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Molecular and clinical significance of fibroblast growth factor 2 (FGF2 /bFGF) in malignancies of solid and hematological cancers for personalized therapies

Mohamed R. Akl, Poonam Nagpal, Nehad M. Ayoub and 6 more

Oncotarget · 2016 · Review

Abstract

// Mohamed R. Akl 1 , Poonam Nagpal 1 , Nehad M. Ayoub 2 , Betty Tai 1 , Sathyen A. Prabhu 1 , Catherine M. Capac 1 , Matthew Gliksman 1 , Andre Goy 3 and K. Stephen Suh 1 1 Genomics and Biomarkers Program, The John Theurer Cancer Center, Hackensack University Medical Center, Hackensack, NJ, USA 2 Department of Clinical Pharmacy, Faculty of Pharmacy, Jordan University of Science and Technology, Irbid, Jordan 3 Lymphoma Division, The John Theurer Cancer Center, Hackensack University Medical Center, Hackensack, NJ, USA Correspondence to: K. Stephen Suh, email: // Keywords : bFGF, FGF2, diagnosis, prognosis, malignancy, Received : October 20, 2015 Accepted : March 10, 2016 Published : March 19, 2016 Abstract Fibroblast growth factor (FGF) signaling is essential for normal and cancer biology. Mammalian FGF family members participate in multiple signaling pathways by binding to heparan sulfate and FGF receptors (FGFR) with varying affinities. FGF2 is the prototype member of the FGF family and interacts with its receptor to mediate receptor dimerization, phosphorylation, and activation of signaling pathways, such as Ras-MAPK and PI3K pathways. Excessive mitogenic signaling through the FGF/FGFR axis may induce carcinogenic effects by promoting cancer progression and increasing the angiogenic potential, which can lead to metastatic tumor phenotypes. Dysregulated FGF/FGFR signaling is associated with aggressive cancer phenotypes, enhanced chemotherapy resistance and poor clinical outcomes. In vitro experimental settings have indicated that extracellular FGF2 affects proliferation, drug sensitivity, and apoptosis of cancer cells. Therapeutically targeting FGF2 and FGFR has been extensively assessed in multiple preclinical studies and numerous drugs and treatment options have been tested in clinical trials. Diagnostic assays are used to quantify FGF2, FGFRs, and downstream signaling molecules to better select a target patient population for higher efficacy of cancer therapies. This review focuses on the prognostic significance of FGF2 in cancer with emphasis on therapeutic intervention strategies for solid and hematological malignancies.

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From PubMed Central, U.S. National Library of Medicine, as current on Oct 21, 2026. Paragraph numbers are ours, so an answer can point at one.

INTRODUCTION

1The fibroblast growth factor (FGF) family consists of 23 FGF signaling polypeptides that function as potent mitogens. FGFs exert broad mitogenic activity by stimulating the growth of fibroblasts, endothelial, and cancer cells. The family plays important roles in embryonic development, maintenance of adult organ systems, tissue regeneration, wound repair, and hematopoiesis. FGF2, also known as basic FGF (bFGF), is the prototypical and most studied member of the FGF superfamily. FGF2 is an important regulator of cell growth and differentiation under physiological and pathological conditions. Previous studies have suggested a role of FGF2 as a prognostic marker for different types of malignancies. This review summarizes the biology of FGF signaling by demonstrating biological roles of FGF2 in regards to pathogenesis and prognosis of solid and hematological tumors with a special focus on clinical development of FGF2 inhibitors in the era of personalized medicine.

FGF2 isoforms, receptors, binding partners, and signaling

2FGF2 exists in low and high molecular weight isoforms, which are translated from a single common mRNA through alternative translation-initiation codons. Low molecular weight (LMW) FGF2 is an 18 kDa protein translated from a conventional AUG start codon. LMW FGF2 is found in the cytoplasm and nucleus and can be also secreted by target cells. In order to initiate signaling, LMW FGF2 interacts with cell surface heparan sulfate proteoglycans (HSPGs) and fibroblast growth factor receptor (FGFR) in a ternary complex consisting of FGF2, FGFR, and HSPG resulting in activation of downstream signaling pathways, including Ras, Raf, MAPK and ERK (Figure 1A). High molecular weight (HMW) FGF2 isoforms (22-, 22.5-, 24-, and 34-kDa) are produced through translation initiation at CUG sites upstream and in frame of the AUG codon. HMW FGF2 localizes to the nucleus and signals independently of FGFRs. Similar to HMW FGF2, LMW FGF2 can also function in the cytosol and nucleus of cells through endocytosis of activated FGF-FGFR complexes. FGFR1 and FGF2 have been shown to co-localize in the nuclear matrix, where together they may co-activate transcription and thus control cell proliferation (Figure 1A).

3Five FGFRs have been identified, four of which (1-4) are highly conserved single-pass transmembrane tyrosine kinase receptors. The extracellular regions of these receptors contain three immunoglobulin (Ig)-like domains (designated as IgI, IgII, and IgIII) linked to the cytoplasmic domain via a transmembrane α-helix (Figure 1A). FGFRs 1-3 can undergo alternative splicing during gene expression, and the IgIII domain is composed of an invariant IgIIIa exon alternatively spliced to IgIIIb or IgIIIc. The expression of IgIIIb and IgIIIc is important in defining FGF signaling specificity. While FGF1 binds to all FGFRs, FGF2 binds to FGFR1 (IIIb), FGFR1 (IIIc), FGFR2 (IIIc), and FGFR4. It has been reported that LMW FGF2 predominantly binds to FGFR1 (IIIc) and weakly to the other FGFRs. The cytoplasmic domain of FGFRs 1-4 contains a juxtamembrane split kinase domain, which contains tyrosine kinase motifs and a C-terminal tail. Although FGFR5 lacks intracellular tyrosine kinase domain, this receptor can bind to multiple FGF ligands acting as a negative regulator of signaling.

4FGF2 utilizes HSPGs, such as syndecans (SDC), as binding partners to stabilize the FGF-FGFR interaction and enhance resistance to proteolysis. FGF2 cannot activate FGFRs in cells lacking heparan sulfate. After the binding of FGF and HSPG to FGFR to form a ternary FGF:FGFR:HSPG complex, FGFRs dimerize leading to conformational changes in FGFR structure and subsequent intermolecular transphosphorylation of multiple cytoplasmic tyrosine residues (Figure 1A). FGFR transmits extracellular signals to two main intracellular substrates, which are phospholipase C-γ1 (PLC-γ1) (also known as FRS1) and FGFR substrate 2 (also known as FRS2) (Figure 1A). The phosphorylation of FGFR1 tyrosine residues creates binding sites for SH2 domain of PLC-γ required for phosphorylation and activation of PLC-γ. Conversely, FRS2 constitutively associates with the juxtamembrane region of the FGFR. The phosphorylation of FRS2 is essential for activation of the Ras-mitogen-activated protein kinase (MAPK) and phosphoinositide 3-kinase-Akt (PI3K-Akt) signaling pathways in cancer and endothelial cells (Figure 1A).

5FGF2 also interacts with immobilized molecules bound to extracellular matrix (ECM), including cell membrane receptors and soluble molecules (Table 1, Figure 1B). The complex interactions between FGF2 and these molecules control bioavailability, stability, and concentration of FGF2 in the microenvironment. FGF2 can tightly bind HSPG in ECM and is only released through the action of FGF-binding protein (FGF-BP), which is a critical controller of FGF bioavailability (Table 1, Figure 1B). In addition, the binding of FGF to heparin, released HSPG, or cell surface-bound HSPG also regulate FGF bioavailability and the interactions with FGFRs (Table 1, Figure 1B). Conversely, thrombospondin-1 (TSP-1) and pentraxin 3 (PTX3) prevent the interaction of FGF2 with cell surface HSPGs and FGFRs. Similarly; xcFGFR1 (a soluble form of the extracellular portion of FGFR1) binds FGF2 and prevents FGF2/FGFR interaction (Table 1, Figure 1B).

6Gangliosides are glycosphingolipids bound to cell membranes regulating growth of a wide variety of normal cells by binding to FGFs. Gangliosides are highly synthesized in metastatic tumors and are known to shed into the ECM. Integrins are transmembrane receptors that regulate the response to soluble FGF2 in endothelial cells. The interaction between αvβ3 integrin and FGF2 promotes endothelial cell proliferation by activating the MAPK pathway. In addition, the binding of fibrinogen to FGF2 requires αvβ3 integrin to promote endothelial cell proliferation (Table 1, Figure 1B). These findings indicate that FGF2 bioactivity and interaction with FGFR is highly regulated by a complex network of interactions with various FGF2 binding partners.

ROLES OF FGF2 IN TUMOR PROGRESSION

7Accumulating evidence suggests that FGF2/FGFR signaling is involved in several biological functions, such as embryonic development, tissue regeneration, wound repair, and normal hematopoiesis. Expression of FGF2 and FGFRs in normal cells is highly regulated, and termination of FGF2 signaling is achieved through receptor internalization (Figure 2A). However, FGF2/FGFR signaling in cancer cells is dysregulated, which may contribute to the pathogenesis of many types of cancer (Figure 2A). Several studies have shown that FGF2 is a key tumor-promoting factor in the tumor microenvironment. The following section reviews current knowledge of the molecular pathways associated with FGF2 signaling in cancer, which represents a critical step for the implementation of strategies toward the development of personalized cancer therapy.

Deregulation of FGFR signaling

8FGFR amplification and/or upregulation occur in cancer due to deregulated transcription or chromosomal amplification (Figure 2A). The upregulation of FGFR1 induces cellular transformation of non-transformed cells. FGFR2 upregulation is associated with poor prognosis in patients of multiple cancer types. Furthermore, FGFR2 amplification has been shown to be accompanied with C-terminal exon abrogation, which regulates receptor internalization. Impaired termination of FGFR signaling leads to continuous receptor activation. In addition, mutation of FGFR can also render it insensitive to endocytosis by maintaining its expression at the cell surface. A number of germline activating point mutations of FGFRs have been identified in human cancers and are associated with poor survival and chemoresistance. Mutations in the extracellular domain of FGFRs facilitate ligand binding, while mutations in transmembrane and kinase domains lead to constitutive activation of receptors (Figure 2A). Furthermore, alternative splicing of the third Ig-like domain could promote tumorigenesis. Paracrine signaling typically occurs through FGFR-IIIb that is expressed on mesenchymal cells and -IIIc expressed on epithelial cells. In cancer models, however, the switch from FGFR IIIb to FGFR IIIc by alternative splicing results in autocrine activation of the receptor (Figure 2A). For example, FGFR2-IIIb to IIIc switch is related to increased invasiveness in bladder and prostate cancers. In addition, FGFR1-IIIc has been upregulated in pancreatic cancer where it is regarded as a strong oncogene.

FGF2 as pro-angiogenic agent

9FGF2 is an extremely potent pro-angiogenic growth factor. FGF2 exerts its effects on endothelial cells via a paracrine mode after being released by tumor and stromal cells or through mobilization from ECM (Figure 2B). In addition, FGF2 plays autocrine roles in endothelial cells. It has been reported that endothelial cells predominantly express FGFR1 and to some extent FGFR2. Activation of these receptors by FGF2 leads to endothelial cell proliferation, migration, protease production, and angiogenesis. Furthermore, the full mitogenic and chemotactic responses of FGF2 in endothelial cells require activation of ERK1/2 and protein kinase C (PKC) signaling pathways. FGF2 upregulates plasmin-plasminogen activator (uPA) and matrix metalloproteinase (MMP) production in endothelial cells eventually leading to ECM degradation and angiogenesis. In addition, the response of endothelial cells to FGF2 can be regulated by integrins. Immobilized FGF2 binds to αvβ3 integrin causing endothelial cell adhesion, migration, proliferation, and morphogenesis (Figure 2B). There is also considerable cross-talk between FGF and vascular endothelial growth factor (VEGF) signaling, whereby FGF-induced signaling promotes resistance to VEGF receptor signaling for blocking of the VEGF. Moreover, transient expression of FGF2 in endothelial cells control the expression of genes implicated in cell cycle, differentiation, adhesion, and cell survival. Taken together, these data suggest an important role of FGF2 in promoting endothelial cell angiogenesis (Figure 2B).

FGF2 as mitogen for tumor cells

10Although FGF2 levels are elevated in several human cancers, FGF2 levels do not always correlate with microvessel density. For example, in a study conducted by Kuwahara et al, majority of pancreatic ductal carcinomas were positive for VEGF and FGF2. A significant correlation was observed between VEGF expression and MVD but not between FGF2 and MVD. However, in a study conducted by Garcia de la Torre et al, FGF2 expression was high in primary parathyroid hyperplasia (PPH) and FGF2 scores and MVD were significantly correlated. Therefore, FGF2 may contribute to cancer progression through alternative mechanisms involve acting directly on tumor cells. Mutations in genes encoding FGFs and FGFRs deregulate FGFR signaling. However, no activating mutations have been reported as yet for FGF2. FGF2-induced activation of FGFR signaling and subsequent activation of PI3K/Akt and ERK1/2 signaling pathways in cancer cells. FGF2 contributes to tumor progression through enhanced expression and/or release from tumor, endothelial, or stromal cells as well as release from local reservoirs in the ECM (Figure 2B). Secretion of proteases leads to release of the sequestered FGF2. Therefore, FGF2 functions in an autocrine or paracrine manner in cancer cells (Figure 2B).

FGF2 as mitogen for stromal cells

11Tumor progression to metastatic stage is promoted by fibroblasts in tumor stroma through secretion of multiple paracrine factors. FGF2 secreted by stromal fibroblasts induces tumor cell proliferation via FGFR paracrine signaling (Figures 2A, 2B). In addition, fibroblasts within tumor stroma can be activated by FGF2 secreted from endothelial and tumor cells (Figure 2B). Activated fibroblasts also produce proteases, such as MMPs that degrade ECM and promote secretion of growth factors including FGF2 in the tumor microenvironment.

Dysregulated downstream FGF2/FGFR signaling pathway in hematological tumors

12Growing evidence supports a role of FGF2 in hematopoiesis starting at early stages of development through adulthood. In early stages of development, FGF2 has an important role in the proliferation of hemangioblasts, which are common progenitors of hematopoietic and endothelial cells that play a central role in hematopoietic and angiogenic differentiation. In addition, FGF2 plays a role in self-renewal, cell survival, and cell adhesion of human embryonic stem cells. In adult hematopoiesis, FGF2 induces proliferation of stromal cells of bone marrow. FGF2 also induces the production of interleukin-6 (IL-6) and counteracts the suppressive effect of transforming growth factor beta (TGF-β) on myeloid progenitor cells. Myeloid precursor cells can be induced by FGF2 to give rise to erythroid progenitors. In the absence of FGF2, myeloid progenitors generate cells of the neutrophil-granulocyte lineage upon FGF2 induction.

13Neoplastic cells that define each hematological tumor are descendants of a specific lineage of the hematopoietic process. The involvement of FGF2 in various stages of hematopoiesis suggests that its dysregulation can result in hematological cancers. FGFRs are expressed on all cell types of haematopoietic origin, and deregulation of FGFR gene expression or mutation has been observed in haematologic malignancies. The ability of FGF2 to induce stem cell proliferation and differentiation implies that FGF2 is involved in very early stages of hematopoiesis. It has been reported that lymphoma cell lines express FGF2 and FGFRs and release FGF2 into culture media.

Putative mechanisms of FGF2 in Hodgkin Lymphoma

14Hodgkin lymphoma (HL) is a rare B-cell malignant neoplasm characterized by a paucity of malignant Hodgkin and Reed-Sternberg cells (HRS cells) embedded within an inflammatory infiltrate. FGF2 causes aberrant signaling activities in HRS cells involving SDC1, NF-κB, IL-6, Ras/ERK, and JAK/STAT as shown below.

15SDC1 regulates bioavailability, dimerization, and interaction of FGF2 with FGFRs. Witzig and colleagues reported that SDC1 was expressed in the bone marrow of patients with plasma cell proliferative disorders. In line with this, increased expression of FGF2 and SDC1 was also reported in HL cell lines. Overall, findings suggest that increased expression of FGF2, FGFR, and SCD1 is associated with poor prognosis and chemoresistance.

16Activation of the NF-κB pathway is a well-established mechanism for protection of tumor cells from apoptosis. In HL, NF-κB is constitutively activated and represents an important step for the proliferation of neoplastic HRS cells (Figure 3). Epstein-Barr Virus (EBV) is a risk factor for HL. In EBV-positive (EBV+) HL, the EBV oncoprotein, latent membrane protein-1 (LMP1), has been implicated in the activation of NF-κB signaling leading to enhanced B-cell survival. Alternatively, NF-κB may serve as a transcription factor for the FGF2 gene regulating expression and release of FGF2 by LMP1. This process could be of clinical importance for determining the relationship between EBV status and FGF2 levels in HL patients (Figure 3). IL-1β, which is expressed in subsets of cells in the HL tumor microenvironment, activates PI3K signaling pathway to upregulate FGF2 production through NF-κB.

17The interleukin-6 (IL-6) signaling pathway has also been implicated in tumor progression. In multiple myeloma, stromal-derived IL-6 stimulates FGF2 expression in tumor cells, which in turn stimulates the secretion of IL-6. In addition, IL-6 and FGF2 together can enhance proliferation of myeloma cells. In HL, IL-6 and its receptors are expressed by HRS cells (Figure 3). Moreover, IL-6 is upregulated in serum of HL patients resulting in poor prognosis. FGF2 upregulates IL-6 gene expression in the fibroblast NIH-3T3 cell line. Moreover, in a basal cell carcinoma cell line, IL-6 mediates upregulation of FGF2 through activation of JAK/STAT3 and PI3K/Akt pathways which are aberrantly activated in HL. Therefore, IL-6 and FGF2 may be involved in paracrine and autocrine interactions to promote chemoresistance in relapsed/refractory HL.

18Components of the Ras/ERK pathway are aberrantly expressed in malignancies and associated with chemoresistance. MEK/ERK signaling pathway is essential for proliferation and survival of neoplastic HRS cells (Figure 3). FGF2 induces MEK signaling to upregulate anti-apoptotic proteins and enhance chemoresistance. In addition, FGF2 mediates chemoresistance to doxorubicin in endothelial cells by inhibiting the pro-apoptotic protein ASK1, which is a member of the MEKK family.

19The Janus kinase-signal transducer and activator of transcription (JAK/STAT) is a frequently altered pathway in the pathogenesis of HL. The JAK/STAT pathway has been implicated in FGF2-induced chemoresistance in human cancer cells. The JAK2 inhibitor lestaurtinib can overcome JAK/STAT-induced drug resistance in refractory HL cell lines. Therefore, FGF2 may promote chemoresistance by deregulation of JAK/STAT signaling in HRS cells of relapsed and refractory HL patients (Figure 3).

20The above studies demonstrated key downstream signaling pathways in HL, including cell growth, survival, and angiogenesis. It seems clear that the main pathways contributing to HL are regulated, at least in part, by FGF2 (Figure 3). Therefore, clinical trials using agents that target FGF pathway may be promising for treatment of HL.

CLINICAL PROGNOSTIC VALUE AND FUNCTIONAL SIGNIFICANCE OF FGF2 IN SOLID AND HEMATOLOGICAL TUMORS

21Several studies have compared FGF2 serum levels in cancer patients to those in healthy volunteers (Tables 2 and 3). FGF2 expression in sera quantified by ELISA was strongly increased in cancer patients compared to healthy donors. Significant correlations between serum FGF2 levels and tumor stage, size, and metastasis were reported in endometrial, colorectal, esophageal, head and neck, liver, renal, and testicular cancers. However, no significant correlation was observed between increased serum FGF2 levels and tumor grade in bladder, breast, lung, and prostate cancers. In all leukemia and lymphoma studies, there was no correlation between increased serum levels of FGF2 and microvessel density or stage of the disease. However, high serum FGF2 levels were significantly correlated with tumor bulkiness in Non-Hodgkin's lymphoma (NHL). Therefore, the levels of serum FGF2 may have prognostic significance in these cancers, and quantification of FGF2 may provide an indirect, non-invasive way to monitor patients with high risk of relapse from solid and hematological tumors (Tables 2 and 3).

22FGF2 expression in cancer surgical sections has been evaluated using immunohistochemical, Western blot, and qRT-PCR techniques (Tables 2 and 3). Up-to-date diagnostics and antibodies that allow detection and precise quantification of FGF2 are listed in Table 4. Immunohistochemical and immunofluorescence studies have shown that FGF2 staining is heterogeneous and significantly increased in malignant tissues compared to benign or normal tissues (Tables 2 and 3). The differential expression and localization of FGF2 was also studied in different cancers. For example, FGF2 expression is generally limited to the cytoplasm of breast cancer tissues, while it is exclusively expressed in the nuclei of normal mammary tissues. Similarly, FGF2 is strongly expressed in the cytoplasm of malignant melanocytes and prostate cancer tissues, while it is almost entirely restricted to the nuclei of benign cells. In pancreatic cancer cells, FGF2 staining is intense in both the cytoplasm and nucleus, while it is weak in normal control tissues. Different expression and localization of FGF2 suggests that FGF2 and different members of FGFR may have different functions and signaling in various cancers. Moreover, FGF2 expression was elevated in tumor stroma, including inflammatory cells, myofibroblasts, and endothelial cells in colorectal, pancreatic, and prostate carcinomas, respectively (Table 2). These findings suggest that FGF2 can modulate tumor progression by activating signaling pathways in cancer-associated fibroblasts, endothelial cells, and cancer cells. In addition, fibroblasts that are abundant in the stroma of carcinomas at advanced stages of disease can mediate resistance to treatment via FGF2 secretion. Additional studies on tissue sections have revealed that high FGF2 intratumoral levels are associated with advanced tumor stages of bladder, glioma, head and neck, liver, and prostate cancers (Table 2).

23There is an urgent need for the identification of novel prognostic biomarkers to improve treatment of poor outcome cancer patients. It is worth noting that in the vast majority of studies, high serum and intratumoral FGF2 levels were associated with reduced cancer patient survival. In addition, high intratumoral and serum levels of FGF2 were associated with relapse and/or recurrence in various cancers such as bladder, breast, esophageal cancers and HL (Tables 2 and 3). In spite of a few contradictory finding, FGF2 is considered a significant tumor biomarker and a potential therapeutic target. Ongoing and future clinical trials are warranted to determine whether FGF2 could be incorporated in cancer prognosis and whether FGF targeting therapies have a favorable effect on cancer recurrence and mortality.

TARGETING THE FGF2/FGFR PATHWAY IN CANCER

24The trend in cancer personalized medicine is to search for biomarkers to predict a patient's response to the targeted therapy and the emergence of secondary resistance. High expression of FGF2 correlates with a worse survival for relapsed/refractory cancer patients (Tables 2 and 3). Therefore, targeting FGF signaling may provide opportunities for personalized therapy in those patients. Several FGF2/FGFR inhibitors have shown promising anticancer and antiangiogenic efficacy in several in vitro assays and in vivo preclinical animal models (Table 5, Figure 4). Clinical studies on these compounds have been conducted in the last decade to evaluate their safety, efficacy, and tolerability (Table 6). Ongoing clinical trials are recruiting patients with metastatic, advanced, or relapsed/refractory cancers to evaluate the importance of blocking the FGF2/FGFR signaling in progressive and poor outcome cancer patients (Table 6).

25It has been reported that various molecules can inhibit FGF2 (ligand) activity, binding, or expression in endothelial and tumor cells (Table 5, Figure 4). FGF ligand traps, such as FP-1039, block FGF2 interaction with FGFR (Tables 5 and 6, Figure 4). A phase I clinical trial was conducted to investigate the safety and tolerability of FP-1039 in advanced solid tumors (Table 6). FP-1039 is a soluble FGFR1 Fc fusion protein that was engineered to strongly bind all mitogenic FGF ligands. This compound showed promising results and inhibited FGF-mediated cell proliferation and angiogenesis in lung and endometrial cancer models. AGM-1470, miRNA 646, and interferon alpha downregulate FGF2 expression in cancer cells (Table 5, Figure 4). A phase II clinical study was conducted to evaluate the efficacy of pegintron (peginterferon alpha-2b) in patients with stage IV metastatic melanoma overexpressing FGF2 (Table 6). The results showed that peginterferon alpha-2b suppressed FGF2 levels in 97% of patients with metastatic melanoma to reference range with a median progression free survival (PFS) and overall survival (OS) of 2.0 and 9.7 months, respectively (Table 6).

26Other FGF2 antagonists are under investigation for cell line and animal preclinical cancer models. Small molecules, such as sm27, pentosan, and PI-88 as well as proteins such as pentraxin-3 inhibit FGF2 binding to FGFRs (Table 5, Figure 4). The capability of FGF2 to bind heparin/heparan sulfate indicates that molecules able to interfere with this interaction may act as angiogenesis inhibitors. On this basis, compounds such as suramin, which mimic heparin, can interfere with FGF2 signaling (Table 5). Thalidomide, PAMPS, sirolimus, suramin, and platelet factor 4 inhibit FGF2-induced angiogenesis, while anvirzel inhibits FGF2 export via Na+/K+ pumps (Table 5).

27It has been reported that direct inhibition of FGFRs using small molecule inhibitors may be effective in cancer treatment. Several FGFR tyrosine kinase inhibitors (TKIs) are currently in early clinical development (Tables 5 and 6, Figure 4), and many of them exhibit dual specificity for FGFR and VEGFR due to similarity in the ATP binding pocket structure. The first generation of inhibitors were developed as VEGFR and PDGFR inhibitors, but also can inhibit FGFR. These compounds were successful in clinical trials and some of these drugs and drug combinations were subsequently approved by regulatory administrations worldwide for the treatment of different cancers (Tables 5 and 6).

28Recently, the U.S. Food and Drug Administration (FDA) granted approval to Lenvima (lenvatinib, developed by Eisai) based on the results of a study on 392 patients with locally recurrent or metastatic, progressive, radioactive iodine-refractory differentiated thyroid cancer (DTC) who were randomly assigned to receive either Lenvima or a placebo. Study results showed that Lenvima-treated participants lived a median of 18.3 months (PFS) compared to a median of 3.6 months for participants who received placebo. Moreover, approximately two thirds of participants treated with Lenvima showed a reduction in tumor size compared to only two percent of participants who received placebo. Similarly, FDA recently approved Iclusig (ponatinib, developed by ARIAD Pharmaceuticals), which is a multi-tyrosine kinase inhibitor for the treatment of adult patients with chronic myeloid leukemia or acute lymphoblastic leukemia (Table 5). Moreover, the multi-tyrosine kinase inhibitor Votrient (pazopanib, developed by GlaxoSmithKline) was approved by FDA to treat patients with advanced renal cell cancer and patients with advanced soft tissue sarcoma who have received chemotherapy in the past (Tables 5 and 6).

29Dovitinib (TKI-258, CHIR-258, developed by Novartis) is a potent VEGFR, PDGFR and FGFR inhibitor. Dovitinib showed promising anticancer and antiangiogenic activity against multiple myeloma and colon cancer models. A phase II trial was conducted to evaluate the safety and tolerability of Dovitinib in relapsed or refractory multiple myeloma patients, who are with or without t(4;14) chromosomal translocation (Table 6). The t(4;14) translocation is observed in approximately 15-20% of multiple myeloma patients, and it is associated with upregulation of FGFR3 and poor prognosis. Upregulation of FGFR3 occurs in nearly 70% of patients with the t(4;14) translocation. Therefore, development of inhibitors such as Dovitinib may show promise in t(4;14) multiple myeloma patients. Further phase II clinical trials were conducted on Dovitinib for treatment of other types of cancers including lung, bladder and gastric cancers (Table 6).

30Other investigational multi-kinase inhibitors, such as Brivanib, Orantinib, and Lucitanib, are currently progressing into phases II and III of clinical trials (Tables 5 and 6). Recent clinical trials have assessed the combination of a tyrosine kinase inhibitor with cytotoxic agents (Table 6). Combination strategies that involve the blockade of FGFR signaling with cytotoxic agents have the best clinical outcome for cancer treatment. Recently, Vargatef (nintedanib, developed by Boehringer Ingelheim) was approved in the EU based on the results of a phase III study comparing Vargatef plus docetaxel to placebo plus docetaxel in patients with locally advanced/metastatic non-small-cell lung carcinoma (NSCLC) after first-line therapy in over 1,300 patients in 27 countries. Vargatef is an oral triple angiokinase inhibitor that simultaneously inhibits the VEGFR, PDGFR, and FGFR signaling pathways. The results indicated that treatment with Vargatef and docetaxel significantly extended the median overall survival from 10.3 to 12.6 months for patients with adenocarcinoma compared to placebo and docetaxel, with a quarter of patients surviving for two years or more with minimum side effects. Several clinical trials are ongoing currently with compounds targeted for FGF2; a phase III study was designed to compare the safety and efficacy of a multi-tyrosine kinase inhibitor, masitinib, in combination with bortezomib and dexamethasone to placebo in combination with bortezomib and dexamethasone in patients with relapsing multiple myeloma. Masitinib is an orally active and bioavailable compound that is a weak inhibitor of FGFR3.

31More recently, second-generation inhibitors targeting FGFRs with high selectivity have been developed (Table 5, Figure 4). For example, Debio 1347, developed by Debiopharm Group, a Swiss-based global biopharmaceutical company, is an orally bioavailable inhibitor of FGFRs 1-3 that inhibits FGFR-mediated signal transduction pathways and consequently tumor cell proliferation and angiogenesis. Debio 1347 will be used for personalized cancer treatment through the development of a companion diagnostic. It is currently being evaluated in Europe and the USA in a phase I trial to evaluate its safety and tolerability in patients with advanced solid tumors displaying alterations in FGFRs 1, 2, or 3 genes (Tables 5 and 6). Similarly, AZD4547, developed by AstraZeneca, is an orally tolerated inhibitor of FGFRs 1-3. AZD4547 inhibits FGFR kinase activity and tumor growth in vitro and in vivo. This compound is currently being tested for safety and efficacy in different clinical trials against advanced tumors (Table 6). Other small molecule FGFR inhibitors, such as BGJ398, JNJ-42756493, ARQ 087, LY2874455, and TAS-120, are currently under clinical investigation for advanced, relapsed or refractory tumors and most of these trials are still recruiting patients (Tables 5 and 6). Other selective small molecule tyrosine kinase inhibitors, such as PD 161570, PD 173074, PD 166285 dihydrochloride, PD 166866, FIIN hydrochloride, SU 5402, and SSR128129E are currently being tested for their antitumor activity on cell lines and in vivo preclinical models (Table 5). Monoclonal antibodies specifically targeting particular FGFR isoforms are also being developed. MFGR1877S (developed by Genentech) is a human anti-FGFR3 monoclonal antibody that inhibits tumor progression of bladder carcinoma and multiple myeloma xenografts in mice by antagonizing FGFR3 signaling. A phase I clinical trial was conducted to evaluate the response to MFGR1877S in patients with relapsed or refractory multiple myeloma (Tables 5 and 6). Similarly, BAY 1179470 (developed by Bayer) is a human anti-FGFR2 monoclonal antibody. BAY 1179470 showed antitumor activity in gastric cancer xenograft models with high FGFR2 expression. The anti-FGFR2 antibody BAY 1179470 is currently in Phase I testing in subjects with advanced, refractory solid tumors (Tables 5 and 6)

CONCLUSIONS

32FGF2 is frequently dysregulated in cancer, especially in advanced stages of disease. The upregulation of FGF2 or FGFRs can promote resistance to chemotherapy. FGF2 is currently being evaluated in clinical studies as a potential predictive biomarker for hematological and solid tumors. In addition, FGF2/FGFR inhibitors are being developed and evaluated as monotherapy or as part of a combination therapy for the treatment of different types of cancer. Identifying patients with advanced, relapsed or refractory cancers that would benefit from FGF2/FGFR signaling inhibition will allow for better treatment options of those patients in the era of personalized medicine.

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Not in our library10.1091/mbc.12.2.449
12.
Eswarakumar V, Lax I, Schlessinger J. Cellular signaling by fibroblast growth factor receptors. Cytokine Growth Factor Rev. 2005;16:139-149.
Not in our library10.1016/j.cytogfr.2005.01.001
13.
Zhang X, Ibrahimi OA, Olsen SK, Umemori H, Mohammadi M, Ornitz DM. Receptor specificity of the fibroblast growth factor family. The complete mammalian FGF family. J Biol Chem. 2006;281:15694-15700.
Not in our library10.1074/jbc.m601252200
14.
Turner N, Grose R. Fibroblast growth factor signalling: from development to cancer. Nat Rev Cancer. 2010;10:116-129.
Not in our library10.1038/nrc2780
15.
Goetz R, Mohammadi M. Exploring mechanisms of FGF signalling through the lens of structural biology. Nat Rev Mol Cell Biol. 2013;14:166-180.
Not in our library10.1038/nrm3528
16.
Akl M, Nagpal P, Ayoub N, Prabhu S, Gliksman M, Tai B, Hatipoglu A, Goy A, Suh K. Molecular and clinical profiles of syndecan-1 in solid and hematological cancer for prognosis and precision medicine. Oncotarget. 2015;6:28693-715.
Not in our library10.18632/oncotarget.4981
17.
Ornitz D, Yayon A, Flanagan J, Svahn C, Levi E, Leder P. Heparin is required for cell-free binding of basic fibroblast growth factor to a soluble receptor and for mitogenesis in whole cells. Mol Cell Biol. 1992;12:240-247.
Not in our library10.1128/mcb.12.1.240-247.1992
18.
Lew ED, Furdui CM, Anderson KS, Schlessinger J. The precise sequence of FGF receptor autophosphorylation is kinetically driven and is disrupted by oncogenic mutations. Sci Signal. 2009;2:ra6.
Not in our library10.1126/scisignal.2000021
19.
Karajannis MA, Vincent L, Direnzo R, Shmelkov SV, Zhang F, Feldman EJ, Bohlen P, Zhu Z, Sun H, Kussie P, Rafii S. Activation of FGFR1beta signaling pathway promotes survival, migration and resistance to chemotherapy in acute myeloid leukemia cells. Leukemia. 2006;20:979-986.
Not in our library10.1038/sj.leu.2404203
20.
Presta M, Dell'Era P, Mitola S, Moroni E, Ronca R, Rusnati M. Fibroblast growth factor/fibroblast growth factor receptor system in angiogenesis. Cytokine Growth Factor Rev. 2005;16:159-178.
Not in our library10.1016/j.cytogfr.2005.01.004
21.
Eliceiri BP. Integrin and growth factor receptor crosstalk. Circ Res. 2001;89:1104-1110.
Not in our library10.1161/hh2401.101084
22.
Ahmad I, Iwata T, Leung HY. Mechanisms of FGFR-mediated carcinogenesis. Biochim Biophys Acta. 2012;4:850-860.
Not in our library10.1016/j.bbamcr.2012.01.004
23.
Behbod F, Xian W, Shaw CA, Hilsenbeck SG, Tsimelzon A, Rosen JM. Transcriptional profiling of mammary gland side population cells. Stem Cells. 2006;24:1065-1074.
Not in our library10.1634/stemcells.2005-0375
24.
Jang JH, Shin KH, Park JG. Mutations in fibroblast growth factor receptor 2 and fibroblast growth factor receptor 3 genes associated with human gastric and colorectal cancers. Cancer Res. 2001;61:3541-3543.
Not in our library
25.
Cha JY, Maddileti S, Mitin N, Harden TK, Der CJ. Aberrant receptor internalization and enhanced FRS2-dependent signaling contribute to the transforming activity of the fibroblast growth factor receptor 2 IIIb C3 isoform. J Biol Chem. 2009;284:6227-6240.
Not in our library10.1074/jbc.m803998200
26.
Taylor JGt, Cheuk AT, Tsang PS, Chung JY, Song YK, Desai K, Yu Y, Chen QR, Shah K, Youngblood V, Fang J, Kim SY, Yeung C, Helman LJ, Mendoza A, Ngo V, et al. Identification of FGFR4-activating mutations in human rhabdomyosarcomas that promote metastasis in xenotransplanted models. J Clin Invest. 2009;119:3395-3407.
Not in our library10.1172/jci39703
27.
Thussbas C, Nahrig J, Streit S, Bange J, Kriner M, Kates R, Ulm K, Kiechle M, Hoefler H, Ullrich A, Harbeck N. FGFR4 Arg388 allele is associated with resistance to adjuvant therapy in primary breast cancer. J Clin Oncol. 2006;24:3747-3755.
Not in our library10.1200/jco.2005.04.8587
28.
Savagner P, Valles AM, Jouanneau J, Yamada KM, Thiery JP. Alternative splicing in fibroblast growth factor receptor 2 is associated with induced epithelial-mesenchymal transition in rat bladder carcinoma cells. Mol Biol Cell. 1994;5:851-862.
Not in our library10.1091/mbc.5.8.851
29.
Chaffer CL, Brennan JP, Slavin JL, Blick T, Thompson EW, Williams ED. Mesenchymal-to-epithelial transition facilitates bladder cancer metastasis: role of fibroblast growth factor receptor-2. Cancer Res. 2006;66:11271-11278.
Not in our library10.1158/0008-5472.can-06-2044
30.
Matsubara A, Kan M, Feng S, McKeehan WL. Inhibition of growth of malignant rat prostate tumor cells by restoration of fibroblast growth factor receptor 2. Cancer Res. 1998;58:1509-1514.
Not in our library
31.
Kornmann M, Ishiwata T, Matsuda K, Lopez ME, Fukahi K, Asano G, Beger HG, Korc M. IIIc isoform of fibroblast growth factor receptor 1 is overexpressed in human pancreatic cancer and enhances tumorigenicity of hamster ductal cells. Gastroenterology. 2002;123:301-313.
Not in our library10.1053/gast.2002.34174
32.
Gualandris A, Rusnati M, Belleri M, Nelli EE, Bastaki M, Molinari-Tosatti MP, Bonardi F, Parolini S, Albini A, Morbidelli L, Ziche M, Corallini A, Possati L, Vacca A, Ribatti D, Presta M. Basic fibroblast growth factor overexpression in endothelial cells: an autocrine mechanism for angiogenesis and angioproliferative diseases. Cell Growth Differ. 1996;7:147-160.
Not in our library
33.
Javerzat S, Auguste P, Bikfalvi A. The role of fibroblast growth factors in vascular development. Trends Mol Med. 2002;8:483-489.
Not in our library10.1016/s1471-4914(02)02394-8
34.
Dell'Era P, Belleri M, Stabile H, Massardi ML, Ribatti D, Presta M. Paracrine and autocrine effects of fibroblast growth factor-4 in endothelial cells. Oncogene. 2001;20:2655-2663.
Not in our library10.1038/sj.onc.1204368
35.
Presta M, Tiberio L, Rusnati M, Dell'Era P, Ragnotti G. Basic fibroblast growth factor requires a long-lasting activation of protein kinase C to induce cell proliferation in transformed fetal bovine aortic endothelial cells. Cell Regul. 1991;2:719-726.
Not in our library10.1091/mbc.2.9.719
36.
Dell'Era P, Mohammadi M, Presta M. Different tyrosine autophosphorylation requirements in fibroblast growth factor receptor-1 mediate urokinase-type plasminogen activator induction and mitogenesis. Mol Biol Cell. 1999;10:23-33.
Not in our library10.1091/mbc.10.1.23
37.
Tanghetti E, Ria R, Dell'Era P, Urbinati C, Rusnati M, Ennas MG, Presta M. Biological activity of substrate-bound basic fibroblast growth factor (FGF2): recruitment of FGF receptor-1 in endothelial cell adhesion contacts. Oncogene. 2002;21:3889-3897.
Not in our library10.1038/sj.onc.1205407
38.
Casanovas O, Hicklin DJ, Bergers G, Hanahan D. Drug resistance by evasion of antiangiogenic targeting of VEGF signaling in late-stage pancreatic islet tumors. Cancer Cell. 2005;8:299-309.
Not in our library10.1016/j.ccr.2005.09.005
39.
Dell'Era P, Coco L, Ronca R, Sennino B, Presta M. Gene expression profile in fibroblast growth factor 2-transformed endothelial cells. Oncogene. 2002;21:2433-2440.
Not in our library10.1038/sj.onc.1205301
40.
Hoying JB, Williams SK. Effects of basic fibroblast growth factor on human microvessel endothelial cell migration on collagen I correlates inversely with adhesion and is cell density dependent. J Cell Physiol. 1996;168:294-304.
Not in our library10.1002/(sici)1097-4652(199608)168:2<294::aid-jcp8>3.0.co;2-k
41.
Kuwahara K, Sasaki T, Kuwada Y, Murakami M, Yamasaki S, Chayama K. Expressions of angiogenic factors in pancreatic ductal carcinoma: a correlative study with clinicopathologic parameters and patient survival. Pancreas. 2003;26:344-349.
Not in our library10.1097/00006676-200305000-00006
42.
Garcia de la Torre N, Buley I, Wass JA, Jackson DG, Turner HE. Angiogenesis and lymphangiogenesis in parathyroid proliferative lesions. J Clin Endocrinol Metab. 2004;89:2890-2896.
Not in our library10.1210/jc.2003-031651
43.
Haugsten EM, Wiedlocha A, Olsnes S, Wesche J. Roles of fibroblast growth factor receptors in carcinogenesis. Mol Cancer Res. 2010;8:1439-1452.
Not in our library10.1158/1541-7786.mcr-10-0168
44.
Ribatti D, Vacca A, Rusnati M, Presta M. The discovery of basic fibroblast growth factor/fibroblast growth factor-2 and its role in haematological malignancies. Cytokine Growth Factor Rev. 2007;18(3-4):327-334.
Not in our library10.1016/j.cytogfr.2007.04.011
45.
Krejci P, Faitova J, Laurell H, Hampl A, Dvorak P. FGF-2 expression and its action in human leukemia and lymphoma cell lines: Leukemia. 2003;17:818-20.
Not in our library10.1038/sj.leu.2402861
46.
Elenbaas B, Weinberg RA. Heterotypic signaling between epithelial tumor cells and fibroblasts in carcinoma formation. Exp Cell Res. 2001;264:169-184.
Not in our library10.1006/excr.2000.5133
47.
Su G, Sung KE, Beebe DJ, Friedl A. Functional screen of paracrine signals in breast carcinoma fibroblasts. PLoS One. 2012;7:8.
Not in our library10.1371/journal.pone.0046685
48.
Gleave M, Hsieh JT, Gao CA, von Eschenbach AC, Chung LW. Acceleration of human prostate cancer growth in vivo by factors produced by prostate and bone fibroblasts. Cancer Res. 1991;51:3753-3761.
Not in our library
49.
Choi TH, Tseng SC. In vivo and in vitro demonstration of epithelial cell-induced myofibroblast differentiation of keratocytes and an inhibitory effect by amniotic membrane. Cornea. 2001;20:197-204.
Not in our library10.1097/00003226-200103000-00019
50.
Rodemann HP, Muller GA. Characterization of human renal fibroblasts in health and disease: II. In vitro growth, differentiation, and collagen synthesis of fibroblasts from kidneys with interstitial fibrosis. Am J Kidney Dis. 1991;17:684-686.
Not in our library10.1016/s0272-6386(12)80352-0
51.
Kashiwakura I, Takahashi TA. Basic fibroblast growth factorstimulated ex vivo expansion of haematopoietic progenitor cells from human placental and umbilical cord blood. British journal of haematology. 2003;122:479-488.
Not in our library10.1046/j.1365-2141.2003.04444.x
52.
Pearson S, Sroczynska P, Lacaud G, Kouskoff V. The stepwise specification of embryonic stem cells to hematopoietic fate is driven by sequential exposure to Bmp4, activin A, bFGF and VEGF. Development. 2008;135:1525-1535.
Not in our library10.1242/dev.011767
53.
A Complex Role for FGF-2 in Self-Renewal, Survival, and Adhesion of Human Embryonic Stem Cells · 2009
No notice
54.
Yoon S-Y, Tefferi A, Li C-Y. Bone marrow stromal cell distribution of basic fibroblast growth factor in chronic myeloid disorders. Haematologica. 2001;86:52-57.
Not in our library
55.
Berardi AC, Wang A, Abraham J, Scadden DT. Basic fibroblast growth factor mediates its effects on committed myeloid progenitors by direct action and has no effect on hematopoietic stem cells. Blood. 1995;86:2123-2129.
Not in our library
56.
Gabrilove J, Wong G, Bollenbacher E, White K, Kojima S, Wilson E. Basic fibroblast growth factor counteracts the suppressive effect of. Blood. 1993;81(4).
Not in our library
57.
Koritschoner NP, Bartunek P, Knespel S, Blendinger G, Zenke M. The fibroblast growth factor receptor FGFR-4 acts as a ligand dependent modulator of erythroid cell proliferation. Oncogene. 1999;18:5904-5914.
Not in our library10.1038/sj.onc.1202979
58.
Wilson EL, Rifkin DB, Kelly F, Hannocks M-J, Gabrilove JL. Basic fibroblast growth factor stimulates myelopoiesis in long-term human bone marrow cultures. Blood. 1991;77:954-960.
Not in our library
59.
Moroni E, Dell'Era P, Rusnati M, Presta M. Fibroblast growth factors and their receptors in hematopoiesis and hematological tumors. J Hematother Stem Cell Res. 2002;11:19-32.
Not in our library10.1089/152581602753448513
60.
Fhu CW, Graham AM, Yap CT, Al-Salam S, Castella A, Chong SM, Lim YC. Reed-Sternberg cell-derived lymphotoxin-alpha activates endothelial cells to enhance T-cell recruitment in classical Hodgkin lymphoma. Blood. 2014;124:2973-2982.
Not in our library10.1182/blood-2014-05-576140
61.
Witzig TE, Kimlinger T, Stenson M, Therneau T. Syndecan-1 expression on malignant cells from the blood and marrow of patients with plasma cell proliferative disorders and B-cell chronic lymphocytic leukemia. Leuk Lymphoma. 1998;31(1-2):167-175.
Not in our library10.3109/10428199809057596
62.
Gharbaran R, Goy A, Tanaka T, Park J, Kim C, Hasan N, Vemulapalli S, Sarojini S, Tuluc M, Nalley K, Bhattacharyya P, Pecora A, Suh KS. Fibroblast growth factor-2 (FGF2) and syndecan-1 (SDC1) are potential biomarkers for putative circulating CD15+/CD30+ cells in poor outcome Hodgkin lymphoma patients. Journal of hematology & oncology. 2013;6:1756-8722.
Not in our library10.1186/1756-8722-6-62
63.
Panta GR, Kaur S, Cavin LG, Cortes ML, Mercurio F, Lothstein L, Sweatman TW, Israel M, Arsura M. ATM and the catalytic subunit of DNA-dependent protein kinase activate NF-kappaB through a common MEK/extracellular signal-regulated kinase/p90(rsk) signaling pathway in response to distinct forms of DNA damage. Mol Cell Biol. 2004;24:1823-1835.
Not in our library10.1128/mcb.24.5.1823-1835.2004
64.
Rocha S, Martin AM, Meek DW, Perkins ND. p53 represses cyclin D1 transcription through down regulation of Bcl-3 and inducing increased association of the p52 NF-kappaB subunit with histone deacetylase 1. Mol Cell Biol. 2003;23:4713-4727.
Not in our library10.1128/mcb.23.13.4713-4727.2003
65.
Küppers R. The biology of Hodgkin's lymphoma. Nat Rev Cancer. 2009;9:15-27.
Not in our library10.1038/nrc2542
66.
Wakisaka N, Murono S, Yoshizaki T, Furukawa M, Pagano JS. Epstein-Barr virus latent membrane protein 1 induces and causes release of fibroblast growth factor-2. Cancer research. 2002;62:6337-6344.
Not in our library
67.
Lee JG, Kay EP. NF-B is the transcription factor for FGF-2 that causes endothelial mesenchymal transformation in cornea. Invest Ophthalmol Vis Sci. 2012;53:1530-1538.
Not in our library10.1167/iovs.11-9102
68.
Hardin J, MacLeod S, Grigorieva I, Chang R, Barlogie B, Xiao H, Epstein J. Interleukin-6 prevents dexamethasone-induced myeloma cell death. Blood. 1994;84:3063-3070.
Not in our library
69.
Lichtenstein A, Tu Y, Fady C, Vescio R, Berenson J. Interleukin-6 inhibits apoptosis of malignant plasma cells. Cell Immunol. 1995;162:248-255.
Not in our library10.1006/cimm.1995.1076
70.
Bisping G, Leo R, Wenning D, Dankbar B, Padró T, Kropff M, Scheffold C, Kröger M, Mesters RM, Berdel WE. Paracrine interactions of basic fibroblast growth factor and interleukin-6 in multiple myeloma. Blood. 2003;101:2775-2783.
Not in our library10.1182/blood-2002-09-2907
71.
Ishikawa H, Tsuyama N, Liu S, Abroun S, Li F-J, Otsuyama K-i, Zheng X, Ma Z, Maki Y, Iqbal MS. Accelerated proliferation of myeloma cells by interleukin-6 cooperating with fibroblast growth factor receptor 3-mediated signals. Oncogene. 2005;24:6328-6332.
Not in our library10.1038/sj.onc.1208782
72.
Reynolds GM, Billingham LJ, Gray LJ, Flavell JR, Najafipour S, Crocker J, Nelson P, Young LS, Murray PG. Interleukin 6 expression by Hodgkin/Reed-Sternberg cells is associated with the presence of ‘B'symptoms and failure to achieve complete remission in patients with advanced Hodgkin's disease. Br J Haematol. 2002;118:195-201.
Not in our library10.1046/j.1365-2141.2002.03575.x
73.
Khnykin D, Troen G, Berner JM, Delabie J. The expression of fibroblast growth factors and their receptors in Hodgkin's lymphoma. J Pathol. 2006;208:431-438.
Not in our library10.1002/path.1900
74.
Kurzrock R, Redman J, Cabanillas F, Jones D, Rothberg J, Talpaz M. Serum interleukin 6 levels are elevated in lymphoma patients and correlate with survival in advanced Hodgkin's disease and with B symptoms. Cancer research. 1993;53:2118-2122.
Not in our library
75.
Delrieu I, Arnaud E, Ferjoux G, Bayard F, Faye JC. Overexpression of the FGF-2 24-kDa isoform up-regulates IL-6 transcription in NIH-3T3 cells. FEBS letters. 1998;436:17-22.
Not in our library10.1016/s0014-5793(98)01086-2
76.
McCubrey J, Abrams S, Ligresti G, Misaghian N, Wong E, Steelman L, Bäsecke J, Troppmair J, Libra M, Nicoletti F. Involvement of p53 and Raf/MEK/ERK pathways in hematopoietic drug resistance. Leukemia. 2008;22:2080-2090.
Not in our library10.1038/leu.2008.207
77.
Zheng B, Fiumara P, Li YV, Georgakis G, Snell V, Younes M, Vauthey JN, Carbone A, Younes A. MEK/ERK pathway is aberrantly active in Hodgkin disease: a signaling pathway shared by CD30, CD40, and RANK that regulates cell proliferation and survival. Blood. 2003;102:1019-1027.
Not in our library10.1182/blood-2002-11-3507
78.
Pardo OE, Arcaro A, Salerno G, Raguz S, Downward J, Seckl MJ. Fibroblast growth factor-2 induces translational regulation of Bcl-XL and Bcl-2 via a MEK-dependent pathway: correlation with resistance to etoposide-induced apoptosis. J Biol Chem. 2002;277:12040-12046.
Not in our library10.1074/jbc.m109006200
79.
Alavi AS, Acevedo L, Min W, Cheresh DA. Chemoresistance of endothelial cells induced by basic fibroblast growth factor depends on Raf-1-mediated inhibition of the proapoptotic kinase, ASK1. Cancer Res. 2007;67:2766-2772.
Not in our library10.1158/0008-5472.can-06-3648
80.
Joos S, Küpper M, Ohl S, von Bonin F, Mechtersheimer G, Bentz M, Marynen P, Möller P, Pfreundschuh M, Trümper L. Genomic imbalances including amplification of the tyrosine kinase gene JAK2 in CD30+ Hodgkin cells. Cancer Res. 2000;60:549-552.
Not in our library
81.
Carmo CR, Lyons-Lewis J, Seckl MJ, Costa-Pereira AP. A novel requirement for Janus kinases as mediators of drug resistance induced by fibroblast growth factor-2 in human cancer cells. PloS one. 2011;6:e19861.
Not in our library10.1371/journal.pone.0019861
82.
Lestaurtinib inhibition of the Jak/STAT signaling pathway in hodgkin lymphoma inhibits proliferation and induces apoptosis. · 2011
Not checked
83.
Functions of Paracrine PDGF Signaling in the Proangiogenic Tumor Stroma Revealed by Pharmacological Targeting · 2008
No notice
84.
Tanase C, Codrici E, Popescu ID, Cruceru ML, Enciu A-M, Albulescu R, Ciubotaru V, Arsene D. Angiogenic markers: molecular targets for personalized medicine in pituitary adenoma. Personalized Med. 2013;10:539-548.
Not in our library10.2217/pme.13.61
85.
Lieu C, Heymach J, Overman M, Tran H, Kopetz S. Beyond VEGF: inhibition of the fibroblast growth factor pathway and antiangiogenesis. Clin Cancer Res. 2011;17:6130-6139.
Not in our library10.1158/1078-0432.ccr-11-0659
86.
Harding TC, Long L, Palencia S, Zhang H, Sadra A, Hestir K, Patil N, Levin A, Hsu AW, Charych D, Brennan T, Zanghi J, Halenbeck R, Marshall SA, Qin M, Doberstein SK, et al. Blockade of nonhormonal fibroblast growth factors by FP-1039 inhibits growth of multiple types of cancer. Sci Transl Med. 2013;5:3005414.
Not in our library10.1126/scitranslmed.3005414
87.
Go RS, Lee SJ, Shin D, Callister SM, Jobe DA, Conry RM, Tarhini AA, Kirkwood JM. ECOG phase II trial of graded-dose peginterferon alpha-2b in patients with metastatic melanoma overexpressing basic fibroblast growth factor (E2602). Clin Cancer Res. 2013;19:6597-6604.
Not in our library10.1158/1078-0432.ccr-13-1414
88.
Jain VK, Turner NC. Challenges and opportunities in the targeting of fibroblast growth factor receptors in breast cancer. Breast Cancer Res. 2012;14:208.
Not in our library10.1186/bcr3139
89.
O'Hare T, Shakespeare WC, Zhu X, Eide CA, Rivera VM, Wang F, Adrian LT, Zhou T, Huang WS, Xu Q, Metcalf CA, Tyner JW, Loriaux MM, Corbin AS, Wardwell S, Ning Y, et al. AP24534, a pan-BCR-ABL inhibitor for chronic myeloid leukemia, potently inhibits the T315I mutant and overcomes mutation-based resistance. Cancer Cell. 2009;16:401-412.
Not in our library10.1016/j.ccr.2009.09.028
90.
Zivi A, Cerbone L, Recine F, Sternberg CN. Safety and tolerability of pazopanib in the treatment of renal cell carcinoma. Expert Opin Drug Saf. 2012;11:851-859.
Not in our library10.1517/14740338.2012.712108
91.
Kumar SK, Mikhael JR, Buadi FK, Dingli D, Dispenzieri A, Fonseca R, Gertz MA, Greipp PR, Hayman SR, Kyle RA. Management of newly diagnosed symptomatic multiple myeloma: updated Mayo Stratification of Myeloma and Risk-Adapted Therapy (mSMART) consensus guidelines. Mayo Clin Proc: Elsevier). 2009;1095-1110.
Not in our library10.4065/mcp.2009.0603
92.
Lee SH, de Menezes DL, Vora J, Harris A, Ye H, Nordahl L, Garrett E, Samara E, Aukerman SL, Gelb AB. In vivo target modulation and biological activity of CHIR-258, a multitargeted growth factor receptor kinase inhibitor, in colon cancer models. Clin Cancer Res. 2005;11:3633-3641.
Not in our library10.1158/1078-0432.ccr-04-2129
93.
Moreau P, Facon T, Leleu X, Morineau N, Huyghe P, Harousseau J-L, Bataille R, Avet-Loiseau H. Recurrent 14q32 translocations determine the prognosis of multiple myeloma, especially in patients receiving intensive chemotherapy. Blood. 2002;100:1579-1583.
Not in our library10.1182/blood-2002-03-0749
94.
Kalff A, Spencer A. The t (4; 14) translocation and FGFR3 overexpression in multiple myeloma: prognostic implications and current clinical strategies. Blood cancer journal. 2012;2:e89.
Not in our library10.1038/bcj.2012.37
95.
Reck M, Kaiser R, Mellemgaard A, Douillard JY, Orlov S, Krzakowski M, von Pawel J, Gottfried M, Bondarenko I, Liao M, Gann CN, Barrueco J, Gaschler-Markefski B, Novello S. Docetaxel plus nintedanib versus docetaxel plus placebo in patients with previously treated non-small-cell lung cancer (LUME-Lung 1): a phase 3, double-blind, randomised controlled trial. Lancet Oncol. 2014;15:143-155.
Not in our library10.1016/s1470-2045(13)70586-2
96.
Masitinib (AB1010), a Potent and Selective Tyrosine Kinase Inhibitor Targeting KIT · 2009
No notice
97.
Nakanishi Y, Akiyama N, Tsukaguchi T, Fujii T, Sakata K, Sase H, Isobe T, Morikami K, Shindoh H, Mio T. The fibroblast growth factor receptor genetic status as a potential predictor of the sensitivity to CH5183284/Debio 1347, a novel selective FGFR inhibitor. Mol Cancer Ther. 2014;13:2547-2558.
Not in our library10.1158/1535-7163.mct-14-0248
98.
Gavine PR, Mooney L, Kilgour E, Thomas AP, Al-Kadhimi K, Beck S, Rooney C, Coleman T, Baker D, Mellor MJ, Brooks AN, Klinowska T. AZD4547: an orally bioavailable, potent, and selective inhibitor of the fibroblast growth factor receptor tyrosine kinase family. Cancer Res. 2012;72:2045-2056.
Not in our library10.1158/0008-5472.can-11-3034
99.
Qing J, Du X, Chen Y, Chan P, Li H, Wu P, Marsters S, Stawicki S, Tien J, Totpal K. Antibody-based targeting of FGFR3 in bladder carcinoma and t (4; 14)-positive multiple myeloma in mice. The Journal of clinical investigation. 2009;119:1216.
Not in our library10.1172/jci38017
100.
Schatz CA, Kopitz C, Wittemer-Rump S, Sommer A, Lindbom L, Osada M, Yamanouchi H, Huynh H, Krahn T, Asadullah K. Pharmacodynamic and stratification biomarker for the anti-FGFR2 antibody (BAY1179470) and the FGFR2-ADC. Cancer Res. 2014;74(19 Supplement):4766-4766.
Not in our library
101.
Ornitz DM, Itoh N. Fibroblast growth factors. Genome Biol. 2001;2:1-12.
Not in our library10.1186/gb-2001-2-3-reviews3005
102.
Horowitz A, Tkachenko E, Simons M. Fibroblast growth factor-specific modulation of cellular response by syndecan-4. J Cell Biol. 2002;157:715-725.
Not in our library10.1083/jcb.200112145
103.
Rusnati M, Urbinati C, Presta M. Internalization of basic fibroblast growth factor (bFGF) in cultured endothelial cells: Role of the low affinity heparinlike bFGF receptors. J Cell Physiol. 1993;154:152-161.
Not in our library10.1002/jcp.1041540119
104.
Rusnati M, Presta M. Interaction of angiogenic basic fibroblast growth factor with endothelial cell heparan sulfate proteoglycans. Int J Clin Lab Res. 1996;26:15-23.
Not in our library10.1007/bf02644769
105.
Rusnati M, Tanghetti E, Dell'Era P, Gualandris A, Presta M. v3 integrin mediates the cell-adhesive capacity and biological activity of basic fibroblast growth factor (FGF-2) in cultured endothelial cells. Mol Biol Cell. 1997;8:2449-2461.
Not in our library10.1091/mbc.8.12.2449
106.
Rusnati M, Urbinati C, Tanghetti E, Dell'Era P, Lortat-Jacob H, Presta M. Cell membrane GM1 ganglioside is a functional coreceptor for fibroblast growth factor 2. Proc Natl Acad Sci U S A. 2002;99:4367-4372.
Not in our library10.1073/pnas.072651899
107.
Hanneken A, Maher PA, Baird A. High affinity immunoreactive FGF receptors in the extracellular matrix of vascular endothelial cells—implications for the modulation of FGF-2. J Cell Biol. 1995;128:1221-1228.
Not in our library10.1083/jcb.128.6.1221
108.
Bergonzoni L, Caccia P, Cletni O, Sarmientos P, Isacchi A. Characterization of a biologically active extracellular domain of fibroblast growth factor receptor 1 expressed in Escherichia coli. Eur J Biochem. 1992;210:823-829.
Not in our library10.1111/j.1432-1033.1992.tb17485.x
109.
Naumnik W, Ossolinska M, Plonska I, Chyczewska E, Niklinski J. Circulating Thrombospondin-2 and FGF-2 in Patients with Advanced Non-small Cell Lung Cancer: Correlation with Survival. Adv Exp Med Biol. 2015;833:9-14.
Not in our library10.1007/5584_2014_78
110.
Margosio B, Marchetti D, Vergani V, Giavazzi R, Rusnati M, Presta M, Taraboletti G. Thrombospondin 1 as a scavenger for matrix-associated fibroblast growth factor 2. Blood. 2003;102:4399-4406.
Not in our library10.1182/blood-2003-03-0893
111.
Rusnati M, Camozzi M, Moroni E, Bottazzi B, Peri G, Indraccolo S, Amadori A, Mantovani A, Presta M. Selective recognition of fibroblast growth factor-2 by the long pentraxin PTX3 inhibits angiogenesis. Blood. 2004;104:92-99.
Not in our library10.1182/blood-2003-10-3433
112.
Sahni A, Baker CA, Sporn LA, Francis CW. Fibrinogen and fibrin protect fibroblast growth factor-2 from proteolytic degradation. Thromb Haemost. 2000;83:736-741.
Not in our library
113.
Sahni A, Francis CW. Plasmic degradation modulates activity of fibrinogen-bound fibroblast growth factor-2. J Thromb Haemost. 2003;1:1271-1277.
Not in our library10.1046/j.1538-7836.2003.00228.x
114.
Sauer H, Ravindran F, Beldoch M, Sharifpanah F, Jedelska J, Strehlow B, Wartenberg M. alpha2-Macroglobulin enhances vasculogenesis/angiogenesis of mouse embryonic stem cells by stimulation of nitric oxide generation and induction of fibroblast growth factor-2 expression. Stem Cells Dev. 2013;22:1443-1454.
Not in our library10.1089/scd.2012.0640
115.
Nissen LJ, Cao R, Hedlund EM, Wang Z, Zhao X, Wetterskog D, Funa K, Brakenhielm E, Cao Y. Angiogenic factors FGF2 and PDGF-BB synergistically promote murine tumor neovascularization and metastasis. J Clin Invest. 2007;117:2766-2777.
Not in our library10.1172/jci32479
116.
Sulpice E, Bryckaert M, Lacour J, Contreres JO, Tobelem G. Platelet factor 4 inhibits FGF2-induced endothelial cell proliferation via the extracellular signal-regulated kinase pathway but not by the phosphatidylinositol 3-kinase pathway. Blood. 2002;100:3087-3094.
Not in our library10.1182/blood.v100.9.3087
117.
Perollet C, Han ZC, Savona C, Caen JP, Bikfalvi A. Platelet factor 4 modulates fibroblast growth factor 2 (FGF-2) activity and inhibits FGF-2 dimerization. Blood. 1998;91:3289-3299.
Not in our library
118.
Mignatti P, Mazzieri R, Rifkin DB. Expression of the urokinase receptor in vascular endothelial cells is stimulated by basic fibroblast growth factor. J Cell Biol. 1991;113:1193-1201.
Not in our library10.1083/jcb.113.5.1193
119.
Spinetti G, Camarda G, Bernardini G, Romano Di Peppe S, Capogrossi MC, 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
120.
Andoh A, Bamba S, Fujino S, Inatomi O, Zhang Z, Kim S, Takayanagi A, Shimizu N, Fujiyama Y. Fibroblast growth factor-2 stimulates interleukin-6 secretion in human pancreatic periacinar myofibroblasts. Pancreas. 2004;29:278-283.
Not in our library10.1097/00006676-200411000-00006
121.
Delrieu I, Arnaud E, Ferjoux G, Bayard F, Faye JC. Overexpression of the FGF-2 24-kDa isoform up-regulates IL-6 transcription in NIH-3T3 cells. FEBS Lett. 1998;436:17-22.
Not in our library10.1016/s0014-5793(98)01086-2
122.
Jee SH, Chu CY, Chiu HC, Huang YL, Tsai WL, Liao YH, Kuo ML. Interleukin-6 induced basic fibroblast growth factor-dependent angiogenesis in basal cell carcinoma cell line via JAK/STAT3 and PI3-kinase/Akt pathways. J Invest Dermatol. 2004;123:1169-1175.
Not in our library10.1111/j.0022-202x.2004.23497.x
123.
Lau M-T, So W-K, Leung PC. Fibroblast growth factor 2 induces E-cadherin down-regulation via PI3K/Akt/mTOR and MAPK/ERK signaling in ovarian cancer cells. PLoS One. 2013;8:e59083.
Not in our library10.1371/journal.pone.0059083
124.
Maloof P, Wang Q, Wang H, Stein D, Denny TN, Yahalom J, Fenig E, Wieder R. Overexpression of basic fibroblast growth factor (FGF-2) downregulates Bcl-2 and promotes apoptosis in MCF-7 human breast cancer cells. Breast Cancer Res Treat. 1999;56:151-165.
Not in our library10.1023/a:1006258510381
125.
Cao X-C, Zhang W-R, Cao W-F, Liu B-W, Zhang F, Zhao H-M, Meng R, Zhang L, Niu R-F, Hao X-S. Aquaporin3 is required for FGF-2-induced migration of human breast cancers. PLoS One. 2013;8:e56735.
Not in our library10.1371/journal.pone.0056735
126.
Bossard C, Laurell H, Van den Berghe L, Meunier S, Zanibellato C, Prats H. Translokin is an intracellular mediator of FGF-2 trafficking. Nat Cell Biol. 2003;5:433-439.
Not in our library10.1038/ncb979
127.
Yu P-J, Ferrari G, Pirelli L, Galloway AC, Mignatti P, Pintucci G. Thrombin cleaves the high molecular weight forms of basic fibroblast growth factor (FGF-2): a novel mechanism for the control of FGF-2 and thrombin activity. Oncogene. 2008;27:2594-2601.
Not in our library10.1038/sj.onc.1210899
128.
Tassi E, Al-Attar A, Aigner A, Swift MR, McDonnell K, Karavanov A, Wellstein A. Enhancement of fibroblast growth factor (FGF) activity by an FGF-binding protein. J Biol Chem. 2001;276:40247-40253.
Not in our library10.1074/jbc.m104933200
129.
Gazzaniga P, Gandini O, Gradilone A, Silvestri I, Giuliani L, Magnanti M, Gallucci M, Saccani G, Frati L, Agliano A. Detection of basic fibroblast growth factor mRNA in urinary bladder cancer: correlation with local relapses. Int J Oncol. 1999;14:1123-1130.
Not in our library10.3892/ijo.14.6.1123
130.
Szatmari T, Mundt F, Heidari-Hamedani G, Zong F, Ferolla E, Alexeyenko A, Hjerpe A, Dobra K. Novel genes and pathways modulated by syndecan-1: implications for the proliferation and cell-cycle regulation of malignant mesothelioma cells. PLoS One. 2012;7:e48091.
Not in our library10.1371/journal.pone.0048091
131.
Relf M, LeJeune S, Scott PA, Fox S, Smith K, Leek R, Moghaddam A, Whitehouse R, Bicknell R, Harris AL. Expression of the angiogenic factors vascular endothelial cell growth factor, acidic and basic fibroblast growth factor, tumor growth factor −1, platelet-derived endothelial cell growth factor, placenta growth factor, and pleiotrophin in human primary breast cancer and its relation to angiogenesis. Cancer Res. 1997;57:963-969.
Not in our library
132.
Visscher D, DeMattia F, Ottosen S, Sarkar F, Crissman J. Biologic and clinical significance of basic fibroblast growth factor immunostaining in breast carcinoma. Mod Pathol. 1995;8:665-670.
Not in our library
133.
Granato AM, Nanni O, Falcini F, Folli S, Mosconi G, De Paola F, Medri L, Amadori D, Volpi A. Basic fibroblast growth factor and vascular endothelial growth factor serum levels in breast cancer patients and healthy women: useful as diagnostic tools. Breast Cancer Res. 2004;6:R38-45.
Not in our library10.1186/bcr745
134.
Faridi A, Rudlowski C, Biesterfeld S, Schuh S, Rath W, Schröder W. Long-term follow-up and prognostic significance of angiogenic basic fibroblast growth factor (bFGF) expression in patients with breast cancer. Pathol Res Pract. 2002;198:1-5.
Not in our library10.1078/0344-0338-00176
135.
Smith K, Fox S, Whitehouse R, Taylor M, Greenall M, Clarke J, Harris A. Upregulation of basic fibroblast growth factor in breast carcinoma and its relationship to vascular density, oestrogen receptor, epidermal growth factor receptor and survival. Ann Oncol. 1999;10:707-713.
Not in our library10.1023/a:1008303614441
136.
Hsiung R, Zhu W, Klein G, Qin W, Rosenberg A, Park P, Rosato E, Sauter E. High basic fibroblast growth factor levels in nipple aspirate fluid are correlated with breast cancer. Cancer J. 2002;8:303-310.
Not in our library10.1097/00130404-200207000-00006
137.
Lee HJ, Seo AN, Park SY, Kim JY, Park JY, Yu JH, Ahn J-H, Gong G. Low Prognostic Implication of Fibroblast Growth Factor Family Activation in Triple-negative Breast Cancer Subsets. Ann Surg Oncol. 2014;21:1561-1568.
Not in our library10.1245/s10434-013-3456-x
138.
George M, Tutton M, Abulafi A, Eccles S, Swift R. Plasma basic fibroblast growth factor levels in colorectal cancer: a clinically useful assay? Clin Exp Metastasis. 2002;19:735-738.
Not in our library10.1023/a:1021322201816
139.
Xu C-J, Mikami T, Nakamura T, Tsuruta T, Nakada N, Yanagisawa N, Jiang S-X, Okayasu I. Tumor budding, myofibroblast proliferation, and fibrosis in obstructing colon carcinoma: The roles of Hsp47 and basic fibroblast growth factor. Pathol Res Pract. 2013;209:69-74.
Not in our library10.1016/j.prp.2012.10.008
140.
Dobrzycka B, Mackowiak-Matejczyk B, Kinalski M, Terlikowski SJ. Pretreatment serum levels of bFGF and VEGF and its clinical significance in endometrial carcinoma. Gynecol Oncol. 2013;128:454-460.
Not in our library10.1016/j.ygyno.2012.11.035
141.
Chen Y, Li X, Yang H, Xia Y, Guo L, Wu X, He C, Lu Y. Expression of basic fibroblast growth factor, CD31, and -smooth muscle actin and esophageal cancer recurrence after definitive chemoradiation. Tumour Biol. 2014;35:7275-7282.
Not in our library10.1007/s13277-014-1987-9
142.
Takahashi JA, Fukumoto M, Igarashi K, Oda Y, Kikuchi H, Hatanaka M. Correlation of basic fibroblast growth factor expression levels with the degree of malignancy and vascularity in human gliomas. J Neurosurg. 1992;76:792-798.
Not in our library10.3171/jns.1992.76.5.0792
143.
Bian X-W, Du L-L, Shi J-Q, Cheng Y-S, Liu F-X. Correlation of bFGF, FGFR-1 and VEGF expression with vascularity and malignancy of human astrocytomas. Anal Quant Cytol Histol. 2000;22:267-274.
Not in our library
144.
Dellacono FR, Spiro J, Eisma R, Kreutzer D. Expression of basic fibroblast growth factor and its receptors by head and neck squamous carcinoma tumor and vascular endothelial cells. Am J Surg. 1997;174:540-544.
Not in our library10.1016/s0002-9610(97)00169-4
145.
Poon RT-P, Ng IO-L, Lau C, Yu W-C, Fan S-T, Wong J. Correlation of serum basic fibroblast growth factor levels with clinicopathologic features and postoperative recurrence in hepatocellular carcinoma. Am J Surg. 2001;182:298-304.
Not in our library10.1016/s0002-9610(01)00708-5
146.
Kin M, Sata M, Ueno T, Torimura T, Inuzuka S, Tsuji R, Sujaku K, Sakamoto M, Sugawara H, Tamaki S. Basic fibroblast growth factor regulates proliferation and motility of human hepatoma cells by an autocrine mechanism. J Hepatol. 1997;27:677-687.
Not in our library10.1016/s0168-8278(97)80085-2
147.
Ueno K, Inoue Y, Kawaguchi T, Hosoe S, Kawahara M. Increased serum levels of basic fibroblast growth factor in lung cancer patients: relevance to response of therapy and prognosis. Lung Cancer. 2001;31:213-219.
Not in our library10.1016/s0169-5002(00)00187-2
148.
Ruotsalainen T, Joensuu H, Mattson K, Salven P. High pretreatment serum concentration of basic fibroblast growth factor is a predictor of poor prognosis in small cell lung cancer. Cancer Epidemiol Biomarkers Prev. 2002;11:1492-1495.
Not in our library
149.
Joensuu H, Anttonen A, Eriksson M, Mäkitaro R, Alfthan H, Kinnula V, Leppä S. Soluble syndecan-1 and serum basic fibroblast growth factor are new prognostic factors in lung cancer. Cancer Res. 2002;62:5210-5217.
Not in our library
150.
Naumnik W, Ossoliska M, Poska I, Chyczewska E, Nikliski J. Circulating Thrombospondin-2 and FGF-2 in Patients with Advanced Non-small Cell Lung Cancer: Correlation with Survival. Adv Exp Med Biol. 2015;833:9-14.
Not in our library10.1007/5584_2014_78
151.
Fiuraskova M, Brychtova S, Sedlakova E, Benes P, Zalesak B, Hlobilkova A, Tichy M, Kolar Z. Molecular changes in PDEGF and bFGF in malignant melanomas in relation to the stromal microenvironment. Anticancer Res. 2005;25(6B):4299-4303.
Not in our library
152.
Hase T, Kawashiri S, Tanaka A, Nozaki S, Noguchi N, Kato K, Nakaya H, Nakagawa K. Correlation of basic fibroblast growth factor expression with the invasion and the prognosis of oral squamous cell carcinoma. J Oral Pathol Med. 2006;35:136-139.
Not in our library10.1111/j.1600-0714.2006.00397.x
153.
Ren T, Qing Y, Dai N, Li M, Qian C, Yang Y, Cheng Y, Li Z, Zhang S, Zhong Z. Apurinic/apyrimidinic endonuclease 1 induced upregulation of fibroblast growth factor 2 and its receptor 3 induces angiogenesis in human osteosarcoma cells. Cancer Sci. 2014;105:186-194.
Not in our library10.1111/cas.12334
154.
Madsen CV, Steffensen KD, Olsen DA, Waldstrøm M, SØGAARD CH, Brandslund I, Jakobsen A. Serum platelet-derived growth factor and fibroblast growth factor in patients with benign and malignant ovarian tumors. Anticancer Res. 2012;32:3817-3825.
Not in our library
155.
Le Page C, Ouellet V, Madore J, Hudson TJ, Tonin PN, Provencher DM, MesMasson AM. From gene profiling to diagnostic markers: IL18 and FGF2 complement CA125 as serumbased markers in epithelial ovarian cancer. Int J Cancer. 2006;118:1750-1758.
Not in our library10.1002/ijc.21521
156.
Yamanaka Y, Friess H, Buchler M, Beger HG, Uchida E, Onda M, Kobrin MS, Korc M. Overexpression of acidic and basic fibroblast growth factors in human pancreatic cancer correlates with advanced tumor stage. Cancer Res. 1993;53:5289-5296.
Not in our library
157.
Nuclear translocation of FGFR1 and FGF2 in pancreatic stellate cells facilitates pancreatic cancer cell invasion · 2014
No notice
158.
Meyer GE, Yu E, Siegal JA, Petteway JC, Blumenstein BA, Brawer MK. Serum basic fibroblast growth factor in men with and without prostate carcinoma. Cancer. 1995;76:2304-2311.
Not in our library10.1002/1097-0142(19951201)76:11<2304::aid-cncr2820761119>3.0.co;2-n
159.
Cronauer MV, Hittmair A, Eder IE, Hobisch A, Culig Z, Ramoner R, Zhang J, Bartsch G, Reissigl A, Radmayr C. Basic fibroblast growth factor levels in cancer cells and in sera of patients suffering from proliferative disorders of the prostate. Prostate. 1997;31:223-233.
Not in our library10.1002/(sici)1097-0045(19970601)31:4<223::aid-pros3>3.0.co;2-l
160.
Giri D, Ropiquet F, Ittmann M. Alterations in expression of basic fibroblast growth factor (FGF) 2 and its receptor FGFR-1 in human prostate cancer. Clin Cancer Res. 1999;5:1063-1071.
Not in our library
161.
Rasmuson T, Grankvist K, Jacobsen J, Ljungberg B. Impact of serum basic fibroblast growth factor on prognosis in human renal cell carcinoma. Eur J Cancer. 2001;37:2199-2203.
Not in our library10.1016/s0959-8049(01)00290-8
162.
Aigner A, Brachmann P, Beyer J, Jäger R, Raulais D, Vigny M, Neubauer A, Heidenreich A, Weinknecht S, Czubayko F. Marked increase of the growth factors pleiotrophin and fibroblast growth factor-2 in serum of testicular cancer patients. Ann Oncol. 2003;14:1525-1529.
Not in our library10.1093/annonc/mdg416
163.
Pasieka Z, Stpie H, Komorowski J, Koomecki K, Kuzdak K. Evaluation of the levels of bFGF, VEGF, sICAM-1, and sVCAM-1 in serum of patients with thyroid cancer. Recent Results Cancer Res. 2003;162:189-194.
Not in our library10.1007/978-3-642-59349-9_18
164.
Aguayo A, Kantarjian H, Manshouri T, Gidel C, Estey E, Thomas D, Koller C, Estrov Z, O'Brien S, Keating M, Freireich E, Albitar M. Angiogenesis in acute and chronic leukemias and myelodysplastic syndromes. Blood. 2000;96:2240-2245.
Not in our library
165.
Perez-Atayde AR, Sallan SE, Tedrow U, Connors S, Allred E, Folkman J. Spectrum of tumor angiogenesis in the bone marrow of children with acute lymphoblastic leukemia. Am J Pathol. 1997;150:815-821.
Not in our library
166.
Bieker R, Padro T, Kramer J, Steins M, Kessler T, Retzlaff S, Herrera F, Kienast J, Berdel WE, Mesters RM. Overexpression of basic fibroblast growth factor and autocrine stimulation in acute myeloid leukemia. Cancer Res. 2003;63:7241-7246.
Not in our library
167.
Krejci P, Dvorakova D, Krahulcova E, Pachernik J, Mayer J, Hampl A, Dvorak P. FGF-2 abnormalities in B cell chronic lymphocytic and chronic myeloid leukemias. Leukemia. 2001;15:228-237.
Not in our library10.1038/sj.leu.2402012
168.
Kini AR, Kay NE, Peterson LC. Increased bone marrow angiogenesis in B cell chronic lymphocytic leukemia. Leukemia. 2000;14:1414-1418.
Not in our library10.1038/sj.leu.2401825
169.
Menzel T, Rahman Z, Calleja E, White K, Wilson EL, Wieder R, Gabrilove J. Elevated intracellular level of basic fibroblast growth factor correlates with stage of chronic lymphocytic leukemia and is associated with resistance to fludarabine. Blood. 1996;87:1056-1063.
Not in our library
170.
Gruber G, Schwarzmeier JD, Shehata M, Hilgarth M, Berger R. Basic fibroblast growth factor is expressed by CD19/CD11c-positive cells in hairy cell leukemia. Blood. 1999;94:1077-1085.
Not in our library
171.
Giles FJ, Vose JM, Do KA, Johnson MM, Manshouri T, Bociek G, Bierman PJ, O'Brien SM, Kantarjian HM, Armitage JO, Albitar M. Clinical relevance of circulating angiogenic factors in patients with non-Hodgkin's lymphoma or Hodgkin's lymphoma. Leuk Res. 2004;28:595-604.
Not in our library10.1016/j.leukres.2003.11.002
172.
Vacca A, Ribatti D, Presta M, Minischetti M, Iurlaro M, Ria R, Albini A, Bussolino F, Dammacco F. Bone marrow neovascularization, plasma cell angiogenic potential, and matrix metalloproteinase-2 secretion parallel progression of human multiple myeloma. Blood. 1999;93:3064-3073.
Not in our library
173.
Sezer O, Jakob C, Eucker J, Niemöller K, Gatz F, Wernecke KD, Possinger K. Serum levels of the angiogenic cytokines basic fibroblast growth factor (bFGF), vascular endothelial growth factor (VEGF) and hepatocyte growth factor (HGF) in multiple myeloma. Eur J Haematol. 2001;66:83-88.
Not in our library10.1034/j.1600-0609.2001.00348.x
174.
Pazgal I, Zimra Y, Tzabar C, Okon E, Rabizadeh E, Shaklai M, Bairey O. Expression of basic fibroblast growth factor is associated with poor outcome in non-Hodgkin's lymphoma. Br J Cancer. 2002;86:1770-1775.
Not in our library10.1038/sj.bjc.6600330
175.
Salven P, Teerenhovi L, Joensuu H. A high pretreatment serum basic fibroblast growth factor concentration is an independent predictor of poor prognosis in non-Hodgkin's lymphoma. Blood. 1999;94:3334-3339.
Not in our library
176.
Ho CL, Sheu LF, Li CY. Immunohistochemical expression of basic fibroblast growth factor, vascular endothelial growth factor, and their receptors in stage IV non-Hodgkin lymphoma. Appl Immunohistochem Mol Morphol. 2002;10:316-321.
Not in our library10.1097/00129039-200212000-00005
177.
Gonzalez RM, Seurynck-Servoss SL, Crowley SA, Brown M, Omenn GS, Hayes DF, Zangar RC. Development and validation of sandwich ELISA microarrays with minimal assay interference. J Proteome Res. 2008;7:2406-2414.
Not in our library10.1021/pr700822t
178.
Rodriguez-Porcel M, Zhu X-Y, Chade AR, Amores-Arriaga B, Caplice NM, Ritman EL, Lerman A, Lerman LO. Functional and structural remodeling of the myocardial microvasculature in early experimental hypertension. Am J Physiol Heart Circ Physiol. 2006;290:H978-H984.
Not in our library10.1152/ajpheart.00538.2005
179.
Wang L, Park H, Chhim S, Ding Y, Jiang W, Queen C, Kim KJ. A novel monoclonal antibody to fibroblast growth factor 2 effectively inhibits growth of hepatocellular carcinoma xenografts. Mol Cancer Ther. 2012;11:864-872.
Not in our library10.1158/1535-7163.mct-11-0813
180.
Zong F, Fthenou E, Wolmer N, Hollosi P, Kovalszky I, Szilak L, Mogler C, Nilsonne G, Tzanakakis G, Dobra K. Syndecan-1 and FGF-2, but not FGF receptor-1, share a common transport route and co-localize with heparanase in the nuclei of mesenchymal tumor cells. PLoS One. 2009;4:e7346.
Not in our library10.1371/journal.pone.0007346
181.
Prasse AA, Zauner T, Büttner K, Hoffmann R, Zuchner T. Improvement of an antibody-enzyme coupling yield by enzyme surface supercharging. BMC biotechnology. 2014;14:88.
Not in our library10.1186/s12896-014-0088-6
182.
Candela ME, Geraci F, Turturici G, Taverna S, Albanese I, Sconzo G. Membrane vesicles containing matrix metalloproteinase9 and fibroblast growth factor2 are released into the extracellular space from mouse mesoangioblast stem cells. J Cell Physiol. 2010;224:144-151.
Not in our library10.1002/jcp.22111
183.
Gutiérrez J, Brandan E. A novel mechanism of sequestering fibroblast growth factor 2 by glypican in lipid rafts, allowing skeletal muscle differentiation. Mol Cell Biol. 2010;30:1634-1649.
Not in our library10.1128/mcb.01164-09
184.
Increased fibroblast telomerase expression precedes myofibroblast α-smooth muscle actin expression in idiopathic pulmonary fibrosis · 2012
Not checked
185.
DO MKQ, Suzuki T, Gerelt B, Sato Y, Mizunoya W, Nakamura M, Ikeuchi Y, Anderson JE, Tatsumi R. Timecoordinated prevalence of extracellular HGF, FGF2 and TGF3 in crushinjured skeletal muscle. Anim Sci J. 2012;83:712-717.
Not in our library10.1111/j.1740-0929.2012.01057.x
186.
Kujawski M, Kortylewski M, Lee H, Herrmann A, Kay H, Yu H. Stat3 mediates myeloid cell-dependent tumor angiogenesis in mice. J Clin Invest. 2008;118:3367.
Not in our library10.1172/jci35213
187.
Slaton JW, Perrotte P, Inoue K, Dinney CP, Fidler IJ. Interferon-alpha-mediated down-regulation of angiogenesis-related genes and therapy of bladder cancer are dependent on optimization of biological dose and schedule. Clin Cancer Res. 1999;5:2726-2734.
Not in our library
188.
Sun XH, Geng XL, Zhang J, Zhang C. miRNA-646 suppresses osteosarcoma cell metastasis by downregulating fibroblast growth factor 2 (FGF2). Tumour Biol. 2015;36:2127-2134.
Not in our library10.1007/s13277-014-2822-z
189.
Colombo G, Margosio B, Ragona L, Neves M, Bonifacio S, Annis DS, Stravalaci M, Tomaselli S, Giavazzi R, Rusnati M, Presta M, Zetta L, Mosher DF, Ribatti D, Gobbi M, Taraboletti G. Non-peptidic thrombospondin-1 mimics as fibroblast growth factor-2 inhibitors: an integrated strategy for the development of new antiangiogenic compounds. J Biol Chem. 2010;285:8733-8742.
Not in our library10.1074/jbc.m109.085605
190.
Smith JA, Madden T, Vijjeswarapu M, Newman RA. Inhibition of export of fibroblast growth factor-2 (FGF-2) from the prostate cancer cell lines PC3 and DU145 by Anvirzel and its cardiac glycoside component, oleandrin. Biochem Pharmacol. 2001;62:469-472.
Not in our library10.1016/s0006-2952(01)00690-6
191.
Alessi P, Leali D, Camozzi M, Cantelmo A, Albini A, Presta M. Anti-FGF2 approaches as a strategy to compensate resistance to anti-VEGF therapy: long-pentraxin 3 as a novel antiangiogenic FGF2-antagonist. Eur Cytokine Netw. 2009;20:225-234.
Not in our library10.1684/ecn.2009.0175
192.
Inoue K, Chikazawa M, Fukata S, Yoshikawa C, Shuin T. Frequent administration of angiogenesis inhibitor TNP-470 (AGM-1470) at an optimal biological dose inhibits tumor growth and metastasis of metastatic human transitional cell carcinoma in the urinary bladder. Clin Cancer Res. 2002;8:2389-2398.
Not in our library
193.
Marshall JL, Wellstein A, Rae J, DeLap RJ, Phipps K, Hanfelt J, Yunmbam MK, Sun JX, Duchin KL, Hawkins MJ. Phase I trial of orally administered pentosan polysulfate in patients with advanced cancer. Clin Cancer Res. 1997;3(12 Pt 1):2347-2354.
Not in our library
194.
Ferro V, Dredge K, Liu L, Hammond E, Bytheway I, Li C, Johnstone K, Karoli T, Davis K, Copeman E, Gautam A. PI-88 and novel heparan sulfate mimetics inhibit angiogenesis. Semin Thromb Hemost. 2007;33:557-568.
Not in our library10.1055/s-2007-982088
195.
Zhou S, Wang F, Hsieh TC, Wu JM, Wu E. Thalidomide-a notorious sedative to a wonder anticancer drug. Curr Med Chem. 2013;20:4102-4108.
Not in our library10.2174/09298673113209990198
196.
Liekens S, Leali D, Neyts J, Esnouf R, Rusnati M, Dell'Era P, Maudgal PC, De Clercq E, Presta M. Modulation of fibroblast growth factor-2 receptor binding, signaling, and mitogenic activity by heparin-mimicking polysulfonated compounds. Mol Pharmacol. 1999;56:204-213.
Not in our library10.1124/mol.56.1.204
197.
Sehgal SN. Sirolimus: its discovery, biological properties, and mechanism of action. Transplant Proc. 2003;35(3 Suppl):7S-14S.
Not in our library10.1016/s0041-1345(03)00211-2
198.
Tayel A, Abd El Galil KH, Ebrahim MA, Ibrahim AS, El-Gayar AM, Al-Gayyar MM. Suramin inhibits hepatic tissue damage in hepatocellular carcinoma through deactivation of heparanase enzyme. Eur J Pharmacol. 2014;728:151-160.
Not in our library10.1016/j.ejphar.2014.02.001
199.
Hagedorn M, Zilberberg L, Lozano RM, Cuevas P, Canron X, Redondo-Horcajo M, Gimenez-Gallego G, Bikfalvi A. A short peptide domain of platelet factor 4 blocks angiogenic key events induced by FGF-2. FASEB J. 2001;15:550-552.
Not in our library10.1096/fj.00-0285fje
200.
Matsui J, Funahashi Y, Uenaka T, Watanabe T, Tsuruoka A, Asada M. Multi-kinase inhibitor E7080 suppresses lymph node and lung metastases of human mammary breast tumor MDA-MB-231 via inhibition of vascular endothelial growth factor-receptor (VEGF-R) 2 and VEGF-R3 kinase. Clin Cancer Res. 2008;14:5459-5465.
Not in our library10.1158/1078-0432.ccr-07-5270
201.
Popat S, Mellemgaard A, Fahrbach K, Martin A, Rizzo M, Kaiser R, Griebsch I, Reck M. Nintedanib plus docetaxel as second-line therapy in patients with non-small-cell lung cancer: a network meta-analysis. Future Oncol. 2015;11:409-420.
Not in our library10.2217/fon.14.290
202.
Ayers M, Fargnoli J, Lewin A, Wu Q, Platero JS. Discovery and validation of biomarkers that respond to treatment with brivanib alaninate, a small-molecule VEGFR-2/FGFR-1 antagonist. Cancer Res. 2007;67:6899-6906.
Not in our library10.1158/0008-5472.can-06-4555
203.
Ueda Y, Shimoyama T, Murakami H, Yamamoto N, Yamada Y, Arioka H, Tamura T. Phase I and pharmacokinetic study of TSU-68, a novel multiple receptor tyrosine kinase inhibitor, by twice daily oral administration between meals in patients with advanced solid tumors. Cancer Chemother Pharmacol. 2011;67:1101-1109.
Not in our library10.1007/s00280-010-1404-z
204.
Inaba Y, Kanai F, Aramaki T, Yamamoto T, Tanaka T, Yamakado K, Kaneko S, Kudo M, Imanaka K, Kora S, Nishida N, Kawai N, Seki H, Matsui O, Arioka H, Arai Y. A randomised phase II study of TSU-68 in patients with hepatocellular carcinoma treated by transarterial chemoembolisation. Eur J Cancer. 2013;49:2832-2840.
Not in our library10.1016/j.ejca.2013.05.011
205.
Angevin E, Lopez-Martin JA, Lin CC, Gschwend JE, Harzstark A, Castellano D, Soria JC, Sen P, Chang J, Shi M, Kay A, Escudier B. Phase I study of dovitinib (TKI258), an oral FGFR, VEGFR, and PDGFR inhibitor, in advanced or metastatic renal cell carcinoma. Clin Cancer Res. 2013;19:1257-1268.
Not in our library10.1158/1078-0432.ccr-12-2885
206.
Bello E, Colella G, Scarlato V, Oliva P, Berndt A, Valbusa G, Serra SC, D'Incalci M, Cavalletti E, Giavazzi R, Damia G, Camboni G. E-3810 is a potent dual inhibitor of VEGFR and FGFR that exerts antitumor activity in multiple preclinical models. Cancer Res. 2011;71:1396-1405.
Not in our library10.1158/0008-5472.can-10-2700
207.
Sequist LV, Cassier P, Varga A, Tabernero J, Schellens JH, Delord J-P, LoRusso P, Camidge DR, Medina MH, Schuler M. Abstract CT326: Phase I study of BGJ398, a selective pan-FGFR inhibitor in genetically preselected advanced solid tumors. Cancer Res. 2014;74(19 Supplement):CT326-CT326.
Not in our library
208.
Perera T, Jovcheva E, Vialard J, Verhulst T, Esser N, Wroblowski B, Gilissen R, Freyne E, King P, Platero S. JNJ-42756493 is an inhibitor of FGFR-1, 2, 3 and 4 with nanomolar affinity for targeted therapy. Cancer Res. 2014;74(19 Supplement):1738-1738.
Not in our library
209.
Dransfield D, Lee J, Waghorne C, Bull C, Savage RE, Zhao X, Yuan S, Chang E, Nakuci E, Eathiraj S. Abstract A278: ARQ 087, a multi-tyrosine kinase inhibitor with potent in vitro and in vivo activity in FGFR2 driven models. Mol Cancer Ther. 2013;12(11 Supplement):A278-A278.
Not in our library
210.
Zhao G, Li W-y, Chen D, Henry JR, Li H-Y, Chen Z, Zia-Ebrahimi M, Bloem L, Zhai Y, Huss K. A novel, selective inhibitor of fibroblast growth factor receptors that shows a potent broad spectrum of antitumor activity in several tumor xenograft models. Mol Cancer Ther. 2011;10:2200-2210.
Not in our library10.1158/1535-7163.mct-11-0306
211.
Ochiiwa H, Fujita H, Itoh K, Sootome H, Hashimoto A, Fujioka Y, Nakatsuru Y, Oda N, Yonekura K, Hirai H. Abstract A270: TAS-120, a highly potent and selective irreversible FGFR inhibitor, is effective in tumors harboring various FGFR gene abnormalities. Mol Cancer Ther. 2013;12(11 Supplement):A270-A270.
Not in our library
212.
Qing J, Du X, Chen Y, Chan P, Li H, Wu P, Marsters S, Stawicki S, Tien J, Totpal K. Antibody-based targeting of FGFR3 in bladder carcinoma and t (4; 14)-positive multiple myeloma in mice. J Clin Invest. 2009;119:1216.
Not in our library10.1172/jci38017
213.
Trudel S, Bergsagel PL, Singhal S, Niesvizky R, Comenzo RL, Bensinger WI, Lebovic D, Choi Y, Lu D, French D. A phase I study of the safety and pharmacokinetics of escalating doses of MFGR1877S, a fibroblast growth factor receptor 3 (FGFR3) antibody, in patients with relapsed or refractory t (4; 14)-positive multiple myeloma. ASH Annual Meeting Abstracts. 2012;4029.
Not in our library
214.
Batley BL, Doherty AM, Hamby JM, Lu GH, Keller P, Dahring TK, Hwang O, Crickard K, Panek RL. Inhibition of FGF-1 receptor tyrosine kinase activity by PD 161570, a new protein-tyrosine kinase inhibitor. Life Sci. 1997;62:143-150.
Not in our library10.1016/s0024-3205(97)01060-6
215.
Pardo OE, Latigo J, Jeffery RE, Nye E, Poulsom R, Spencer-Dene B, Lemoine NR, Stamp GW, Aboagye EO, Seckl MJ. The fibroblast growth factor receptor inhibitor PD173074 blocks small cell lung cancer growth in vitro and in vivo. Cancer Res. 2009;69:8645-8651.
Not in our library10.1158/0008-5472.can-09-1576
216.
Panek RL, Lu GH, Klutchko SR, Batley BL, Dahring TK, Hamby JM, Hallak H, Doherty AM, Keiser JA. In vitro pharmacological characterization of PD 166285, a new nanomolar potent and broadly active protein tyrosine kinase inhibitor. J Pharmacol Exp Ther. 1997;283:1433-1444.
Not in our library
217.
Panek RL, Lu GH, Dahring TK, Batley BL, Connolly C, Hamby JM, Brown KJ. In vitro biological characterization and antiangiogenic effects of PD 166866, a selective inhibitor of the FGF-1 receptor tyrosine kinase. J Pharmacol Exp Ther. 1998;286:569-577.
Not in our library
218.
Fischer H, Taylor N, Allerstorfer S, Grusch M, Sonvilla G, Holzmann K, Setinek U, Elbling L, Cantonati H, Grasl-Kraupp B. Fibroblast growth factor receptor-mediated signals contribute to the malignant phenotype of non-small cell lung cancer cells: therapeutic implications and synergism with epidermal growth factor receptor inhibition. Mol Cancer Ther. 2008;7:3408-3419.
Not in our library10.1158/1535-7163.mct-08-0444
219.
Zhou W, Hur W, McDermott U, Dutt A, Xian W, Ficarro SB, Zhang J, Sharma SV, Brugge J, Meyerson M. A structure-guided approach to creating covalent FGFR inhibitors. Chem Biol. 2010;17:285-295.
Not in our library10.1016/j.chembiol.2010.02.007
220.
Herbert C, Schieborr U, Saxena K, Juraszek J, De Smet F, Alcouffe C, Bianciotto M, Saladino G, Sibrac D, Kudlinzki D. Molecular mechanism of SSR128129E, an extracellularly acting, small-molecule, allosteric inhibitor of FGF receptor signaling. Cancer Cell. 2013;23:489-501.
Not in our library10.1016/j.ccr.2013.02.018
221.
Bono F, De Smet F, Herbert C, De Bock K, Georgiadou M, Fons P, Tjwa M, Alcouffe C, Ny A, Bianciotto M. Inhibition of tumor angiogenesis and growth by a small-molecule multi-FGF receptor blocker with allosteric properties. Cancer cell. 2013;23:477-488.
Not in our library10.1016/j.ccr.2013.02.019

Cited by papers we hold 3

Data on the evaluation of FGF2 gene expression in Colorectal Cancer · 2020
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Targeting Adenosine in Cancer Immunotherapy to Enhance T-Cell Function · 2019
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Estrogen is involved in hemangioma regression associated with mast cells · 2018
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