700482
246.
Zagzag D., Esencay M., Mendez O., Yee H., Smirnova I., Huang Y., Chiriboga L., Lukyanov E., Liu M., Newcomb E.W. Hypoxia- and vascular endothelial growth factor-induced stromal cell-derived factor-1alpha/CXCR4 expression in glioblastomas: One plausible explanation of Scherer’s structures. Am. J. Pathol. 2008;173:545-560.
Not in our library10.2353/ajpath.2008.071197
247.
Hiroi M., Mori K., Sakaeda Y., Shimada J., Ohmori Y. STAT1 represses hypoxia-inducible factor-1-mediated transcription. Biochem. Biophys. Res. Commun. 2009;387:806-810.
Not in our library10.1016/j.bbrc.2009.07.138
248.
Liu Y.L., Yu J.M., Song X.R., Wang X.W., Xing L.G., Gao B.B. Regulation of the chemokine receptor CXCR4 and metastasis by hypoxia-inducible factor in non small cell lung cancer cell lines. Cancer Biol. Ther. 2006;5:1320-1326.
Not in our library10.4161/cbt.5.10.3162
249.
Kang N., Choi S.Y., Kim B.N., Yeo C.D., Park C.K., Kim Y.K., Kim T.J., Lee S.B., Lee S.H., Park J.Y., et al. Hypoxia-induced cancer stemness acquisition is associated with CXCR4 activation by its aberrant promoter demethylation. BMC Cancer. 2019;19:148.
Not in our library10.1186/s12885-019-5360-7
250.
Schutyser E., Su Y., Yu Y., Gouwy M., Zaja-Milatovic S., Van Damme J., Richmond A. Hypoxia enhances CXCR4 expression in human microvascular endothelial cells and human melanoma cells. Eur. Cytokine Netw. 2007;18:59-70.
Not in our library10.1684/ecn.2007.0087
251.
Dong L., You S., Zhang Q., Osuka S., Devi N.S., Kaluz S., Ferguson J.H., Yang H., Chen G., Wang B., et al. Arylsulfonamide 64B Inhibits Hypoxia/HIF-Induced Expression of c-Met and CXCR4 and Reduces Primary Tumor Growth and Metastasis of Uveal Melanoma. Clin. Cancer Res. 2019;25:2206-2218.
Not in our library10.1158/1078-0432.ccr-18-1368
252.
Azab A.K., Hu J., Quang P., Azab F., Pitsillides C., Awwad R., Thompson B., Maiso P., Sun J.D., Hart C.P., et al. Hypoxia promotes dissemination of multiple myeloma through acquisition of epithelial to mesenchymal transition-like features. Blood. 2012;119:5782-5794.
Not in our library10.1182/blood-2011-09-380410
253.
Ishikawa T., Nakashiro K., Klosek S.K., Goda H., Hara S., Uchida D., Hamakawa H. Hypoxia enhances CXCR4 expression by activating HIF-1 in oral squamous cell carcinoma. Oncol. Rep. 2009;21:707-712.
Not in our library
254.
Guo M., Cai C., Zhao G., Qiu X., Zhao H., Ma Q., Tian L., Li X., Hu Y., Liao B., et al. Hypoxia promotes migration and induces CXCR4 expression via HIF-1α activation in human osteosarcoma. PLoS ONE. 2014;9:e90518.
Not in our library10.1371/journal.pone.0090518
255.
Guan G., Zhang Y., Lu Y., Liu L., Shi D., Wen Y., Yang L., Ma Q., Liu T., Zhu X., et al. The HIF-1α/CXCR4 pathway supports hypoxia-induced metastasis of human osteosarcoma cells. Cancer Lett. 2015;357:254-264.
Not in our library10.1016/j.canlet.2014.11.034
256.
Marchesi F., Monti P., Leone B.E., Zerbi A., Vecchi A., Piemonti L., Mantovani A., Allavena P. Increased survival, proliferation, and migration in metastatic human pancreatic tumor cells expressing functional CXCR4. Cancer Res. 2004;64:8420-8427.
Not in our library10.1158/0008-5472.can-04-1343
257.
Sun J.S., Zhang X.L., Yang Y.J., Nie Z.G., Zhang Y. Hypoxia promotes C-X-C chemokine receptor type 4 expression through microRNA-150 in pancreatic cancer cells. Oncol. Lett. 2015;10:835-840.
Not in our library10.3892/ol.2015.3344
258.
Stromal Derived Factor-1 (SDF-1/CXCL12) and CXCR4 in renal cell carcinoma metastasis · 2006
No notice
259.
Tang M., Yang Y., Yu J., Wu N., Chen P., Xu L., Wang Q., Xu Z., Ge J., Yu K., et al. Discordant mRNA and protein expression of CXCR4 under in vitro CoCl2-induced hypoxic conditions. Biochem. Biophys. Res. Commun. 2017;484:285-291.
Not in our library10.1016/j.bbrc.2017.01.102
260.
Kim S.W., Kim H.Y., Song I.C., Jin S.A., Lee H.J., Yun H.J., Kim S., Jo D.Y. Cytoplasmic trapping of CXCR4 in hepatocellular carcinoma cell lines. Cancer Res. Treat. 2008;40:53-61.
Not in our library10.4143/crt.2008.40.2.53
261.
Esencay M., Sarfraz Y., Zagzag D. CXCR7 is induced by hypoxia and mediates glioma cell migration towards SDF-1α. BMC Cancer. 2013;13:347.
Not in our library10.1186/1471-2407-13-347
262.
Kim H.Y., Lee S.Y., Kim D.Y., Moon J.Y., Choi Y.S., Song I.C., Lee H.J., Yun H.J., Kim S., Jo D.Y. Expression and functional roles of the chemokine receptor CXCR7 in acute myeloid leukemia cells. Blood Res. 2015;50:218-226.
Not in our library10.5045/br.2015.50.4.218
263.
Schioppa T., Uranchimeg B., Saccani A., Biswas S.K., Doni A., Rapisarda A., Bernasconi S., Saccani S., Nebuloni M., Vago L., et al. Regulation of the chemokine receptor CXCR4 by hypoxia. J. Exp. Med. 2003;198:1391-1402.
Not in our library10.1084/jem.20030267
264.
Huang X., Zhou J., Liu J., Tang B., Zhao F., Qu Y. Biological characteristics of prostate cancer cells are regulated by hypoxia-inducible factor 1α. Oncol. Lett. 2014;8:1217-1221.
Not in our library10.3892/ol.2014.2259
265.
Micucci C., Matacchione G., Valli D., Orciari S., Catalano A. HIF2α is involved in the expansion of CXCR4-positive cancer stem-like cells in renal cell carcinoma. Br. J. Cancer. 2015;113:1178-1185.
Not in our library10.1038/bjc.2015.338
266.
Hypoxia and TGF-β Drive Breast Cancer Bone Metastases through Parallel Signaling Pathways in Tumor Cells and the Bone Microenvironment · 2009
No notice
267.
Tu T.C., Nagano M., Yamashita T., Hamada H., Ohneda K., Kimura K., Ohneda O. A Chemokine Receptor, CXCR4, Which Is Regulated by Hypoxia-Inducible Factor 2α, Is Crucial for Functional Endothelial Progenitor Cells Migration to Ischemic Tissue and Wound Repair. Stem Cells Dev. 2016;25:266-276.
Not in our library10.1089/scd.2015.0290
268.
Sun X., Wei L., Chen Q., Terek R.M. MicroRNA regulates vascular endothelial growth factor expression in chondrosarcoma cells. Clin. Orthop. Relat. Res. 2015;473:907-913.
Not in our library10.1007/s11999-014-3842-0
269.
Vandyke K., Zeissig M.N., Hewett D.R., Martin S.K., Mrozik K.M., Cheong C.M., Diamond P., To L.B., Gronthos S., Peet D.J., et al. HIF-2α Promotes Dissemination of Plasma Cells in Multiple Myeloma by Regulating CXCL12/CXCR4 and CCR1. Cancer Res. 2017;77:5452-5463.
Not in our library10.1158/0008-5472.can-17-0115
270.
Spinello I., Quaranta M.T., Paolillo R., Pelosi E., Cerio A.M., Saulle E., Lo Coco F., Testa U., Labbaye C. Differential hypoxic regulation of the microRNA-146a/CXCR4 pathway in normal and leukemic monocytic cells: Impact on response to chemotherapy. Haematologica. 2015;100:1160-1171.
Not in our library10.3324/haematol.2014.120295
271.
Fiegl M., Samudio I., Clise-Dwyer K., Burks J.K., Mnjoyan Z., Andreeff M. CXCR4 expression and biologic activity in acute myeloid leukemia are dependent on oxygen partial pressure. Blood. 2009;113:1504-1512.
Not in our library10.1182/blood-2008-06-161539
272.
Saba F., Soleimani M., Abroun S. New role of hypoxia in pathophysiology of multiple myeloma through miR-210. EXCLI J. 2018;17:647-662.
Not in our library10.17179/excli2018-1109
273.
Namiki A., Brogi E., Kearney M., Kim E.A., Wu T., Couffinhal T., Varticovski L., Isner J.M. Hypoxia induces vascular endothelial growth factor in cultured human endothelial cells. J. Biol. Chem. 1995;270:31189-31195.
Not in our library10.1074/jbc.270.52.31189
274.
Scheurer S.B., Rybak J.N., Rösli C., Neri D., Elia G. Modulation of gene expression by hypoxia in human umbilical cord vein endothelial cells: A transcriptomic and proteomic study. Proteomics. 2004;4:1737-1760.
Not in our library10.1002/pmic.200300689
275.
Zeng H., Wei W., Xu X. Chemokine (C-X-C motif) receptor 4 RNA interference inhibits bone metastasis in breast cancer. Oncol. Lett. 2014;8:77-81.
Not in our library10.3892/ol.2014.2096
276.
Müller A., Homey B., Soto H., Ge N., Catron D., Buchanan M.E., McClanahan T., Murphy E., Yuan W., Wagner S.N., et al. Involvement of chemokine receptors in breast cancer metastasis. Nature. 2001;410:50-56.
Not in our library10.1038/35065016
277.
Andre F., Xia W., Conforti R., Wei Y., Boulet T., Tomasic G., Spielmann M., Zoubir M., Berrada N., Arriagada R., et al. CXCR4 expression in early breast cancer and risk of distant recurrence. Oncologist. 2009;14:1182-1188.
Not in our library10.1634/theoncologist.2009-0161
278.
Hung C.S., Su H.Y., Liang H.H., Lai C.W., Chang Y.C., Ho Y.S., Wu C.H., Ho J.D., Wei P.L., Chang Y.J. High-level expression of CXCR4 in breast cancer is associated with early distant and bone metastases. Tumour Biol. 2014;35:1581-1588.
Not in our library10.1007/s13277-013-1218-9
279.
Devignes C.S., Aslan Y., Brenot A., Devillers A., Schepers K., Fabre S., Chou J., Casbon A.J., Werb Z., Provot S. HIF signaling in osteoblast-lineage cells promotes systemic breast cancer growth and metastasis in mice. Proc. Natl. Acad. Sci. USA. 2018;115:E992-E1001.
Not in our library10.1073/pnas.1718009115
280.
Nomura R., Yoshida D., Teramoto A. Stromal cell-derived factor-1 expression in pituitary adenoma tissues and upregulation in hypoxia. J. Neurooncol. 2009;94:173-181.
Not in our library10.1007/s11060-009-9835-2
281.
Menu E., Asosingh K., Indraccolo S., De Raeve H., Van Riet I., Van Valckenborgh E., Vande Broek I., Fujii N., Tamamura H., Van Camp B., et al. The involvement of stromal derived factor 1alpha in homing and progression of multiple myeloma in the 5TMM model. Haematologica. 2006;91:605-612.
Not in our library
282.
Pennathur-Das R., Levitt L. Augmentation of in vitro human marrow erythropoiesis under physiological oxygen tensions is mediated by monocytes and T lymphocytes. Blood. 1987;69:899-907.
Not in our library10.1182/blood.v69.3.899.899
283.
Asosingh K., De Raeve H., de Ridder M., Storme G.A., Willems A., Van Riet I., Van Camp B., Vanderkerken K. Role of the hypoxic bone marrow microenvironment in 5T2MM murine myeloma tumor progression. Haematologica. 2005;90:810-817.
Not in our library
284.
Storti P., Bolzoni M., Donofrio G., Airoldi I., Guasco D., Toscani D., Martella E., Lazzaretti M., Mancini C., Agnelli L., et al. Hypoxia-inducible factor (HIF)-1α suppression in myeloma cells blocks tumoral growth in vivo inhibiting angiogenesis and bone destruction. Leukemia. 2013;27:1697-1706.
Not in our library10.1038/leu.2013.24
285.
Bao Y., Wang Z., Liu B., Lu X., Xiong Y., Shi J., Li P., Chen J., Zhang Z., Chen M., et al. A feed-forward loop between nuclear translocation of CXCR4 and HIF-1α promotes renal cell carcinoma metastasis. Oncogene. 2019;38:881-895.
Not in our library10.1038/s41388-018-0452-4
286.
Kusuyama J., Bandow K., Ohnishi T., Amir M.S., Shima K., Semba I., Matsuguchi T. CXCL13 is a differentiation- and hypoxia-induced adipocytokine that exacerbates the inflammatory phenotype of adipocytes through PHLPP1 induction. Biochem. J. 2019;476:3533-3548.
Not in our library10.1042/bcj20190709
287.
Ammirante M., Shalapour S., Kang Y., Jamieson C.A., Karin M. Tissue injury and hypoxia promote malignant progression of prostate cancer by inducing CXCL13 expression in tumor myofibroblasts. Proc. Natl. Acad. Sci. USA. 2014;111:14776-14781.
Not in our library10.1073/pnas.1416498111
288.
Lee H.T., Liu S.P., Lin C.H., Lee S.W., Hsu C.Y., Sytwu H.K., Hsieh C.H., Shyu W.C. A Crucial Role of CXCL14 for Promoting Regulatory T Cells Activation in Stroke. Theranostics. 2017;7:855-875.
Not in our library10.7150/thno.17558
289.
Yue F., Cheng Y., Breschi A., Vierstra J., Wu W., Ryba T., Sandstrom R., Ma Z., Davis C., Pope B.D., et al. A comparative encyclopedia of DNA elements in the mouse genome. Nature. 2014;515:355-364.
Not in our library10.1038/nature13992
290.
Chaturvedi P., Gilkes D.M., Takano N., Semenza G.L. Hypoxia-inducible factor-dependent signaling between triple-negative breast cancer cells and mesenchymal stem cells promotes macrophage recruitment. Proc. Natl. Acad. Sci. USA. 2014;111:E2120-E2129.
Not in our library10.1073/pnas.1406655111
291.
Lin S., Sun L., Hu J., Wan S., Zhao R., Yuan S., Zhang L. Chemokine C-X-C motif receptor 6 contributes to cell migration during hypoxia. Cancer Lett. 2009;279:108-117.
Not in our library10.1016/j.canlet.2009.01.029
292.
Ronkainen V.P., Tuomainen T., Huusko J., Laidinen S., Malinen M., Palvimo J.J., Ylä-Herttuala S., Vuolteenaho O., Tavi P. Hypoxia-inducible factor 1-induced G protein-coupled receptor 35 expression is an early marker of progressive cardiac remodelling. Cardiovasc. Res. 2014;101:69-77.
Not in our library10.1093/cvr/cvt226
293.
Chen K., He L., Li Y., Li X., Qiu C., Pei H., Yang D. Inhibition of GPR35 Preserves Mitochondrial Function After Myocardial Infarction by Targeting Calpain 1/2. J. Cardiovasc. Pharmacol. 2020;75:556-563.
Not in our library10.1097/fjc.0000000000000819
294.
Maravillas-Montero J.L., Burkhardt A.M., Hevezi P.A., Carnevale C.D., Smit M.J., Zlotnik A. Cutting edge: GPR35/CXCR8 is the receptor of the mucosal chemokine CXCL17. J. Immunol. 2015;194:29-33.
Not in our library10.4049/jimmunol.1401704
295.
Binti Mohd Amir N.A.S., Mackenzie A.E., Jenkins L., Boustani K., Hillier M.C., Tsuchiya T., Milligan G., Pease J.E. Evidence for the Existence of a CXCL17 Receptor Distinct from GPR35. J. Immunol. 2018;201:714-724.
Not in our library10.4049/jimmunol.1700884
296.
Park S.J., Lee S.J., Nam S.Y., Im D.S. GPR35 mediates lodoxamide-induced migration inhibitory response but not CXCL17-induced migration stimulatory response in THP-1 cells; is GPR35 a receptor for CXCL17? Br. J. Pharmacol. 2018;175:154-161.
Not in our library10.1111/bph.14082
297.
Albadari N., Deng S., Li W. The transcriptional factors HIF-1 and HIF-2 and their novel inhibitors in cancer therapy. Expert Opin. Drug Discov. 2019;14:667-682.
Not in our library10.1080/17460441.2019.1613370
298.
Hyperbaric oxygen therapy and cancer—a review · 2012
No notice
299.
Wu X., Zhu Y., Huang W., Li J., Zhang B., Li Z., Yang X. Hyperbaric Oxygen Potentiates Doxil Antitumor Efficacy by Promoting Tumor Penetration and Sensitizing Cancer Cells. Adv. Sci. 2018;5:1700859.
Not in our library10.1002/advs.201700859
300.
Parmar K., Mauch P., Vergilio J.A., Sackstein R., Down J.D. Distribution of hematopoietic stem cells in the bone marrow according to regional hypoxia. Proc. Natl. Acad. Sci. USA. 2007;104:5431-5436.
Not in our library10.1073/pnas.0701152104
301.
Takubo K., Goda N., Yamada W., Iriuchishima H., Ikeda E., Kubota Y., Shima H., Johnson R.S., Hirao A., Suematsu M., et al. Regulation of the HIF-1alpha level is essential for hematopoietic stem cells. Cell Stem Cell. 2010;7:391-402.
Not in our library10.1016/j.stem.2010.06.020
302.
Winkler I.G., Barbier V., Wadley R., Zannettino A.C., Williams S., Lévesque J.P. Positioning of bone marrow hematopoietic and stromal cells relative to blood flow in vivo: Serially reconstituting hematopoietic stem cells reside in distinct nonperfused niches. Blood. 2010;116:375-385.
Not in our library10.1182/blood-2009-07-233437
303.
Coleman R.L., Brady M.F., Herzog T.J., Sabbatini P., Armstrong D.K., Walker J.L., Kim B.G., Fujiwara K., Tewari K.S., O’Malley D.M., et al. Bevacizumab and paclitaxel-carboplatin chemotherapy and secondary cytoreduction in recurrent, platinum-sensitive ovarian cancer (NRG Oncology/Gynecologic Oncology Group study GOG-0213): A multicentre, open-label, randomised, phase 3 trial. Lancet Oncol. 2017;18:779-791.
Not in our library10.1016/s1470-2045(17)30279-6
304.
Zhu P., Du X.L., Lu G., Zhu J.J. Survival benefit of glioblastoma patients after FDA approval of temozolomide concomitant with radiation and bevacizumab: A population-based study. Oncotarget. 2017;8:44015-44031.
Not in our library10.18632/oncotarget.17054
305.
PD-L1 blockade enhances anti-tumor efficacy of NK cells · 2018
Not checked
306.
Ni X., Xing Y., Sun X., Suo J. The safety and efficacy of anti-PD-1/anti-PD-L1 antibody therapy in the treatment of previously treated, advanced gastric or gastro-oesophageal junction cancer: A meta-analysis of prospective clinical trials. Clin. Res. Hepatol. Gastroenterol. 2020;44:211-222.
Not in our library10.1016/j.clinre.2019.05.007
307.
Wang J., Hu W., Wang K., Yu J., Luo B., Luo G., Wang W., Wang H., Li J., Wen J. Repertaxin, an inhibitor of the chemokine receptors CXCR1 and CXCR2, inhibits malignant behavior of human gastric cancer MKN45 cells in vitro and in vivo and enhances efficacy of 5-fluorouracil. Int. J. Oncol. 2016;48:1341-1352.
Not in our library10.3892/ijo.2016.3371
308.
Fu S., Chen X., Lin H.J., Lin J. Inhibition of interleukin 8/C-X-C chemokine receptor 1,/2 signaling reduces malignant features in human pancreatic cancer cells. Int. J. Oncol. 2018;53:349-357.
Not in our library10.3892/ijo.2018.4389
309.
Dufies M., Grytsai O., Ronco C., Camara O., Ambrosetti D., Hagege A., Parola J., Mateo L., Ayrault M., Giuliano S., et al. New CXCR1/CXCR2 inhibitors represent an effective treatment for kidney or head and neck cancers sensitive or refractory to reference treatments. Theranostics. 2019;9:5332-5346.
Not in our library10.7150/thno.34681
310.
Xu M., Jiang H., Wang H., Liu J., Liu B., Guo Z. SB225002 inhibits prostate cancer invasion and attenuates the expression of BSP, OPN and MMP-2. Oncol. Rep. 2018;40:726-736.
Not in our library10.3892/or.2018.6504
311.
Dominguez C., McCampbell K.K., David J.M., Palena C. Neutralization of IL-8 decreases tumor PMN-MDSCs and reduces mesenchymalization of claudin-low triple-negative breast cancer. JCI Insight. 2017;2:e94296.
Not in our library10.1172/jci.insight.94296
312.
Phase I trial of HuMax-IL8 (BMS-986253), an anti-IL-8 monoclonal antibody, in patients with metastatic or unresectable solid tumors · 2019
No notice
313.
Aalinkeel R., Nair B., Chen C.K., Mahajan S.D., Reynolds J.L., Zhang H., Sun H., Sykes D.E., Chadha K.C., Turowski S.G., et al. Nanotherapy silencing the interleukin-8 gene produces regression of prostate cancer by inhibition of angiogenesis. Immunology. 2016;148:387-406.
Not in our library10.1111/imm.12618
314.
Miyake M., Furuya H., Onishi S., Hokutan K., Anai S., Chan O., Shi S., Fujimoto K., Goodison S., Cai W., et al. Monoclonal Antibody against CXCL1 (HL2401) as a Novel Agent in Suppressing IL6 Expression and Tumoral Growth. Theranostics. 2019;9:853-867.
Not in our library10.7150/thno.29553
315.
Idorn M., Olsen M., Halldórsdóttir H.R., Skadborg S.K., Pedersen M., Høgdall C., Høgdall E., Met Ö., Thor Straten P. Improved migration of tumor ascites lymphocytes to ovarian cancer microenvironment by CXCR2 transduction. Oncoimmunology. 2017;7:e1412029.
Not in our library10.1080/2162402x.2017.1412029
316.
Genetic engineering of human NK cells to express CXCR2 improves migration to renal cell carcinoma · 2017
Corrected
317.
Broussas M., Boute N., Akla B., Berger S., Beau-Larvor C., Champion T., Robert A., Beck A., Haeuw J.F., Goetsch L., et al. A New Anti-CXCR4 Antibody That Blocks the CXCR4/SDF-1 Axis and Mobilizes Effector Cells. Mol. Cancer Ther. 2016;15:1890-1899.
Not in our library10.1158/1535-7163.mct-16-0041
318.
Reeves P.M., Abbaslou M.A., Kools F.R.W., Poznansky M.C. CXCR4 blockade with AMD3100 enhances Taxol chemotherapy to limit ovarian cancer cell growth. Anticancer Drugs. 2017;28:935-942.
Not in our library10.1097/cad.0000000000000518
319.
Luo Y., Azad A.K., Karanika S., Basourakos S.P., Zuo X., Wang J., Yang L., Yang G., Korentzelos D., Yin J., et al. Enzalutamide and CXCR7 inhibitor combination treatment suppresses cell growth and angiogenic signaling in castration-resistant prostate cancer models. Int. J. Cancer. 2018;142:2163-2174.
Not in our library10.1002/ijc.31237
320.
Zhou K.X., Xie L.H., Peng X., Guo Q.M., Wu Q.Y., Wang W.H., Zhang G.L., Wu J.F., Zhang G.J., Du C.W. CXCR4 antagonist AMD3100 enhances the response of MDA-MB-231 triple-negative breast cancer cells to ionizing radiation. Cancer Lett. 2018;418:196-203.
Not in our library10.1016/j.canlet.2018.01.009
321.
Bockorny B., Semenisty V., Macarulla T., Borazanci E., Wolpin B.M., Stemmer S.M., Golan T., Geva R., Borad M.J., Pedersen K.S., et al. BL-8040, a CXCR4 antagonist, in combination with pembrolizumab and chemotherapy for pancreatic cancer: The COMBAT trial. Nat. Med. 2020;26:878-885.
Not in our library10.1038/s41591-020-0880-x
322.
D’Alterio C., Zannetti A., Trotta A.M., Ieranò C., Napolitano M., Rea G., Greco A., Maiolino P., Albanese S., Scognamiglio G., et al. New CXCR4 Antagonist Peptide R (Pep R) Improves Standard Therapy in Colorectal Cancer. Cancers. 2020;12:1952.
Not in our library10.3390/cancers12071952
323.
CXCR4 Antagonist AMD3100 Reverses the Resistance to Tamoxifen in Breast Cancer via Inhibiting AKT Phosphorylation · 2020
Not checked
324.
Vela M., Bueno D., González-Navarro P., Brito A., Fernández L., Escudero A., Valentín J., Mestre-Durán C., Arranz-Álvarez M., Pérez de Diego R., et al. Anti-CXCR4 Antibody Combined with Activated and Expanded Natural Killer Cells for Sarcoma Immunotherapy. Front. Immunol. 2019;10:1814.
Not in our library10.3389/fimmu.2019.01814
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Li Z., Wang Y., Shen Y., Qian C., Oupicky D., Sun M. Targeting pulmonary tumor microenvironment with CXCR4-inhibiting nanocomplex to enhance anti-PD-L1 immunotherapy. Sci. Adv. 2020;6:eaaz9240.
Not in our library10.1126/sciadv.aaz9240
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Chittasupho C., Anuchapreeda S., Sarisuta N. CXCR4 targeted dendrimer for anti-cancer drug delivery and breast cancer cell migration inhibition. Eur. J. Pharm. Biopharm. 2017;119:310-321.
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Céspedes M.V., Unzueta U., Aviñó A., Gallardo A., Álamo P., Sala R., Sánchez-Chardi A., Casanova I., Mangues M.A., Lopez-Pousa A., et al. Selective depletion of metastatic stem cells as therapy for human colorectal cancer. EMBO Mol. Med. 2018;10:e8772.
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Taslimi Y., Zahedifard F., Habibzadeh S., Taheri T., Abbaspour H., Sadeghipour A., Mohit E., Rafati S. Antitumor Effect of IP-10 by Using Two Different Approaches: Live Delivery System and Gene Therapy. J. Breast Cancer. 2016;19:34-44.
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336.
Wu X., Sun A., Yu W., Hong C., Liu Z. CXCL10 mediates breast cancer tamoxifen resistance and promotes estrogen-dependent and independent proliferation. Mol. Cell Endocrinol. 2020;512:110866.
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337.
Ma J.J., Jiang L., Tong D.Y., Ren Y.N., Sheng M.F., Liu H.C. CXCL13 inhibition induce the apoptosis of MDA-MB-231 breast cancer cells through blocking CXCR5/ERK signaling pathway. Eur. Rev. Med. Pharmacol. Sci. 2018;22:8755-8762.
Not in our library10.26355/eurrev_201812_16641
338.
Matsumura S., Demaria S. Up-regulation of the pro-inflammatory chemokine CXCL16 is a common response of tumor cells to ionizing radiation. Radiat. Res. 2010;173:418-425.
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