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The Functional Role of Extracellular Matrix Proteins in Cancer

Nadezhda V. Popova, Manfred Jücker

Cancers · 2022 · Review · CC BY

Abstract

Simple Summary. Extracellular matrix is a three-dimensional network of macromolecules that provide structural and biochemical support to surrounding cells. Extracellular matrix plays a critical role in the development and progression of cancer. The extracellular matrix of the tumor is very different from the matrix of the normal tissue. Mainly fibroblasts produce and regulate matrix remodeling, but in cancer, the tumor matrix also originates from cancer cells. We describe the mechanisms of how the protein composition and structure of the extracellular matrix changes during cancer progression and how abnormal matrix deregulates the behavior of stromal cells and influences cancer progression.

Abstract. The extracellular matrix (ECM) is highly dynamic as it is constantly deposited, remodeled and degraded to maintain tissue homeostasis. ECM is a major structural component of the tumor microenvironment, and cancer development and progression require its extensive reorganization. Cancerized ECM is biochemically different in its composition and is stiffer compared to normal ECM. The abnormal ECM affects cancer progression by directly promoting cell proliferation, survival, migration and differentiation. The restructured extracellular matrix and its degradation fragments (matrikines) also modulate the signaling cascades mediated by the interaction with cell-surface receptors, deregulate the stromal cell behavior and lead to emergence of an oncogenic microenvironment. Here, we summarize the current state of understanding how the composition and structure of ECM changes during cancer progression. We also describe the functional role of key proteins, especially tenascin C and fibronectin, and signaling molecules involved in the formation of the tumor microenvironment, as well as the signaling pathways that they activate in cancer cells.

Full text

From PubMed Central, U.S. National Library of Medicine, as current on Oct 20, 2026. Paragraph numbers are ours, so an answer can point at one.

1. Introduction

1The tumor microenvironment is a highly heterogeneous environment around a tumor, that includes cellular components (fibroblasts, endothelial cells, adipocytes, immune and inflammatory cells) and a non-cellular component termed the extracellular matrix (ECM). During cancer progression, carcinoma cells recruit host stromal cells, which change their properties and metabolism, and together they create a unique microenvironment to cooperatively remodel the surrounding matrix and promote tumor invasion. Remodeling of the ECM, driven by proteolytic enzymes (such as matrix metalloproteinases), by enzymes that control the modification and cross-linking of extracellular matrix proteins (such as lysyloxidases (LOX)), results in increased stiffness and altered ECM composition. Tumor cells also secrete extracellular vesicles with nucleic acids, lipids and proteins, which can participate in tumor progression and behavior, including tumor environment remodeling, fibroblast activation, angiogenesis, immunomodulation or the establishment of pre-metastatic niches.

2Degradation of ECM is not a passive event as it is accompanied by the release of matrix-bound growth factors as well as matrikines that interact with multiple surface receptors and trigger signal transduction, thus regulating tumor growth and cell migration.

3This review aims to present the functional role of ECM components in tumor development, with particular emphasis on the involvement of fibronectin and tenascin in this process. We also describe the relationships between cancer cells and cancer-associated fibroblasts, and the mechanisms by which cancerized ECM can modulate tumor progression and aggressiveness.

2. Structural Organization and Properties of Extracellular Matrix

4The extracellular matrix is a major structural component of the tumor microenvironment and is comprised of a three-dimensional network consisting of collagens, laminins, elastin and elastic fibers, glycoproteins and proteoglycans. In normal tissue, ECM provides structural support for the cells and also plays a regulatory role in many cellular processes including growth, migration, differentiation, survival, homeostasis and morphogenesis. Every tissue (e.g., connective tissue, cartilage or bone) has a unique ECM composition, and the components of the ECM are produced and arranged by resident cells in accordance with the needs of the tissue (reviewed in).

5Based on biochemical and structural characteristics, the animal extracellular matrix can be classified into interstitial matrix and basement membrane. The interstitial matrix surround cells, whereas the basement membrane, a thin sheet-like extracellular matrix, delimits the stroma from cells of various origins (epithelial and endothelial cells, neurons and muscle cells, or adipocytes) and surrounds muscle fibers, adipose tissue, Schwann cells as part of myelin nerve fibers. The major components of the basement membrane are type IV collagen, laminins, nidogen 1 and 2, and proteoglycans perlecan and agrin (Figure 1).

6Collagens are the major proteins of the ECM. Collagens are typically homo- or heterotrimers made of one, two or three different polypeptide chains (α-chains). For example, there are six different genes designated COL4A1-COL4A6 encoding type IV collagen chains α1(IV)–α6(IV). Laminins are large heterotrimeric glycoproteins, consisting of α, β and γ chains that assemble to form a Y-shaped molecule. Mammalian genomes encode five α (α1–α5), four β (β1–β4) and three γ (γ1–γ3) chains and the laminin isoforms are named according to the three chain composition: i.e., laminin 332 is composed of α3, β3 and γ2 chains.

7Type IV collagen and laminin individually self-assemble into two independent but interconnected networks that serve as the foundation for basement membrane. Globular domain of laminins at the end of the α chain binds to cellular receptors, including integrins, α-dystroglycan, heparan sulfates and sulfated glycolipids. Nidogens and proteoglycans perlecan and agrin bridge the laminin and type IV collagen networks, increase their stability and influence the structural integrity of basement membrane. Basement membrane also contains matricellular proteins such as thrombospondins, secreted protein acidic and rich in cysteine (SPARC), cartilage oligomeric matrix protein (COMP), tenascins and osteopontin (Figure 2) that interact with other matrix components and growth factors as well as with cell surface receptors contributing to tissue-specific functions.

8Interactions of cells with the ECM are mediated by their surface receptors, such as integrins, syndecans and discoidin domain receptors (DDRs). The family of integrins that are the main cell adhesion receptors for components of ECM includes at least 24 transmembrane heterodimers generated from a combination of non-covalently paired α- and β-subunits. Based on ligand substrate, integrins can be classified into receptors recognizing Arg-Gly-Asp (RGD) peptide motifs, collagen, laminin or leukocyte-specific integrins. Integrins are bi-directional signaling receptors involved in outside-in and inside-out signaling. The inside-out signaling mainly acts to bring the integrin into the active conformation. Upon ligand binding, integrins undergo conformation changes leading to outside-in signaling. Ligand-bound integrins engage the actin network via talin and additional cytoskeletal linker proteins, leading to integrin clustering and the following activation of focal adhesion kinase (FAK), Src-family protein tyrosine kinases and integrin-linked kinase (ILK). Integrin adhesion also activates the Ras-ERK, PI3K/AKT and YAP/TAZ pathways.

9Basement membranes are tightly associated with the interstitial matrix (lamina propria) through collagen fibrils, including collagens VI and VII. Collagen VI binds to laminin and collagen IV, as well as to collagen I fibrils in the interstitial matrix. The protein composition of the interstitial matrix mainly includes collagens (I, III, V, VI), fibronectin and elastin.

3. Fibroblasts and Cancer-Associated Fibroblasts

10ECM is a highly dynamic structure that is constantly remodeled, and fibroblasts are the major producers of ECM in normal physiology and in tissue repair. After injury, tissue healing begins by activation of platelets to form a clot consisting of fibrin and fibronectin. Platelets recruit immune cells to the injury site by releasing abundant soluble mediators and also produce adhesive glycoproteins resulting in the deposition of a fibrin clot that serves as a provisional matrix. Platelets, endothelial cells and macrophages secrete signaling molecules including transforming growth factor (TGF-β) and platelet-derived growth factor (PDGF) that recruit resident and immigrating fibroblasts. These signals direct fibroblasts to either obtain pro-fibrotic phenotype, switching to ECM protein synthesis, or differentiate into myofibroblasts which participate in wound contraction. Fibroblasts degrade the provisional matrix by producing matrix metalloproteinases (MMPs) and replace it with immature collagens, elastin, fibronectin and proteoglycans, and forming mature collagen fibrils later in repair. As the wound closes and evolves into a scar, myofibroblasts become apoptotic and finally disappear.

11TGF-β, among other inflammatory cytokines, is a key regulator of fibroblast to myofibroblast differentiation during wound healing and cancer-associated fibroblasts (CAFs) transition in various cancers, including prostate, breast, pancreatic, bladder and colorectal cancer. Active TGF-β can be released from ECM as a result of its degradation (reviewed in) or can be secreted in exosomes by cancer cells. CAFs in turn can also derive not only from resident fibroblasts and myofibroblast-like cells but also from adipocytes, bone marrow-derived mesenchymal cells, hematopoietic stem cells or endothelial cells, which explains, at least in part, the heterogeneity of CAFs in the tumor microenvironment.

12Since CAFs produce a number of proteins that are specific to the origin of the cells and there is no specific protein to CAFs, a combination of proteins is used as markers to identify CAFs. Several intracellular and plasma membrane-associated proteins such as alpha-smooth muscle actin (α-SMA), fibroblast-activating protein (FAP), S100A4 protein/fibroblast specific protein-1 (FSP1) and vimentin have been used as CAF markers. CAFs are characterized by increased proliferative capacity, elevated production of growth factors and ECM proteins, and increased metabolic activity. Cancer-associated fibroblasts have been found to produce highly aligned fibronectin matrix, which promotes directional migration of cancer cells in CAF-derived matrices.

4. ECM Remodeling and Modification in Cancer

13ECM deposition is considered a hallmark of cancer. Mainly CAFs are responsible for ECM synthesis and remodeling. CAFs, driven by cancer cells, not only synthesize, produce and deposit substantial amounts of ECM components but also contract the tissue, thus altering the ECM of the tumor stroma qualitatively and quantitatively. Some tumor cells themselves can also synthesize components of the ECM such as collagen and other ECM- and ECM-associated proteins, including secreted factors and modulators of the matrix. Compared to stromal cells, cancer cells produce less amount of ECM proteins (<10% in pancreatic cancer) but it was found that a number of cancer-cell–derived proteins can promote tumorigenesis and metastasis and correlate with poor patient survival.

4.1. Collagen Reorganization

14Increased deposition of collagen is the most common alteration of ECM in cancer. In healthy tissues, interstitial collagen fibers are wavy, whereas the collagen fibers in tumors are often straightened as well as quantitatively and qualitatively reorganized.

15Three different orientations and deposition of collagen fibers, named tumor-associated collagen signatures (TACS), were revealed in human breast cancer to characterize tumors: TACS-1, the increased collagen fiber accumulation at a region surrounding the small tumors; TACS-2, the presence of straightened collagen fibers stretched around the tumor in noninvasive tumors and lastly TACS-3, the presence of collagen fibers aligned perpendicular to the tumor boundary. Similar structural collagen signatures were found in other cancers such as ovarian cancer, basal cell carcinoma, prostate cancer, glioblastoma, renal cell carcinoma and pancreatic ductal adenocarcinoma. TACS have been shown to promote focal invasion and metastasis, influence disease state and tumor invasion and correlate with significantly worse patient survival in multiple tumor types.

16Linearly aligned collagen fibers are thought to generate migration highways that allow cancer cell invasion and dissemination. It was demonstrated that ECM deposited by CAFs was remarkably aligned in a parallel pattern, and CAFs promoted the dissemination of malignant cells in vivo. Increased collagen density and enzymatic cross-linking of collagen during tumor progression can lead to matrix stiffening, and stiffened cross-linked fibrillar collagen promoted enhanced PI3 kinase (PI3K) activity, and induced the invasion of an oncogene-initiated epithelium.

17To locally degrade and to penetrate ECM barriers, cells use actin-rich protrusions termed invadosomes, which include invadopodia (in cancer cells) or podosomes (in stromal cells). It was shown that a high-density fibrillar collagen matrix can itself induce a formation of invadopodia via a specific integrin signaling pathway even in the absence of a significantly altered gene or specific protein expression. Collagen I and IV have been demonstrated to promote invadopodia extension and migration of tumor cells as well as fibroblasts, endothelial cells and macrophages.

18Some collagens also bind and activate receptor tyrosine kinases discoidin domain receptors (DDR1 and DDR2) that are thought to mediate metastases and cancer aggressiveness. DDR1 activation induces Src, Notch and IKK signaling pathway, DDR2 promotes oncogenic signaling via mTORC2 and AKT pathway, and recent findings have demonstrated that DDR-collagen signaling plays an important role in cancer progression and metastasis (reviewed in).

4.2. Collagens and Laminins

19Many types of collagen are upregulated in cancer and involved in almost all steps of tumor progression including proliferation, invasion, angiogenesis and metastasis.

20Fibril-forming collagens provide three-dimensional frameworks of tissues and organs, and their involvement in cancer progression has been the most studied in comparison to other types of collagens. The most abundant type I collagen plays a significant role in different cancers and metastases. Type I collagen-dense ECM can drive the metastases of estrogen receptor 1 (ERα+) breast cancers by altering hormonal signals. It was also demonstrated that type I collagen can induce resistance to epidermal growth factor receptor tyrosine kinase inhibitors (EGFR-TKIs) via mTOR activation through an AKT-independent pathway. Type XI collagen, a minor fibril-forming collagen, is a component of fibrils both in cartilage and a wide variety of non-cartilaginous tissues. Its alpha 1 chain (COL11A1) has been found to be upregulated in a variety of cancers and is supposed to promote proliferation, angiogenesis, invasion and drug resistance of cancer cells. Proteolytic products of type XI collagen released into the circulation can be used as predictive markers for patients with pancreatic ductal adenocarcinoma. Type V collagen, another minor fibril-forming collagen, was also shown to be upregulated in squamous cell carcinoma, colorectal, gastric and breast cancer and associated with poor prognosis.

21Collagen VI is expressed in many tissues where it interacts with different ECM proteins and cell surface molecules and functions as a bridge between the basement membrane and interstitial matrix. Type VI collagen expression is elevated in many human cancers such as pancreatic, ovarian, lung, breast and colon cancer, favoring cell survival and tumor progression. In recent studies, it has been demonstrated that alpha-3 chain of collagen VI and the cleaved C5 domain fragment, called endotrophin, are highly expressed in a variety of cancers and play a crucial role in tumorigenesis.

22Laminins are also involved in cancer progression, including invasion, migration, angiogenesis, metastasis and drug resistance. Expression of various laminin subunits is often upregulated in tumor or stromal cells of malignant tissues. Laminin-332 has attracted a lot of attention by its altered expression pattern in several human carcinomas: expression of laminin-332, or its γ2 chain, is markedly elevated in mammary, colon, melanoma and sarcoma cancer cells and correlates with tumor invasiveness and poor patient prognosis. It is proposed that laminin-332 involvement in tumor progression is mediated by binding to integrins α6β4 or α3β1 and subsequent activation of focal adhesion kinase (FAK) and extracellular signal-regulated kinase (ERK). Increased laminin-332 γ2 chain expression is a significant poor prognostic indicator for the patients with esophageal or colorectal carcinoma. The fragment of laminin-332 γ2 chain after cleavage by MT1-MMP or MMP-2 can bind to and activate EGFR and downstream MAPK signaling in cancer cells as well as MMP-2 gene expression and cell migration.

4.3. Fibronectin

23Fibronectin is a high-molecular-weight glycoprotein that consists of two subunits, covalently linked by a pair of disulfide bonds at the C-termini. Despite fibronectin protein being produced from a single gene, there are 20 isoforms of human fibronectin as a result of alternative splicing. Fibronectin exists soluble as a dimer in the plasma (pFN) or as an insoluble part of the ECM (cellular FN) where it interacts with many other ECM components. Fibronectins have been shown to interact with integrins, collagen, tenascin-C, fibrillin, glycosaminoglycans as well as with growth factors (reviewed in).

24Plasma fibronectin is synthesized and secreted without ED-A or ED-B segments (Figure 3) by hepatocytes. Cellular fibronectin is synthesized by many cell types, including fibroblasts, endothelial cells, macrophages and tumor cells, and secreted with ED-A and/or ED-B extra-domains. In cancer, CAFs have generally considered a source of fibronectin. CAFs secrete and assemble fibronectin as parallel fibers mediating directional cancer cell migration.

25For instance, in breast tumor tissues the expression of fibronectin, and specifically the ED-B isoform, was significantly higher compared to the adjacent tissues. Immunohistochemical analysis showed ED-B expression in cancer cell-associated fibroblasts, stroma and stromal fibroblasts, as well as in primary breast tumor and lymph node, lung, and brains metastases. The expression of fibronectin is elevated in many solid tumors and is supposed to correlate with tumor grade/aggressiveness and can serve as a prognostic marker.

26Although it is assumed that the role of fibronectin in oncogenesis and malignant progression is highly controversial the mechanisms of fibronectin action in cancer are being actively studied (reviewed in).

27The role of fibronectin in promoting growth, survival and invasion of cancer cells has been highlighted by in vitro studies. It was shown that detachment of pancreatic cancer cells from ECM stimulated necrosis but fibronectin and laminin markedly increased the cells’ survival by inhibiting both mitochondrial dysfunction and caspase activity. Then this group of authors provided evidence that in pancreatic cancer cells fibronectin increased intracellular reactive oxygen species (ROS) production and NADPH oxidase activation. The prosurvival effect of fibronectin on pancreatic cancer cells has been further investigated and shown to be mediated through the trans-activation of IGF-IR. The mechanism involved fibronectin-mediated complex formation between integrin β3 and protein-tyrosine phosphatase SHP-2 that prevented SHP-2 from dephosphorylation of IGF-IR resulting in its sustained phosphorylation and the downstream activation of AKT kinase, up-regulation of anti-apoptotic Bcl-xL and inhibition of apoptosis.

28It was also found that exogenous fibronectin stimulates lung carcinoma cell proliferation via integrin α5β1 through activation of the AKT/mTOR/p70S6K pathway and inhibition of AMPK and LKB1 expression. Exogenous fibronectin significantly enhanced proliferation and invasion in gallbladder cancer cell lines and markedly activated AKT/mTOR/4E-BP1 signaling cascade. The role of fibronectin in promoting growth and migration via Src and TGF-β1 signaling was also demonstrated in renal cell carcinoma. Fibronectin can support cancer cell proliferation through Erk and Rho-kinase signaling. A recent study provided evidence that collagen and fibronectin together, but not alone, facilitate proliferation and tumorigenesis of glioma cells through PI3K/AKT/SOX2 and CDC42/F-actin/YAP-1/Nupr1/Nestin signaling pathways via integrin αvβ3.

29Fibronectin is also a cargo in extracellular vesicles (EV) from different cell types (reviewed in). EV is a term used to define lipid bilayer membrane particles secreted by cells. EVs can be generally divided into exosomes, microvesicles, apoptotic bodies and recently identified matrix-bound nanovesicles (MBV). Exosomes have been shown to play a major role in different stages of cancer progression, including cell proliferation, angiogenesis, invasion and metastasis. MBVs, vesicles integrated within the dense fibrillar network of the ECM, are differ from exosomes in membrane composition and luminal cargo. MBVs are supposed to have a potential role in development, homeostasis, wound healing, tissue regeneration and neoplasia, but to date, there is no information on their involvement in cancer.

30Fibronectin was found on the surface of fibroblast-derived extracellular vesicles. The EV surface–associated fibronectin induced an invasive phenotype in recipient fibroblasts, and the effect was dependent on interaction with the fibronectin receptor α5β1 integrin, and activation of FAK and Src family kinases.

31In a mouse model, circulating fibronectin enhanced the amount of local fibronectin in tumors through a positive feedback loop as well as enhanced tumor growth by increasing vascular endothelial growth factor (VEGF) content and VEGF-mediated signaling.

32The production of fibronectin by cancer cells also contributes to the tumor development. In suspension cultures, squamous cell carcinoma cell aggregates, but not single cells, had high levels of fibronectin and were more resistant to anoikis through a mechanism involving fibronectin and the integrin αv receptor/FAK signaling. An upregulation of fibronectin levels due to detachment has also been demonstrated for lung and breast cancer cell aggregates, and this upregulation was suggested to be important for the development of anoikis resistance and further metastasis. In a mouse model, a decrease in fibronectin production by cancer cells was shown to inhibit cancer growth due to inhibition of proliferation by decreasing ERK phosphorylation and diminishing YAP expression.

4.4. Tenascin

33Tenascin-C, the first discovered member of the tenascin family, is a multifunctional ECM glycoprotein. Other members of the family are tenascin-R, tenascin-W, tenascin-X and tenascin-Y.

34The molecule of tenascin-C consists of six ~250 kDa subunits that are linked together at one end by disulfide bonds, and each subunit has four distinct domains. Eight FNIII repeats (FNIII 1–8) are constitutively present in the tenascin-C molecule (Figure 4), but the nine FNIII repeats located between the fifth and sixth FNIII domain may be present due to alternative splicing. The alternative splicing is thought to control the tenascin-C versatile functions by modulating its interaction with specific binding partners. Moreover, splice isoforms demonstrate different sensitivity to proteases. Tenascin-C has been shown to interact with various ligands, for instance with integrins, EGFR, fibronectin and other ECM components (reviewed in).

35Tenascin-C has highly specific and restricted expression patterns in the embryo but is almost undetectable in most adult tissues. In adults, tenascin-C expression can be upregulated by mechanical stress, upon tissue repair or in cancer (reviewed in). By mechanical stress, tenascin-C expression was found to be regulated by dynamic (cyclic) strain as well as by static tensile stress, for instance by stressed collagen gels. Tenascin-C expression is elevated in fibroblasts in response to TGF-β or PDGF via PI3K/AKT pathway upon inflammation or wound repair (reviewed in). Although the expression of tenascin-C in the adult tissue is usually low, it has been described to be elevated in many human cancers.

36Tenascin-C is highly expressed by cancer-associated fibroblasts and stromal cells, as well as by some cancer cells, and has been involved in promoting proliferation, migration, angiogenesis and metastasis. High expression of tenascin-C correlates with cancer grade and poor prognosis in various cancers, including esophageal squamous cell carcinoma, glioma, gastric, prostate, breast and colorectal cancer.

37Expression of tenascin-C in tumor stroma was found in regions called tumor matrix tracks that are composed of several matrix molecules and are enriched with stromal cells including endothelial cells, fibroblasts and immune cells. It was also found that tenascin-C and thrombospondin-2 co-localize with aligned collagen fibers in patient samples with invasive ductal carcinoma. Tenascin-C expression can be induced in cancer cells as well as in stromal cells by different factors, including EGF, TGF-β, b-FGF and TNF-α. For instance, mammary tumor cells produce TGF-β1, which induces fibroblasts to synthesize tenascin. Ras-transformed epithelial cells express tenascin-C in response to TGF-β, and elevated ERK/MAPK signaling but not PI3K signaling was required for high expression levels of tenascin-C.

38In vitro experiments suggested that tenascin-C can induce epithelial-to-mesenchymal transition (EMT) in breast cancer cells via binding to αvβ6 and αvβ1 integrins, colorectal and pancreatic cancer cells or promote invadopodia formation in Ewing sarcoma. Knockdown of tenascin-C inhibited the proliferation and invasion of gastric cancer cells and EMT process through inhibited ERK phosphorylation. Tenascin-C has been found to induce and activate others signaling pathways in cancer cells such as JNK, Wnt, Notch, AKT/HIF1α and TGF-β.

39The effect of tenascin on stromal formation has also been investigated. The addition of tenascin-C to fibroblasts significantly up-regulated α-smooth muscle actin and calponin that are the specific markers of differentiation to myofibroblasts, as well as significantly up-regulated the production of tenascin itself through integrin αvβ1/TGF-β signaling axis. Yeo et al. demonstrated that tenascin-C is not only produced from fibroblasts but also is essential for their activation. They have found a positive feedback loop comprising basic helix-loop-helix transcription factor Twist1, homeobox transcription factor Prrx1, and tenascin-C functions as a bistable (ON/OFF) switch to initiate fibroblast activation.

40Like fibronectin, tenascin-C was also detected in extracellular vesicles released into the extracellular space by most cell types, including fibroblasts and tumor cells (reviewed in). Moreover, tenascin-C was detected in exosomes isolated from the blood of glioblastoma patients. The authors established an immunosuppressive role for tenascin-C, since it was shown that tenascin-C inhibited T-cell proliferation through interaction with integrins α5β1 and αvβ6 on T lymphocytes and decrease in AKT/mTOR signaling. Jachetti et al. have also demonstrated that tenascin-C produced by prostate cancer stem-like cells inhibited T-cell proliferation by interacting with α5β1 integrin and blocking reorganization of the actin-based cytoskeleton.

41Experiments in vivo showed that knockdown of tenascin-C inhibited tumor growth and peritoneal dissemination and suggested the involvement of tenascin-C in vasculogenic mimicry formation. It was also shown that stromal-derived tenascin-C promotes lung metastasis by impacting blood vessels invasions (BVI) at multiple levels. Tenascin-C may generate barriers for infiltrating T lymphocytes (TIL), thus contributing to the escape from anti-tumor immunity.

42In cancer, not only increased expression of tenascin is observed, but also various splice isoforms generated through alternative splicing of exons within fibronectin type III repeats (reviewed in). Certain splice isoforms of tenascin-C were found in particular types of cancer. Some studies have shown that larger tenascin-C isoforms are expressed only in tumorous but not in healthy tissues and their expression correlate with cancer progression and poor prognosis in glioma, bladder, ovarian breast, pancreatic, esophageal and lung cancer. However, there are also data that the higher molecular weight of the isoform may not be the most relevant to cancer progression as there are examples of cancers where the smallest tenascin-C isoform is predominantly expressed or smaller splice variants promote invasion more effectively than does the unspliced tenascin-C.

5.1. Matrix Remodeling Enzymes

43To permit invasion and cell migration, the extracellular matrix must be destroyed. The ECM is cleaved and degraded by target-specific proteases such as matrix metalloproteinases (MMPs), a disintegrin and metalloproteinases (ADAMs), a disintegrin and metalloproteinases with thrombospondin motifs (ADAMTS), cathepsins and plasminogen activation system components (reviewed in). These proteases are secreted primarily by stromal cells but also by cancer cells. It was found in several studies in vitro and in vivo that CAFs induce migration, invasion and metastasis of cancer cells by producing various MMPs, including MMP-1, -2, -3, -7, -9 and -14.

44Matrix metalloproteinases (MMPs) are a large family of calcium-dependent zinc-containing endopeptidases: 28 different MMPs were found in vertebrates, of which at least 23 MMPs are expressed in humans. On the basis of their substrate specificity and domain organization, MMPs are classified into collagenases, gelatinases, stromelysins, matrilysins, membrane-type (MT)-MMPs and other MMPs. MMPs are initially secreted as inactive zymogens due to the interaction of a cysteine residue of the pro-domain with the zinc ion of the catalytic site. Only after disruption of this interaction by proteolytic removal of the pro-domain the enzyme become proteolytically active.

45Gelatinases MMP-2 and MMP-9 as well as transmembrane MMP-14 (also known as MT1-MMP) are enriched at invadopodia that are essential for the degradation of ECM components and cell invasion. A number of signals from the tumor environment, such as growth factors, hypoxia, extracellular pH, metabolism or direct interactions with stromal cells affect invadopodia formation and function. The number and activity of invadopodia can also be directly increased by ECM rigidity, indicating a potential mechanism for the reported correlation of tissue density with cancer aggressiveness.

46MT1-MMP (MMP14) is considered to play a key role in the early stages of tumor invasion and cancer progression. Cancer cells concentrate MT1-MMP at invadopodia membranes that can degrade a number of ECM molecules including collagen types I, II, III, fibronectin, tenascin, nidogen, perlecan and aggrecan. MT1-MMP also activates MMP-2 and combined action of MT1-MMP and MMP-2 is thought to enhance ECM proteolysis: MT1-MMP denaturates collagen into gelatin, which is subsequently digested by MMP-2 gelatinase. Elevated expression of MMP-2 and MMP-9 is indeed considered a hallmark of cancer aggressiveness, and it is suggested that their levels can be useful prognostic biomarkers. As a result of basement membrane degradation, tumor cells gain access to the blood and lymphatic vessels. As a result of excessive collagen remodeling by matrix metalloproteinases, small protein fragments of degraded collagens are released into the circulation and can be used to measure tumor activity and invasiveness as well as to serve as a prognostic and/or predictive biomarkers in different cancers.

5.2. Matrikines

47Proteases secreted into the tumor microenvironment are not only essential for ECM remodeling, but they also release bioactive ECM fragments matrikines or expose matricryptins. These fragments in turn can regulate a wide array of biological processes, including angiogenesis, cell migration, adhesion and differentiation as well as tumor growth and metastasis. It was found that matrikines can originate from collagen, elastin, tenascin, fibronectin, laminins, decorin, thrombospondin and versican.

48In cancer, the most well-studied matricryptins are derived from collagens (e.g., collagens I, IIB, IV, VIII, XV, XVIII and XIX). A number of well-studied collagen fragments have anti-tumorigenic properties: arresten, canstatin, endostatin, pentastatin and vastatin. In contrast, there are matrikines that exhibit pro-tumorigenic activity. For instance, endotrophin plays a critical role in cancer development and is considered to be a target for anti-tumor therapy.

49Tenascin-C is also proteolytically cleaved by MMP-2 and cathepsin B, and degradation was associated with higher recurrence and a worse prognosis for the patients with lung cancer. It was found that tenascin-C molecule contains cryptic sequence YTITIRGV within the FN type III repeat A2 (Figure 4) that is exposed by MMP-2 processing. The 22-mer peptide containing YTITIRGV termed TNIIIA2 is capable to induce activation of integrin α5β1 and to rescue non-transformed fibroblasts from serum starvation–elicited apoptosis through activation of the AKT/Bcl-2 pathway. It was also found that activation of integrin α5β1 by TNIIIA2 caused active proliferation, disseminative migration and anoikis resistance in glioblastoma cells. In glioblastoma cells, TNIIIA2 was also able to stimulate PDGF production that resulted in upregulation of the tenascin-C expression in these cells. Tenascin-C induced increased expression of the active form of MMP-2 in glioblastoma cells, which was supposed to contribute to continuous PDGF production suggesting a positive feedback loop of tenascin-C/TNIIIA2/PDGF leading to hyper-proliferation of glioblastoma cells. TNIIIA2 also promoted colon cancer cell invasion in vitro by upregulating MMPs and boosted pulmonary metastasis of colon cancer cells in a mouse model.

50Unlike TNIIIA2, which has the ability to activate β1-integrins and is involved in the aggressive development of cancer, FNIII14, the peptide containing the bioactive site of plasma fibronectin, demonstrated an anti-tumor effect. It was found that plasma fibronectin has a cryptic functional site YTIYVIAL, termed FNIII14 within the 14th FN type III repeat (Figure 3). FNIII14 was shown to attenuate the TNIIIA2-induced aggressive phenotype of glioblastoma cells through β1-integrin inactivation as well as delayed glioblastoma growth in a mouse xenograft model. Another proteolytic fragment of fibronectin (Figure 3) secreted by bone marrow-resident mesenchymal stromal cells induced chemotaxis of prostate cancer cells via classic fibronectin-binding integrins α5β1. It was supposed that proteolytic fragments of fibronectin may function as matrikines in the bone marrow niche and are involved in seed-and-soil mechanisms of disease progression.

51Elastin is highly resistant to proteolysis and shows essentially no turnover in healthy tissues. However, MMPs, aspartic proteases, serine proteases and cysteine proteases can fragment elastin to elastin peptides under several pathological processes, and elastin fragments can, in turn, activate MMPs (reviewed in). In melanoma, fragmentation of elastin was found to occur at the invasive front of the tumor. Elastin fragments enhanced MMP-2 and MMP-14 production by melanoma cells that allowed further melanoma cell invasion through a type I collagen matrix by upregulating MMP-2 expression and activation.

52Two categories of elastin-derived peptides have been described: Val-Gly-Val-Ala-Pro-Gly (VGVAPG, VG-6) with a xGxxPG consensus and Ala-Gly-Val-Pro-Gly-Leu-Gly-Val-Gly (AGVPGLGVG, AG-9) with the xGxPGxGxG consensus sequence. Elastin peptide VGVAPG has been shown to stimulate fibrosarcoma cell invasion through the activation of MMP-2 and uPA, upregulate MMP-14 and stimulate the angiogenic phenotype of endothelial cells and increase the invasiveness of lung cancer cells by post-transcriptional regulation of MMP-2 and uPA. VGVAPG increased the migration of melanoma cells and the generation of elastin-derived peptides, enhancing the expression of elastin-degrading MMP-2 and MMP-3 through binding to galectin-3 and EBP receptors. VGVAPG also increased cells attachment and the expression of major adhesion molecules CD44, ICAM-1 and NCAM on melanoma cells through galectin-3 and integrin αvβ3 receptors. The other peptide, AG-9, has been also shown to induce tumor growth, MMP-2 and uPA secretion, cell migration and cell adhesion. The pro-invasive effects of AG-9 in squamous carcinoma cells were mediated through the ribosomal protein SA (RPSA) receptor.

6. Future Perspectives and Approaches in ECM Research

53As outlined above, there are numerous publications implicating ECM proteins in cancer progression. We would like to outline here the main directions and methodological approaches for studying the role of ECM proteins in cancer.

6.1. Animal Models

54In future experiments, experimental mouse models have to be established to further prove the functional role of ECM proteins in the process of tumor metastasis. There have been already several knockdown experiments of ECM proteins performed and analyzed in xenotransplantation mouse models. Recently, knockdown of tenascin-C in a human gastric cancer cell line has been shown to be implicated in the process of epithelial-mesenchymal transition and inhibited subcutaneous tumor growth and peritoneal metastasis in a xenotransplantation mouse model in vivo. In further experiments, tissue-specific knockouts by using e.g., the Cre/LoxP system have to be made in order to analyze the tissue-specific function of ECM proteins during the process of metastasis in distinct organs. Alternatively, by using the same Cre/LoxP system, tissue-specific overexpression of ECM proteins can be induced in order to analyze their functional role in metastasis.

55An additional aspect is the functional role of the tumor microenvironment in mediating the functional role of ECM proteins. As outlined above, distinct signaling processes have been implicated in the functional role of ECM proteins in mediating the metastatic process. Therefore, distinct conditional and/or organ-specific knockout mice with deletions in the proposed signaling molecules like EGF receptors, WNT signaling, RAS-RAF-MAPK and PI3K-AKT-mTOR signal transduction have to be used to further pin down these signaling events in the tumor-infiltrating stroma cells after metastasis in distinct organs.

56As we have already mentioned, there is a close interplay between tumor cells and the surrounding microenvironment. Tumors, arising from a single cell, gradually develop into heterogeneous cancer cell populations. Thus, mouse models can also be used to study tumor heterogeneity. By using red, green, blue (RGB) marking as a lentiviral multi-color clonal cell tracking technology, the clonal development of subpopulations within tumors and metastases can be analyzed after transplantation of the RGB marked cells in mice. The combination of RGB marking with immunohistochemical staining of distinct ECM proteins with fluorescently labeled antibodies will give additional information of the functional role of ECM proteins during the process of clonal development in tumorigenesis and/or metastasis.

6.2. Proteomic Approach

57By analyzing the structure and functions of ECM, the proteomics-based and bioinformatic methods are undoubtedly needed to be mentioned. Proteomic characterization of matrisomes (“a list of all the proteins in any given matrix”) or integrin adhesomes can be performed using mass spectrometry methods.

6.3. Imaging Technologies

58ECM, and especially cancerized ECM, can be characterized not only by the protein composition and spatial organization but also by such a parameter as stiffness. As it was mentioned in the review, ECM remodeling, driven by proteolytic enzymes and cross-linking enzymes results in increased stiffness of ECM surrounding the tumor. Sometimes conventional cell and molecular biology methods are not enough to characterize complex physico-chemical properties of ECM in cancer.

59High-resolution microscopy techniques, for instance, second harmonic generation (SHG) or coherent anti-Stokes Raman scattering (CARS), are successfully used to quantify tissue structural changes during cancer progression. It was also reported about the combined use of SHG microscopy and mass spectrometry.

6.4. 3D Cell Models and Tissue Engineering

60Engineering approaches can be used to examine the effects of tumor-associated alterations in the ECM or ECM composition. To explore the molecular mechanisms of tumor progression and metastasis, 3D cancer models can be used for the imitation of key steps of cancer dissemination (invasion, intravasation and angiogenesis). The decellularized matrix allows a comprehensive study of the ECM role in the regulation of cancer cell behavior.

7. Conclusions

61In this review we have presented a picture of the versatile role of ECM proteins in cancer progression. Researchers focus now not only on the intrinsic properties of cancer cells and consider cancer not only as a disease of uncontrolled cell proliferation, but as a complex interplay of cancer and stromal cells in the dysregulated microenvironment.

62To understand the mechanisms of ECM deregulation in cancer, it is crucial to elucidate the molecular basis of the cancer-dependent ECM remodeling, changes in gene expression and ECM composition, and the involvement of certain signaling pathways. Understanding the molecular mechanisms underlying survival, proliferation and invasion will help in the development of new therapeutic agents targeting tumor development and metastasis.

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96.
Ray A., Provenzano P.P. Aligned Forces: Origins and Mechanisms of Cancer Dissemination Guided by Extracellular Matrix Architecture. Curr. Opin. Cell Biol. 2021;72:63-71.
Not in our library10.1016/j.ceb.2021.05.004
97.
Dumont N., Liu B., Defilippis R.A., Chang H., Rabban J.T., Karnezis A.N., Tjoe J.A., Marx J., Parvin B., Tlsty T.D. Breast Fibroblasts Modulate Early Dissemination, Tumorigenesis, and Metastasis through Alteration of Extracellular Matrix Characteristics. Neoplasia. 2013;15:249-262.
Not in our library10.1593/neo.121950
98.
Levental K.R., Yu H., Kass L., Lakins J.N., Egeblad M., Erler J.T., Fong S.F.T., Csiszar K., Giaccia A., Weninger W., et al. Matrix Crosslinking Forces Tumor Progression by Enhancing Integrin Signaling. Cell. 2009;139:891-906.
Not in our library10.1016/j.cell.2009.10.027
99.
Chen W.T. Proteolytic Activity of Specialized Surface Protrusions Formed at Rosette Contact Sites of Transformed Cells. J. Exp. Zool. 1989;251:167-185.
Not in our library10.1002/jez.1402510206
100.
Artym V.V., Swatkoski S., Matsumoto K., Campbell C.B., Petrie R.J., Dimitriadis E.K., Li X., Mueller S.C., Bugge T.H., Gucek M., et al. Dense Fibrillar Collagen Is a Potent Inducer of Invadopodia via a Specific Signaling Network. J. Cell Biol. 2015;208:331-350.
Not in our library10.1083/jcb.201405099
101.
Juin A., Billottet C., Moreau V., Destaing O., Albiges-Rizo C., Rosenbaum J., Génot E., Saltel F. Physiological Type I Collagen Organization Induces the Formation of a Novel Class of Linear Invadosomes. Mol. Biol. Cell. 2012;23:297-309.
Not in our library10.1091/mbc.e11-07-0594
102.
Yan T., Zhang A., Shi F., Chang F., Mei J., Liu Y., Zhu Y. Integrin Avβ3-Associated DAAM1 Is Essential for Collagen-Induced Invadopodia Extension and Cell Haptotaxis in Breast Cancer Cells. J. Biol. Chem. 2018;293:10172-10185.
Not in our library10.1074/jbc.ra117.000327
103.
Azemikhah M., Ashtiani H.A., Aghaei M., Rastegar H. Evaluation of Discoidin Domain Receptor-2 (DDR2) Expression Level in Normal, Benign, and Malignant Human Prostate Tissues. Res. Pharm. Sci. 2015;10:356-363.
Not in our library
104.
Hur H., Ham I.-H., Lee D., Jin H., Aguilera K.Y., Oh H.J., Han S.-U., Kwon J.E., Kim Y.-B., Ding K., et al. Discoidin Domain Receptor 1 Activity Drives an Aggressive Phenotype in Gastric Carcinoma. BMC Cancer. 2017;17:87.
Not in our library10.1186/s12885-017-3051-9
105.
Jin H., Ham I.-H., Oh H.J., Bae C.A., Lee D., Kim Y.-B., Son S.-Y., Chwae Y.-J., Han S.-U., Brekken R.A., et al. Inhibition of Discoidin Domain Receptor 1 Prevents Stroma-Induced Peritoneal Metastasis in Gastric Carcinoma. Mol. Cancer Res. 2018;16:1590-1600.
Not in our library10.1158/1541-7786.mcr-17-0710
106.
Romayor I., Badiola I., Benedicto A., Márquez J., Herrero A., Arteta B., Olaso E. Silencing of Sinusoidal DDR1 Reduces Murine Liver Metastasis by Colon Carcinoma. Sci. Rep. 2020;10:18398.
Not in our library10.1038/s41598-020-75395-w
107.
Gadiya M., Chakraborty G. Signaling by Discoidin Domain Receptor 1 in Cancer Metastasis. Cell Adh. Migr. 2018;12:315-323.
Not in our library10.1080/19336918.2018.1520556
108.
Majo S., Auguste P. The Yin and Yang of Discoidin Domain Receptors (DDRs): Implications in Tumor Growth and Metastasis Development. Cancers. 2021;13:1725.
Not in our library10.3390/cancers13071725
109.
Mehta V., Chander H., Munshi A. Complex Roles of Discoidin Domain Receptor Tyrosine Kinases in Cancer. Clin. Transl. Oncol. 2021;23:1497-1510.
Not in our library10.1007/s12094-021-02552-6
110.
Collagens and Cancer associated fibroblasts in the reactive stroma and its relation to Cancer biology · 2019
No notice
111.
van Huizen N.A., Coebergh van den Braak R.R.J., Doukas M., Dekker L.J.M., IJzermans J.N.M., Luider T.M. Up-Regulation of Collagen Proteins in Colorectal Liver Metastasis Compared with Normal Liver Tissue. J. Biol. Chem. 2019;294:281-289.
Not in our library10.1074/jbc.ra118.005087
112.
Bourgot I., Primac I., Louis T., Noël A., Maquoi E. Reciprocal Interplay between Fibrillar Collagens and Collagen-Binding Integrins: Implications in Cancer Progression and Metastasis. Front. Oncol. 2020;10:1488.
Not in our library10.3389/fonc.2020.01488
113.
Ferreira A.R., Alho I., Shan N., Matias M., Faria M., Casimiro S., Leitzel K., Ali S., Lipton A., Costa L. N-Telopeptide of Type I Collagen Long-Term Dynamics in Breast Cancer Patients with Bone Metastases: Clinical Outcomes and Influence of Extraskeletal Metastases. Oncologist. 2016;21:1418-1426.
Not in our library10.1634/theoncologist.2015-0527
114.
Hall C.L., Dai J., van Golen K.L., Keller E.T., Long M.W. Type I Collagen Receptor (Alpha 2 Beta 1) Signaling Promotes the Growth of Human Prostate Cancer Cells within the Bone. Cancer Res. 2006;66:8648-8654.
Not in our library10.1158/0008-5472.can-06-1544
115.
Brooks M., Mo Q., Krasnow R., Ho P.L., Lee Y.-C., Xiao J., Kurtova A., Lerner S., Godoy G., Jian W., et al. Positive Association of Collagen Type I with Non-Muscle Invasive Bladder Cancer Progression. Oncotarget. 2016;7:82609-82619.
Not in our library10.18632/oncotarget.12089
116.
Huang C., Yang X., Han L., Fan Z., Liu B., Zhang C., Lu T. The Prognostic Potential of Alpha-1 Type I Collagen Expression in Papillary Thyroid Cancer. Biochem. Biophys. Res. Commun. 2019;515:125-132.
Not in our library10.1016/j.bbrc.2019.04.119
117.
Hou L., Lin T., Wang Y., Liu B., Wang M. Collagen Type 1 Alpha 1 Chain Is a Novel Predictive Biomarker of Poor Progression-Free Survival and Chemoresistance in Metastatic Lung Cancer. J. Cancer. 2021;12:5723-5731.
Not in our library10.7150/jca.59723
118.
Elevated collagen-I augments tumor progressive signals, intravasation and metastasis of prolactin-induced estrogen receptor alpha positive mammary tumor cells · 2017
No notice
119.
Yamazaki S., Higuchi Y., Ishibashi M., Hashimoto H., Yasunaga M., Matsumura Y., Tsuchihara K., Tsuboi M., Goto K., Ochiai A., et al. Collagen Type I Induces EGFR-TKI Resistance in EGFR-Mutated Cancer Cells by MTOR Activation through Akt-Independent Pathway. Cancer Sci. 2018;109:2063-2073.
Not in our library10.1111/cas.13624
120.
Yamazaki S., Su Y., Maruyama A., Makinoshima H., Suzuki J., Tsuboi M., Goto K., Ochiai A., Ishii G. Uptake of Collagen Type I via Macropinocytosis Cause MTOR Activation and Anti-Cancer Drug Resistance. Biochem. Biophys. Res. Commun. 2020;526:191-198.
Not in our library10.1016/j.bbrc.2020.03.067
121.
Nah H.D., Barembaum M., Upholt W.B. The Chicken Alpha 1 (XI) Collagen Gene Is Widely Expressed in Embryonic Tissues. J. Biol. Chem. 1992;267:22581-22586.
Not in our library10.1016/s0021-9258(18)41712-7
122.
Mendler M., Eich-Bender S.G., Vaughan L., Winterhalter K.H., Bruckner P. Cartilage Contains Mixed Fibrils of Collagen Types II, IX, and XI. J. Cell Biol. 1989;108:191-197.
Not in our library10.1083/jcb.108.1.191
123.
Jia D., Liu Z., Deng N., Tan T.Z., Huang R.Y.-J., Taylor-Harding B., Cheon D.-J., Lawrenson K., Wiedemeyer W.R., Walts A.E., et al. A COL11A1-Correlated Pan-Cancer Gene Signature of Activated Fibroblasts for the Prioritization of Therapeutic Targets. Cancer Lett. 2016;382:203-214.
Not in our library10.1016/j.canlet.2016.09.001
124.
Overexpression of COL11A1 by cancer-associated fibroblasts: clinical relevance of a stromal marker in pancreatic cancer. · 2013
Not checked
125.
Cheon D.-J., Tong Y., Sim M.-S., Dering J., Berel D., Cui X., Lester J., Beach J.A., Tighiouart M., Walts A.E., et al. A Collagen-Remodeling Gene Signature Regulated by TGF-β Signaling Is Associated with Metastasis and Poor Survival in Serous Ovarian Cancer. Clin. Cancer Res. 2014;20:711-723.
Not in our library10.1158/1078-0432.ccr-13-1256
126.
Wu Y.-H., Chang T.-H., Huang Y.-F., Huang H.-D., Chou C.-Y. COL11A1 Promotes Tumor Progression and Predicts Poor Clinical Outcome in Ovarian Cancer. Oncogene. 2014;33:3432-3440.
Not in our library10.1038/onc.2013.307
127.
Wu Y.-H., Huang Y.-F., Chang T.-H., Chen C.-C., Wu P.-Y., Huang S.-C., Chou C.-Y. COL11A1 Activates Cancer-Associated Fibroblasts by Modulating TGF-Β3 through the NF-ΚB/IGFBP2 Axis in Ovarian Cancer Cells. Oncogene. 2021;40:4503-4519.
Not in our library10.1038/s41388-021-01865-8
128.
Raglow Z., Thomas S.M. Tumor Matrix Protein Collagen XIα1 in Cancer. Cancer Lett. 2015;357:448-453.
Not in our library10.1016/j.canlet.2014.12.011
129.
Liu Z., Lai J., Jiang H., Ma C., Huang H. Collagen XI Alpha 1 Chain, a Potential Therapeutic Target for Cancer. FASEB J. 2021;35:e21603.
Not in our library10.1096/fj.202100054rr
130.
Lee C.S., Siprashvili Z., Mah A., Bencomo T., Elcavage L.E., Che Y., Shenoy R.M., Aasi S.Z., Khavari P.A. Mutant Collagen COL11A1 Enhances Cancerous Invasion. Oncogene. 2021;40:6299-6307.
Not in our library10.1038/s41388-021-02013-y
131.
Nallanthighal S., Heiserman J.P., Cheon D.-J. Collagen Type XI Alpha 1 (COL11A1): A Novel Biomarker and a Key Player in Cancer. Cancers. 2021;13:935.
Not in our library10.3390/cancers13050935
132.
Wang H., Ren R., Yang Z., Cai J., Du S., Shen X. The COL11A1/Akt/CREB Signaling Axis Enables Mitochondrial-Mediated Apoptotic Evasion to Promote Chemoresistance in Pancreatic Cancer Cells through Modulating BAX/BCL-2 Function. J. Cancer. 2021;12:1406-1420.
Not in our library10.7150/jca.47032
133.
Nissen N.I., Kehlet S., Johansen A.Z., Chen I.M., Karsdal M., Johansen J.S., Diab H.M.H., Jørgensen L.N., Sun S., Manon-Jensen T., et al. Noninvasive Prognostic Biomarker Potential of Quantifying the Propeptides of Type XI Collagen Alpha-1 Chain (PRO-C11) in Patients with Pancreatic Ductal Adenocarcinoma. Int. J. Cancer. 2021;149:228-238.
Not in our library10.1002/ijc.33551
134.
Wang J., Jiang Y.-H., Yang P.-Y., Liu F. Increased Collagen Type V A2 (COL5A2) in Colorectal Cancer Is Associated with Poor Prognosis and Tumor Progression. OncoTargets Ther. 2021;14:2991-3002.
Not in our library10.2147/ott.s288422
135.
Huang G., Ge G., Izzi V., Greenspan D.S. A3 Chains of Type V Collagen Regulate Breast Tumour Growth via Glypican-1. Nat. Commun. 2017;8:14351.
Not in our library10.1038/ncomms14351
136.
Chen H.-C., Tseng Y.-K., Shu C.-W., Weng T.-J., Liou H.-H., Yen L.-M., Hsieh I.-C., Wang C.-C., Wu P.-C., Shiue Y.-L., et al. Differential Clinical Significance of COL5A1 and COL5A2 in Tongue Squamous Cell Carcinoma. J. Oral. Pathol. Med. 2019;48:468-476.
Not in our library10.1111/jop.12861
137.
Tan Y., Chen Q., Xing Y., Zhang C., Pan S., An W., Xu H. High Expression of COL5A2, a Member of COL5 Family, Indicates the Poor Survival and Facilitates Cell Migration in Gastric Cancer. Biosci. Rep. 2021;41:BSR20204293.
Not in our library10.1042/bsr20204293
138.
Cescon M., Gattazzo F., Chen P., Bonaldo P. Collagen VI at a Glance. J. Cell Sci. 2015;128:3525-3531.
Not in our library10.1242/jcs.169748
139.
Williams L., Layton T., Yang N., Feldmann M., Nanchahal J. Collagen VI as a Driver and Disease Biomarker in Human Fibrosis. FEBS J. 2021.
Not in our library10.1111/febs.16039
140.
Iyengar P., Espina V., Williams T.W., Lin Y., Berry D., Jelicks L.A., Lee H., Temple K., Graves R., Pollard J., et al. Adipocyte-Derived Collagen VI Affects Early Mammary Tumor Progression In Vivo, Demonstrating a Critical Interaction in the Tumor/Stroma Microenvironment. J. Clin. Investig. 2005;115:1163-1176.
Not in our library10.1172/jci23424
141.
Chen P., Cescon M., Bonaldo P. Collagen VI in Cancer and Its Biological Mechanisms. Trends. Mol. Med. 2013;19:410-417.
Not in our library10.1016/j.molmed.2013.04.001
142.
Ho C.-M., Chang T.-H., Yen T.-L., Hong K.-J., Huang S.-H. Collagen Type VI Regulates the CDK4/6-p-Rb Signaling Pathway and Promotes Ovarian Cancer Invasiveness, Stemness, and Metastasis. Am. J. Cancer Res. 2021;11:668-690.
Not in our library
143.
Duan Y., Liu G., Sun Y., Wu J., Xiong Z., Jin T., Chen M. Collagen Type VI A5 Gene Variations May Predict the Risk of Lung Cancer Development in Chinese Han Population. Sci. Rep. 2020;10:5010.
Not in our library10.1038/s41598-020-61614-x
144.
Sato T., Tokunaka K., Saiga K., Tomura A., Sugihara H., Hayashi T., Imamura Y., Morita M. Involvement of Non-triple Helical Type VI Collagen A1 Chain, NTH A1(VI), in the Proliferation of Cancer Cells. Oncol. Rep. 2020;44:2297-2305.
Not in our library10.3892/or.2020.7734
145.
Owusu-Ansah K.G., Song G., Chen R., Edoo M.I.A., Li J., Chen B., Wu J., Zhou L., Xie H., Jiang D., et al. COL6A1 Promotes Metastasis and Predicts Poor Prognosis in Patients with Pancreatic Cancer. Int. J. Oncol. 2019;55:391-404.
Not in our library10.3892/ijo.2019.4825
146.
Park J., Scherer P.E. Adipocyte-Derived Endotrophin Promotes Malignant Tumor Progression. J. Clin. Investig. 2012;122:4243-4256.
Not in our library10.1172/jci63930
147.
Wang J., Pan W. The Biological Role of the Collagen Alpha-3 (VI) Chain and Its Cleaved C5 Domain Fragment Endotrophin in Cancer. OncoTargets. Ther. 2020;13:5779-5793.
Not in our library10.2147/ott.s256654
148.
Bu D., Crewe C., Kusminski C.M., Gordillo R., Ghaben A.L., Kim M., Park J., Deng H., Xiong W., Liu X.-Z., et al. Human Endotrophin as a Driver of Malignant Tumor Growth. JCI Insight. 2019;5:125094.
Not in our library10.1172/jci.insight.125094
149.
Kim M.-S., Ha S.-E., Wu M., Zogg H., Ronkon C.F., Lee M.-Y., Ro S. Extracellular Matrix Biomarkers in Colorectal Cancer. Int. J. Mol. Sci. 2021;22:9185.
Not in our library10.3390/ijms22179185
150.
Qin Y., Rodin S., Simonson O.E., Hollande F. Laminins and Cancer Stem Cells: Partners in Crime? Semin. Cancer Biol. 2017;45:3-12.
Not in our library10.1016/j.semcancer.2016.07.004
151.
Maltseva D.V., Rodin S.A. Laminins in Metastatic Cancer. Mol. Biol. 2018;52:411-434.
Not in our library10.1134/s0026893318030093
152.
Rousselle P., Scoazec J.Y. Laminin 332 in Cancer: When the Extracellular Matrix Turns Signals from Cell Anchorage to Cell Movement. Semin. Cancer Biol. 2020;62:149-165.
Not in our library10.1016/j.semcancer.2019.09.026
153.
Zahir N., Lakins J.N., Russell A., Ming W., Chatterjee C., Rozenberg G.I., Marinkovich M.P., Weaver V.M. Autocrine Laminin-5 Ligates Alpha6beta4 Integrin and Activates RAC and NFkappaB to Mediate Anchorage-Independent Survival of Mammary Tumors. J. Cell Biol. 2003;163:1397-1407.
Not in our library10.1083/jcb.200302023
154.
Manohar A., Shome S.G., Lamar J., Stirling L., Iyer V., Pumiglia K., DiPersio C.M. Alpha 3 Beta 1 Integrin Promotes Keratinocyte Cell Survival through Activation of a MEK/ERK Signaling Pathway. J. Cell Sci. 2004;117:4043-4054.
Not in our library10.1242/jcs.01277
155.
Carpenter P.M., Dao A.V., Arain Z.S., Chang M.K., Nguyen H.P., Arain S., Wang-Rodriguez J., Kwon S.-Y., Wilczynski S.P. Motility Induction in Breast Carcinoma by Mammary Epithelial Laminin 332 (Laminin 5). Mol. Cancer Res. 2009;7:462-475.
Not in our library10.1158/1541-7786.mcr-08-0148
156.
Ramovs V., Te Molder L., Sonnenberg A. The Opposing Roles of Laminin-Binding Integrins in Cancer. Matrix Biol. 2017;57–58:213-243.
Not in our library10.1016/j.matbio.2016.08.007
157.
Kato K., Shiga K., Yamaguchi K., Hata K., Kobayashi T., Miyazaki K., Saijo S., Miyagi T. Plasma-Membrane-Associated Sialidase (NEU3) Differentially Regulates Integrin-Mediated Cell Proliferation through Laminin- and Fibronectin-Derived Signalling. Biochem. J. 2006;394:647-656.
Not in our library10.1042/bj20050737
158.
Aoki S., Nakanishi Y., Akimoto S., Moriya Y., Yoshimura K., Kitajima M., Sakamoto M., Hirohashi S. Prognostic Significance of Laminin-5 Gamma2 Chain Expression in Colorectal Carcinoma: Immunohistochemical Analysis of 103 Cases. Dis. Colon. Rectum. 2002;45:1520-1527.
Not in our library10.1007/s10350-004-6460-1
159.
Ito E., Ozawa S., Kijima H., Kazuno A., Miyako H., Nishi T., Chino O., Shimada H., Tanaka M., Inoue S., et al. Clinicopathological Significance of Laminin-5γ2 Chain Expression in Superficial Esophageal Cancer. Dis. Esophagus. 2014;27:463-469.
Not in our library10.1111/j.1442-2050.2012.01416.x
160.
Koshikawa N., Giannelli G., Cirulli V., Miyazaki K., Quaranta V. Role of Cell Surface Metalloprotease MT1-MMP in Epithelial Cell Migration over Laminin-5. J. Cell Biol. 2000;148:615-624.
Not in our library10.1083/jcb.148.3.615
161.
Gilles C., Polette M., Coraux C., Tournier J.M., Meneguzzi G., Munaut C., Volders L., Rousselle P., Birembaut P., Foidart J.M. Contribution of MT1-MMP and of Human Laminin-5 Gamma2 Chain Degradation to Mammary Epithelial Cell Migration. J. Cell Sci. 2001;114:2967-2976.
Not in our library10.1242/jcs.114.16.2967
162.
Giannelli G., Falk-Marzillier J., Schiraldi O., Stetler-Stevenson W.G., Quaranta V. Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5. Science. 1997;277:225-228.
Not in our library10.1126/science.277.5323.225
163.
Schenk S., Hintermann E., Bilban M., Koshikawa N., Hojilla C., Khokha R., Quaranta V. Binding to EGF Receptor of a Laminin-5 EGF-like Fragment Liberated during MMP-Dependent Mammary Gland Involution. J. Cell Biol. 2003;161:197-209.
Not in our library10.1083/jcb.200208145
164.
Engel J., Odermatt E., Engel A., Madri J.A., Furthmayr H., Rohde H., Timpl R. Shapes, Domain Organizations and Flexibility of Laminin and Fibronectin, Two Multifunctional Proteins of the Extracellular Matrix. J. Mol. Biol. 1981;150:97-120.
Not in our library10.1016/0022-2836(81)90326-0
165.
Hynes R.O., Yamada K.M. Fibronectins: Multifunctional Modular Glycoproteins. J. Cell Biol. 1982;95:369-377.
Not in our library10.1083/jcb.95.2.369
166.
Kornblihtt A.R., Umezawa K., Vibe-Pedersen K., Baralle F.E. Primary Structure of Human Fibronectin: Differential Splicing May Generate at Least 10 Polypeptides from a Single Gene. EMBO J. 1985;4:1755-1759.
Not in our library10.1002/j.1460-2075.1985.tb03847.x
167.
Owens R.J., Kornblihtt A.R., Baralle F.E. Fibronectin, the Generation of Multiple Polypeptides from a Single Gene. Oxf. Surv. Eukaryot. Genes. 1986;3:141-160.
Not in our library
168.
Schwarzbauer J.E., Tamkun J.W., Lemischka I.R., Hynes R.O. Three Different Fibronectin MRNAs Arise by Alternative Splicing within the Coding Region. Cell. 1983;35:421-431.
Not in our library10.1016/0092-8674(83)90175-7
169.
Yamada K.M., Kennedy D.W. Fibroblast Cellular and Plasma Fibronectins Are Similar but Not Identical. J. Cell Biol. 1979;80:492-498.
Not in our library10.1083/jcb.80.2.492
170.
Fibronectin: Molecular Structure, Fibrillar Structure and Mechanochemical Signaling · 2021
No notice
171.
Tamkun J.W., Hynes R.O. Plasma Fibronectin Is Synthesized and Secreted by Hepatocytes. J. Biol. Chem. 1983;258:4641-4647.
Not in our library10.1016/s0021-9258(18)32672-3
172.
Mao Y., Schwarzbauer J.E. Fibronectin Fibrillogenesis, a Cell-Mediated Matrix Assembly Process. Matrix Biol. 2005;24:389-399.
Not in our library10.1016/j.matbio.2005.06.008
173.
Plasma and cellular fibronectin: distinct and independent functions during tissue repair · 2011
No notice
174.
Fibronectin-guided migration of carcinoma collectives · 2017
No notice
175.
Rick J.W., Chandra A., Dalle Ore C., Nguyen A.T., Yagnik G., Aghi M.K. Fibronectin in Malignancy: Cancer-Specific Alterations, Protumoral Effects, and Therapeutic Implications. Semin. Oncol. 2019;46:284-290.
Not in our library10.1053/j.seminoncol.2019.08.002
176.
SMART: recent updates, new developments and status in 2020 · 2020
No notice
177.
Pankov R., Yamada K.M. Fibronectin at a Glance. J. Cell Sci. 2002;115:3861-3863.
Not in our library10.1242/jcs.00059
178.
Schwarzbauer J.E., Paul J.I., Hynes R.O. On the Origin of Species of Fibronectin. Proc. Natl. Acad. Sci. USA. 1985;82:1424-1428.
Not in our library10.1073/pnas.82.5.1424
179.
Vaidya A., Wang H., Qian V., Gilmore H., Lu Z.-R. Overexpression of Extradomain-B Fibronectin Is Associated with Invasion of Breast Cancer Cells. Cells. 2020;9:1826.
Not in our library10.3390/cells9081826
180.
Birchler M.T., Milisavlijevic D., Pfaltz M., Neri D., Odermatt B., Schmid S., Stoeckli S.J. Expression of the Extra Domain B of Fibronectin, a Marker of Angiogenesis, in Head and Neck Tumors. Laryngoscope. 2003;113:1231-1237.
Not in our library10.1097/00005537-200307000-00023
181.
Kujawa K.A., Zembala-Nożyńska E., Cortez A.J., Kujawa T., Kupryjańczyk J., Lisowska K.M. Fibronectin and Periostin as Prognostic Markers in Ovarian Cancer. Cells. 2020;9:149.
Not in our library10.3390/cells9010149
182.
Locher R., Erba P.A., Hirsch B., Bombardieri E., Giovannoni L., Neri D., Dürkop H., Menssen H.D. Abundant in Vitro Expression of the Oncofetal ED-B-Containing Fibronectin Translates into Selective Pharmacodelivery of (131)I-L19SIP in a Prostate Cancer Patient. J. Cancer Res. Clin. Oncol. 2014;140:35-43.
Not in our library10.1007/s00432-013-1538-6
183.
Vaidya A., Ayat N., Buford M., Wang H., Shankardass A., Zhao Y., Gilmore H., Wang Z., Lu Z.-R. Noninvasive Assessment and Therapeutic Monitoring of Drug-Resistant Colorectal Cancer by MR Molecular Imaging of Extradomain-B Fibronectin. Theranostics. 2020;10:11127-11143.
Not in our library10.7150/thno.47448
184.
Xiao J., Yang W., Xu B., Zhu H., Zou J., Su C., Rong J., Wang T., Chen Z. Expression of Fibronectin in Esophageal Squamous Cell Carcinoma and Its Role in Migration. BMC Cancer. 2018;18:976.
Not in our library10.1186/s12885-018-4850-3
185.
Fibronectin in Cancer: Friend or Foe · 2019
No notice
186.
Shaping Up the Tumor Microenvironment With Cellular Fibronectin · 2020
No notice
187.
Fibronectin as a multiregulatory molecule crucial in tumor matrisome: from structural and functional features to clinical practice in oncology · 2021
No notice
188.
Topalovski M., Brekken R.A. Matrix Control of Pancreatic Cancer: New Insights into Fibronectin Signaling. Cancer Lett. 2016;381:252-258.
Not in our library10.1016/j.canlet.2015.12.027
189.
Vaquero E.C., Edderkaoui M., Nam K.J., Gukovsky I., Pandol S.J., Gukovskaya A.S. Extracellular Matrix Proteins Protect Pancreatic Cancer Cells from Death via Mitochondrial and Nonmitochondrial Pathways. Gastroenterology. 2003;125:1188-1202.
Not in our library10.1016/s0016-5085(03)01203-4
190.
Edderkaoui M., Hong P., Vaquero E.C., Lee J.K., Fischer L., Friess H., Buchler M.W., Lerch M.M., Pandol S.J., Gukovskaya A.S. Extracellular Matrix Stimulates Reactive Oxygen Species Production and Increases Pancreatic Cancer Cell Survival through 5-Lipoxygenase and NADPH Oxidase. Am. J. Physiol. Gastrointest. Liver Physiol. 2005;289:G1137-G1147.
Not in our library10.1152/ajpgi.00197.2005
191.
Edderkaoui M., Hong P., Lee J.K., Pandol S.J., Gukovskaya A.S. Insulin-like Growth Factor-I Receptor Mediates the Prosurvival Effect of Fibronectin. J. Biol. Chem. 2007;282:26646-26655.
Not in our library10.1074/jbc.m702836200
192.
Han S., Khuri F.R., Roman J. Fibronectin Stimulates Non-Small Cell Lung Carcinoma Cell Growth through Activation of Akt/Mammalian Target of Rapamycin/S6 Kinase and Inactivation of LKB1/AMP-Activated Protein Kinase Signal Pathways. Cancer Res. 2006;66:315-323.
Not in our library10.1158/0008-5472.can-05-2367
193.
Cao Y., Liu X., Lu W., Chen Y., Wu X., Li M., Wang X.-A., Zhang F., Jiang L., Zhang Y., et al. Fibronectin Promotes Cell Proliferation and Invasion through MTOR Signaling Pathway Activation in Gallbladder Cancer. Cancer Lett. 2015;360:141-150.
Not in our library10.1016/j.canlet.2015.01.041
194.
Ou Y.-C., Li J.-R., Wang J.-D., Chang C.-Y., Wu C.-C., Chen W.-Y., Kuan Y.-H., Liao S.-L., Lu H.-C., Chen C.-J. Fibronectin Promotes Cell Growth and Migration in Human Renal Cell Carcinoma Cells. Int. J. Mol. Sci. 2019;20:2792.
Not in our library10.3390/ijms20112792
195.
Han S., Sidell N., Roman J. Fibronectin Stimulates Human Lung Carcinoma Cell Proliferation by Suppressing P21 Gene Expression via Signals Involving Erk and Rho Kinase. Cancer Lett. 2005;219:71-81.
Not in our library10.1016/j.canlet.2004.07.040
196.
Zhong C., Tao B., Tang F., Yang X., Peng T., You J., Xia K., Xia X., Chen L., Peng L. Remodeling Cancer Stemness by Collagen/Fibronectin via the AKT and CDC42 Signaling Pathway Crosstalk in Glioma. Theranostics. 2021;11:1991-2005.
Not in our library10.7150/thno.50613
197.
Extracellular Vesicles: An Emerging Mechanism Governing the Secretion and Biological Roles of Tenascin-C · 2021
Not checked
198.
Théry C., Witwer K.W., Aikawa E., Alcaraz M.J., Anderson J.D., Andriantsitohaina R., Antoniou A., Arab T., Archer F., Atkin-Smith G.K., et al. Minimal Information for Studies of Extracellular Vesicles 2018 (MISEV2018): A Position Statement of the International Society for Extracellular Vesicles and Update of the MISEV2014 Guidelines. J. Extracell. Vesicles. 2018;7:1535750.
Not in our library10.1080/20013078.2018.1535750
199.
van Niel G., D’Angelo G., Raposo G. Shedding Light on the Cell Biology of Extracellular Vesicles. Nat. Rev. Mol. Cell Biol. 2018;19:213-228.
Not in our library10.1038/nrm.2017.125
200.
Huleihel L., Hussey G.S., Naranjo J.D., Zhang L., Dziki J.L., Turner N.J., Stolz D.B., Badylak S.F. Matrix-Bound Nanovesicles within ECM Bioscaffolds. Sci. Adv. 2016;2:e1600502.
Not in our library10.1126/sciadv.1600502
201.
Urabe F., Patil K., Ramm G.A., Ochiya T., Soekmadji C. Extracellular Vesicles in the Development of Organ-Specific Metastasis. J. Extracell. Vesicles. 2021;10:e12125.
Not in our library10.1002/jev2.12125
202.
Stefanius K., Servage K., Orth K. Exosomes in Cancer Development. Curr. Opin. Genet. Dev. 2021;66:83-92.
Not in our library10.1016/j.gde.2020.12.018
203.
Schubert A., Boutros M. Extracellular Vesicles and Oncogenic Signaling. Mol. Oncol. 2021;15:3-26.
Not in our library10.1002/1878-0261.12855
204.
Hussey G.S., Pineda Molina C., Cramer M.C., Tyurina Y.Y., Tyurin V.A., Lee Y.C., El-Mossier S.O., Murdock M.H., Timashev P.S., Kagan V.E., et al. Lipidomics and RNA Sequencing Reveal a Novel Subpopulation of Nanovesicle within Extracellular Matrix Biomaterials. Sci. Adv. 2020;6:eaay4361.
Not in our library10.1126/sciadv.aay4361
205.
Quijano L.M., Naranjo J.D., El-Mossier S.O., Turner N.J., Pineda Molina C., Bartolacci J., Zhang L., White L., Li H., Badylak S.F. Matrix-Bound Nanovesicles: The Effects of Isolation Method upon Yield, Purity, and Function. Tissue. Eng. Part. C Methods. 2020;26:528-540.
Not in our library10.1089/ten.tec.2020.0243
206.
Chanda D., Otoupalova E., Hough K.P., Locy M.L., Bernard K., Deshane J.S., Sanderson R.D., Mobley J.A., Thannickal V.J. Fibronectin on the Surface of Extracellular Vesicles Mediates Fibroblast Invasion. Am. J. Respir. Cell Mol. Biol. 2019;60:279-288.
Not in our library10.1165/rcmb.2018-0062oc
207.
von Au A., Vasel M., Kraft S., Sens C., Hackl N., Marx A., Stroebel P., Hennenlotter J., Todenhöfer T., Stenzl A., et al. Circulating Fibronectin Controls Tumor Growth. Neoplasia. 2013;15:925-938.
Not in our library10.1593/neo.13762
208.
Zhang Y., Lu H., Dazin P., Kapila Y. Squamous Cell Carcinoma Cell Aggregates Escape Suspension-Induced, P53-Mediated Anoikis: Fibronectin and integrin αv mediate survival signals through focal adhesion kinase. J. Biol. Chem. 2004;279:48342-48349.
Not in our library10.1074/jbc.m407953200
209.
Han H.-J., Sung J.Y., Kim S.-H., Yun U.-J., Kim H., Jang E.-J., Yoo H.-E., Hong E.K., Goh S.-H., Moon A., et al. Fibronectin Regulates Anoikis Resistance via Cell Aggregate Formation. Cancer Lett. 2021;508:59-72.
Not in our library10.1016/j.canlet.2021.03.011
210.
Inhibition of fibronectin accumulation suppresses tumor growth · 2021
Not checked
211.
Chiquet M., Fambrough D.M. Chick Myotendinous Antigen. I. A Monoclonal Antibody as a Marker for Tendon and Muscle Morphogenesis. J. Cell Biol. 1984;98:1926-1936.
Not in our library10.1083/jcb.98.6.1926
212.
Erickson H.P., Inglesias J.L. A Six-Armed Oligomer Isolated from Cell Surface Fibronectin Preparations. Nature. 1984;311:267-269.
Not in our library10.1038/311267a0
213.
Grumet M., Hoffman S., Crossin K.L., Edelman G.M. Cytotactin, an Extracellular Matrix Protein of Neural and Non-Neural Tissues That Mediates Glia-Neuron Interaction. Proc. Natl. Acad. Sci. USA. 1985;82:8075-8079.
Not in our library10.1073/pnas.82.23.8075
214.
Kruse J., Keilhauer G., Faissner A., Timpl R., Schachner M. The J1 Glycoprotein--a Novel Nervous System Cell Adhesion Molecule of the L2/HNK-1 Family. Nature. 1985;316:146-148.
Not in our library10.1038/316146a0
215.
Jones F.S., Jones P.L. The Tenascin Family of ECM Glycoproteins: Structure, Function, and Regulation during Embryonic Development and Tissue Remodeling. Dev. Dyn. 2000;218:235-259.
Not in our library10.1002/(sici)1097-0177(200006)218:2<235::aid-dvdy2>3.0.co;2-g
216.
Chiquet M., Fambrough D.M. Chick Myotendinous Antigen. II. A Novel Extracellular Glycoprotein Complex Consisting of Large Disulfide-Linked Subunits. J. Cell Biol. 1984;98:1937-1946.
Not in our library10.1083/jcb.98.6.1937
217.
Jones F.S., Hoffman S., Cunningham B.A., Edelman G.M. A Detailed Structural Model of Cytotactin: Protein Homologies, Alternative RNA Splicing, and Binding Regions. Proc. Natl. Acad. Sci. USA. 1989;86:1905-1909.
Not in our library10.1073/pnas.86.6.1905
218.
Jones F.S., Burgoon M.P., Hoffman S., Crossin K.L., Cunningham B.A., Edelman G.M. A CDNA Clone for Cytotactin Contains Sequences Similar to Epidermal Growth Factor-like Repeats and Segments of Fibronectin and Fibrinogen. Proc. Natl. Acad. Sci. USA. 1988;85:2186-2190.
Not in our library10.1073/pnas.85.7.2186
219.
Giblin S.P., Midwood K.S. Tenascin-C: Form versus Function. Cell Adh. Migr. 2015;9:48-82.
Not in our library10.4161/19336918.2014.987587
220.
Siri A., Knäuper V., Veirana N., Caocci F., Murphy G., Zardi L. Different Susceptibility of Small and Large Human Tenascin-C Isoforms to Degradation by Matrix Metalloproteinases. J. Biol. Chem. 1995;270:8650-8654.
Not in our library10.1074/jbc.270.15.8650
221.
Tucker R.P., Chiquet-Ehrismann R. Tenascin-C: Its Functions as an Integrin Ligand. Int. J. Biochem. Cell Biol. 2015;65:165-168.
Not in our library10.1016/j.biocel.2015.06.003
222.
Swindle C.S., Tran K.T., Johnson T.D., Banerjee P., Mayes A.M., Griffith L., Wells A. Epidermal Growth Factor (EGF)-like Repeats of Human Tenascin-C as Ligands for EGF Receptor. J. Cell Biol. 2001;154:459-468.
Not in our library10.1083/jcb.200103103
223.
Chiquet-Ehrismann R., Matsuoka Y., Hofer U., Spring J., Bernasconi C., Chiquet M. Tenascin Variants: Differential Binding to Fibronectin and Distinct Distribution in Cell Cultures and Tissues. Cell Regul. 1991;2:927-938.
Not in our library10.1091/mbc.2.11.927
224.
Chung C.Y., Zardi L., Erickson H.P. Binding of Tenascin-C to Soluble Fibronectin and Matrix Fibrils. J. Biol. Chem. 1995;270:29012-29017.
Not in our library10.1074/jbc.270.48.29012
225.
Midwood K.S., Chiquet M., Tucker R.P., Orend G. Tenascin-C at a Glance. J. Cell Sci. 2016;129:4321-4327.
Not in our library10.1242/jcs.190546
226.
Midwood K.S., Hussenet T., Langlois B., Orend G. Advances in Tenascin-C Biology. Cell Mol. Life Sci. 2011;68:3175-3199.
Not in our library10.1007/s00018-011-0783-6
227.
Chiquet-Ehrismann R., Mackie E.J., Pearson C.A., Sakakura T. Tenascin: An Extracellular Matrix Protein Involved in Tissue Interactions during Fetal Development and Oncogenesis. Cell. 1986;47:131-139.
Not in our library10.1016/0092-8674(86)90374-0
228.
Chiquet-Ehrismann R., Orend G., Chiquet M., Tucker R.P., Midwood K.S. Tenascins in Stem Cell Niches. Matrix Biol. 2014;37:112-123.
Not in our library10.1016/j.matbio.2014.01.007
229.
Chiovaro F., Chiquet-Ehrismann R., Chiquet M. Transcriptional Regulation of Tenascin Genes. Cell Adh. Migr. 2015;9:34-47.
Not in our library10.1080/19336918.2015.1008333
230.
Scherer C., Pfisterer L., Wagner A.H., Hödebeck M., Cattaruzza M., Hecker M., Korff T. Arterial Wall Stress Controls NFAT5 Activity in Vascular Smooth Muscle Cells. J. Am. Heart Assoc. 2014;3:e000626.
Not in our library10.1161/jaha.113.000626
231.
Yamamoto K., Dang Q.N., Kennedy S.P., Osathanondh R., Kelly R.A., Lee R.T. Induction of Tenascin-C in Cardiac Myocytes by Mechanical Deformation. Role of Reactive Oxygen Species. J. Biol. Chem. 1999;274:21840-21846.
Not in our library10.1074/jbc.274.31.21840
232.
Chiquet-Ehrismann R., Tannheimer M., Koch M., Brunner A., Spring J., Martin D., Baumgartner S., Chiquet M. Tenascin-C Expression by Fibroblasts Is Elevated in Stressed Collagen Gels. J. Cell Biol. 1994;127:2093-2101.
Not in our library10.1083/jcb.127.6.2093
233.
Jinnin M., Ihn H., Asano Y., Yamane K., Trojanowska M., Tamaki K. Tenascin-C Upregulation by Transforming Growth Factor-Beta in Human Dermal Fibroblasts Involves Smad3, Sp1, and Ets1. Oncogene. 2004;23:1656-1667.
Not in our library10.1038/sj.onc.1207064
234.
Pearson C.A., Pearson D., Shibahara S., Hofsteenge J., Chiquet-Ehrismann R. Tenascin: CDNA Cloning and Induction by TGF-Beta. EMBO J. 1988;7:2977-2982.
Not in our library10.1002/j.1460-2075.1988.tb03160.x
235.
Jinnin M., Ihn H., Asano Y., Yamane K., Trojanowska M., Tamaki K. Platelet Derived Growth Factor Induced Tenascin-C Transcription Is Phosphoinositide 3-Kinase/Akt-Dependent and Mediated by Ets Family Transcription Factors. J. Cell Physiol. 2006;206:718-727.
Not in our library10.1002/jcp.20527
236.
Lowy C.M., Oskarsson T. Tenascin C in Metastasis: A View from the Invasive Front. Cell Adh. Migr. 2015;9:112-124.
Not in our library10.1080/19336918.2015.1008331
237.
Silvers C.R., Messing E.M., Miyamoto H., Lee Y.-F. Tenascin-C Expression in the Lymph Node Pre-Metastatic Niche in Muscle-Invasive Bladder Cancer. Br. J. Cancer. 2021;125:1399-1407.
Not in our library10.1038/s41416-021-01554-z
238.
Ishihara A., Yoshida T., Tamaki H., Sakakura T. Tenascin Expression in Cancer Cells and Stroma of Human Breast Cancer and Its Prognostic Significance. Clin. Cancer Res. 1995;1:1035-1041.
Not in our library
239.
Modica C., Olivero M., Zuppini F., Milan M., Basilico C., Vigna E. HGF/MET Axis Induces Tumor Secretion of Tenascin-C and Promotes Stromal Rewiring in Pancreatic Cancer. Cancers. 2021;13:3519.
Not in our library10.3390/cancers13143519
240.
O’Connell J.T., Sugimoto H., Cooke V.G., MacDonald B.A., Mehta A.I., LeBleu V.S., Dewar R., Rocha R.M., Brentani R.R., Resnick M.B., et al. VEGF-A and Tenascin-C Produced by S100A4+ Stromal Cells Are Important for Metastatic Colonization. Proc. Natl. Acad. Sci. USA. 2011;108:16002-16007.
Not in our library10.1073/pnas.1109493108
241.
Oskarsson T., Acharyya S., Zhang X.H.-F., Vanharanta S., Tavazoie S.F., Morris P.G., Downey R.J., Manova-Todorova K., Brogi E., Massagué J. Breast Cancer Cells Produce Tenascin C as a Metastatic Niche Component to Colonize the Lungs. Nat. Med. 2011;17:867-874.
Not in our library10.1038/nm.2379
242.
Saupe F., Schwenzer A., Jia Y., Gasser I., Spenlé C., Langlois B., Kammerer M., Lefebvre O., Hlushchuk R., Rupp T., et al. Tenascin-C Downregulates Wnt Inhibitor Dickkopf-1, Promoting Tumorigenesis in a Neuroendocrine Tumor Model. Cell Rep. 2013;5:482-492.
Not in our library10.1016/j.celrep.2013.09.014
243.
Spenlé C., Gasser I., Saupe F., Janssen K.-P., Arnold C., Klein A., van der Heyden M., Mutterer J., Neuville-Méchine A., Chenard M.-P., et al. Spatial Organization of the Tenascin-C Microenvironment in Experimental and Human Cancer. Cell Adh. Migr. 2015;9:4-13.
Not in our library10.1080/19336918.2015.1005452
244.
Sun Z., Velázquez-Quesada I., Murdamoothoo D., Ahowesso C., Yilmaz A., Spenlé C., Averous G., Erne W., Oberndorfer F., Oszwald A., et al. Tenascin-C Increases Lung Metastasis by Impacting Blood Vessel Invasions. Matrix Biol. 2019;83:26-47.
Not in our library10.1016/j.matbio.2019.07.001
245.
Ming X., Qiu S., Liu X., Li S., Wang Y., Zhu M., Li N., Luo P., Liang C., Tu J. Prognostic Role of Tenascin-C for Cancer Outcome: A Meta-Analysis. Technol. Cancer Res. Treat. 2019;18:1533033818821106.
Not in our library10.1177/1533033818821106
246.
Yang Z.-T., Yeo S.-Y., Yin Y.-X., Lin Z.-H., Lee H.-M., Xuan Y.-H., Cui Y., Kim S.-H. Tenascin-C, a Prognostic Determinant of Esophageal Squamous Cell Carcinoma. PLoS ONE. 2016;11:e0145807.
Not in our library10.1371/journal.pone.0145807
247.
Tenascin-C expression contributes to pediatric brainstem glioma tumor phenotype and represents a novel biomarker of disease · 2019
Not checked
248.
Kang X., Xu E., Wang X., Qian L., Yang Z., Yu H., Wang C., Ren C., Wang Y., Lu X., et al. Tenascin-c Knockdown Suppresses Vasculogenic Mimicry of Gastric Cancer by Inhibiting ERK- Triggered EMT. Cell Death Dis. 2021;12:890.
Not in our library10.1038/s41419-021-04153-1
249.
Ni W.-D., Yang Z.-T., Cui C.-A., Cui Y., Fang L.-Y., Xuan Y.-H. Tenascin-C Is a Potential Cancer-Associated Fibroblasts Marker and Predicts Poor Prognosis in Prostate Cancer. Biochem. Biophys. Res. Commun. 2017;486:607-612.
Not in our library10.1016/j.bbrc.2017.03.021
250.
Yang Z., Ni W., Cui C., Fang L., Xuan Y. Tenascin C Is a Prognostic Determinant and Potential Cancer-Associated Fibroblasts Marker for Breast Ductal Carcinoma. Exp. Mol. Pathol. 2017;102:262-267.
Not in our library10.1016/j.yexmp.2017.02.012
251.
Hashimoto M., Uesugi N., Osakabe M., Yanagawa N., Otsuka K., Kajiwara Y., Ueno H., Sasaki A., Sugai T. Expression Patterns of Microenvironmental Factors and Tenascin-C at the Invasive Front of Stage II and III Colorectal Cancer: Novel Tumor Prognostic Markers. Front. Oncol. 2021;11:690816.
Not in our library10.3389/fonc.2021.690816
252.
Li M., Peng F., Li G., Fu Y., Huang Y., Chen Z., Chen Y. Proteomic Analysis of Stromal Proteins in Different Stages of Colorectal Cancer Establishes Tenascin-C as a Stromal Biomarker for Colorectal Cancer Metastasis. Oncotarget. 2016;7:37226-37237.
Not in our library10.18632/oncotarget.9362
253.
Yang Z., Zhang C., Qi W., Cui C., Cui Y., Xuan Y. Tenascin-C as a Prognostic Determinant of Colorectal Cancer through Induction of Epithelial-to-Mesenchymal Transition and Proliferation. Exp. Mol. Pathol. 2018;105:216-222.
Not in our library10.1016/j.yexmp.2018.08.009
254.
Dhaouadi S., Ben Abderrazek R., Loustau T., Abou-Faycal C., Ksouri A., Erne W., Murdamoothoo D., Mörgelin M., Kungl A., Jung A., et al. Novel Human Tenascin-C Function-Blocking Camel Single Domain Nanobodies. Front. Immunol. 2021;12:635166.
Not in our library10.3389/fimmu.2021.635166
255.
Spenlé C., Loustau T., Murdamoothoo D., Erne W., Beghelli-de la Forest Divonne S., Veber R., Petti L., Bourdely P., Mörgelin M., Brauchle E.-M., et al. Tenascin-C Orchestrates an Immune-Suppressive Tumor Microenvironment in Oral Squamous Cell Carcinoma. Cancer Immunol. Res. 2020;8:1122-1138.
Not in our library10.1158/2326-6066.cir-20-0074
256.
Targeted matrisome analysis identifies thrombospondin-2 and tenascin-C in aligned collagen stroma from invasive breast carcinoma · 2018
Not checked
257.
Chiquet-Ehrismann R., Kalla P., Pearson C.A. Participation of Tenascin and Transforming Growth Factor-Beta in Reciprocal Epithelial-Mesenchymal Interactions of MCF7 Cells and Fibroblasts. Cancer Res. 1989;49:4322-4325.
Not in our library
258.
Maschler S., Grunert S., Danielopol A., Beug H., Wirl G. Enhanced Tenascin-C Expression and Matrix Deposition during Ras/TGF-Beta-Induced Progression of Mammary Tumor Cells. Oncogene. 2004;23:3622-3633.
Not in our library10.1038/sj.onc.1207403
259.
Katoh D., Nagaharu K., Shimojo N., Hanamura N., Yamashita M., Kozuka Y., Imanaka-Yoshida K., Yoshida T. Binding of Avβ1 and Avβ6 Integrins to Tenascin-C Induces Epithelial-Mesenchymal Transition-like Change of Breast Cancer Cells. Oncogenesis. 2013;2:e65.
Not in our library10.1038/oncsis.2013.27
260.
Takahashi Y., Sawada G., Kurashige J., Matsumura T., Uchi R., Ueo H., Ishibashi M., Takano Y., Akiyoshi S., Iwaya T., et al. Tumor-Derived Tenascin-C Promotes the Epithelial–Mesenchymal Transition in Colorectal Cancer Cells. Anticancer Res. 2013;33:1927-1934.
Not in our library
261.
Cai J., Du S., Wang H., Xin B., Wang J., Shen W., Wei W., Guo Z., Shen X. Tenascin-C Induces Migration and Invasion through JNK/c-Jun Signalling in Pancreatic Cancer. Oncotarget. 2017;8:74406-74422.
Not in our library10.18632/oncotarget.20160
262.
Hawkins A.G., Julian C.M., Konzen S., Treichel S., Lawlor E.R., Bailey K.M. Microenvironmental Factors Drive Tenascin C and Src Cooperation to Promote Invadopodia Formation in Ewing Sarcoma. Neoplasia. 2019;21:1063-1072.
Not in our library10.1016/j.neo.2019.08.007
263.
Qian S., Tan X., Liu X., Liu P., Wu Y. Exosomal Tenascin-c Induces Proliferation and Invasion of Pancreatic Cancer Cells by WNT Signaling. OncoTargets Ther. 2019;12:3197-3205.
Not in our library10.2147/ott.s192218
264.
Sarkar S., Mirzaei R., Zemp F.J., Wei W., Senger D.L., Robbins S.M., Yong V.W. Activation of NOTCH Signaling by Tenascin-C Promotes Growth of Human Brain Tumor-Initiating Cells. Cancer Res. 2017;77:3231-3243.
Not in our library10.1158/0008-5472.can-16-2171
265.
Yang Z., Zhang C., Feng Y., Qi W., Cui Y., Xuan Y. Tenascin-C Is Involved in Promotion of Cancer Stemness via the Akt/HIF1α Axis in Esophageal Squamous Cell Carcinoma. Exp. Mol. Pathol. 2019;109:104239.
Not in our library10.1016/j.yexmp.2019.03.007
266.
Katoh D., Kozuka Y., Noro A., Ogawa T., Imanaka-Yoshida K., Yoshida T. Tenascin-C Induces Phenotypic Changes in Fibroblasts to Myofibroblasts with High Contractility through the Integrin Avβ1/Transforming Growth Factor β/SMAD Signaling Axis in Human Breast Cancer. Am. J. Pathol. 2020;190:2123-2135.
Not in our library10.1016/j.ajpath.2020.06.008
267.
Yeo S.-Y., Lee K.-W., Shin D., An S., Cho K.-H., Kim S.-H. A Positive Feedback Loop Bi-Stably Activates Fibroblasts. Nat. Commun. 2018;9:3016.
Not in our library10.1038/s41467-018-05274-6
268.
Mirzaei R., Sarkar S., Dzikowski L., Rawji K.S., Khan L., Faissner A., Bose P., Yong V.W. Brain Tumor-Initiating Cells Export Tenascin-C Associated with Exosomes to Suppress T Cell Activity. Oncoimmunology. 2018;7:e1478647.
Not in our library10.1080/2162402x.2018.1478647
269.
Jachetti E., Caputo S., Mazzoleni S., Brambillasca C.S., Parigi S.M., Grioni M., Piras I.S., Restuccia U., Calcinotto A., Freschi M., et al. Tenascin-C Protects Cancer Stem-like Cells from Immune Surveillance by Arresting T-Cell Activation. Cancer Res. 2015;75:2095-2108.
Not in our library10.1158/0008-5472.can-14-2346
270.
Murdamoothoo D., Sun Z., Yilmaz A., Riegel G., Abou-Faycal C., Deligne C., Velazquez-Quesada I., Erne W., Nascimento M., Mörgelin M., et al. Tenascin-C Immobilizes Infiltrating T Lymphocytes through CXCL12 Promoting Breast Cancer Progression. EMBO Mol. Med. 2021;13:e13270.
Not in our library10.15252/emmm.202013270
271.
Guttery D.S., Shaw J.A., Lloyd K., Pringle J.H., Walker R.A. Expression of Tenascin-C and Its Isoforms in the Breast. Cancer Metastasis. Rev. 2010;29:595-606.
Not in our library10.1007/s10555-010-9249-9
272.
Herold-Mende C., Mueller M.M., Bonsanto M.M., Schmitt H.P., Kunze S., Steiner H.-H. Clinical Impact and Functional Aspects of Tenascin-C Expression during Glioma Progression. Int. J. Cancer. 2002;98:362-369.
Not in our library10.1002/ijc.10233
273.
Berndt A., Anger K., Richter P., Borsi L., Brack S., Silacci M., Franz M., Wunderlich H., Gajda M., Zardi L., et al. Differential Expression of Tenascin-C Splicing Domains in Urothelial Carcinomas of the Urinary Bladder. J. Cancer Res. Clin. Oncol. 2006;132:537-546.
Not in our library10.1007/s00432-006-0106-8
274.
Richter P., Tost M., Franz M., Altendorf-Hofmann A., Junker K., Borsi L., Neri D., Kosmehl H., Wunderlich H., Berndt A. B and C Domain Containing Tenascin-C: Urinary Markers for Invasiveness of Urothelial Carcinoma of the Urinary Bladder? J. Cancer Res. Clin. Oncol. 2009;135:1351-1358.
Not in our library10.1007/s00432-009-0576-6
275.
Wilson K.E., Langdon S.P., Lessells A.M., Miller W.R. Expression of the Extracellular Matrix Protein Tenascin in Malignant and Benign Ovarian Tumours. Br. J. Cancer. 1996;74:999-1004.
Not in our library10.1038/bjc.1996.480
276.
Borsi L., Carnemolla B., Nicolò G., Spina B., Tanara G., Zardi L. Expression of Different Tenascin Isoforms in Normal, Hyperplastic and Neoplastic Human Breast Tissues. Int. J. Cancer. 1992;52:688-692.
Not in our library10.1002/ijc.2910520504
277.
Tsunoda T., Inada H., Kalembeyi I., Imanaka-Yoshida K., Sakakibara M., Okada R., Katsuta K., Sakakura T., Majima Y., Yoshida T. Involvement of Large Tenascin-C Splice Variants in Breast Cancer Progression. Am. J. Pathol. 2003;162:1857-1867.
Not in our library10.1016/s0002-9440(10)64320-9
278.
Hagiwara K., Harimoto N., Yokobori T., Muranushi R., Hoshino K., Gantumur D., Yamanaka T., Ishii N., Tsukagoshi M., Igarashi T., et al. High Co-Expression of Large Tenascin C Splice Variants in Stromal Tissue and Annexin A2 in Cancer Cell Membranes Is Associated with Poor Prognosis in Pancreatic Cancer. Ann. Surg. Oncol. 2020;27:924-930.
Not in our library10.1245/s10434-019-07708-x
279.
Parekh K., Ramachandran S., Cooper J., Bigner D., Patterson A., Mohanakumar T. Tenascin-C, over Expressed in Lung Cancer down Regulates Effector Functions of Tumor Infiltrating Lymphocytes. Lung Cancer. 2005;47:17-29.
Not in our library10.1016/j.lungcan.2004.05.016
280.
Hancox R.A., Allen M.D., Holliday D.L., Edwards D.R., Pennington C.J., Guttery D.S., Shaw J.A., Walker R.A., Pringle J.H., Jones J.L. Tumour-Associated Tenascin-C Isoforms Promote Breast Cancer Cell Invasion and Growth by Matrix Metalloproteinase-Dependent and Independent Mechanisms. Breast Cancer Res. 2009;11:R24.
Not in our library10.1186/bcr2251
281.
Howeedy A.A., Virtanen I., Laitinen L., Gould N.S., Koukoulis G.K., Gould V.E. Differential Distribution of Tenascin in the Normal, Hyperplastic, and Neoplastic Breast. Lab. Investig. 1990;63:798-806.
Not in our library
282.
Sakai T., Kawakatsu H., Hirota N., Yokoyama T., Sakakura T., Saito M. Specific Expression of Tenascin in Human Colonic Neoplasms. Br. J. Cancer. 1993;67:1058-1064.
Not in our library10.1038/bjc.1993.194
283.
Redondo-García S., Peris-Torres C., Caracuel-Peramos R., Rodríguez-Manzaneque J.C. ADAMTS Proteases and the Tumor Immune Microenvironment: Lessons from Substrates and Pathologies. Matrix Biol. Plus. 2021;9:100054.
Not in our library10.1016/j.mbplus.2020.100054
284.
Saha N., Robev D., Himanen J.P., Nikolov D.B. ADAM Proteases: Emerging Role and Targeting of the Non-Catalytic Domains. Cancer Lett. 2019;467:50-57.
Not in our library10.1016/j.canlet.2019.10.003
285.
McKerrow J.H., Bhargava V., Hansell E., Huling S., Kuwahara T., Matley M., Coussens L., Warren R. A Functional Proteomics Screen of Proteases in Colorectal Carcinoma. Mol. Med. 2000;6:450-460.
Not in our library10.1007/bf03401787
286.
Bates A.L., Pickup M.W., Hallett M.A., Dozier E.A., Thomas S., Fingleton B. Stromal Matrix Metalloproteinase 2 Regulates Collagen Expression and Promotes the Outgrowth of Experimental Metastases. J. Pathol. 2015;235:773-783.
Not in our library10.1002/path.4493
287.
Catteau X., Simon P., Noël J.-C. Stromal Expression of Matrix Metalloproteinase 2 in Cancer-Associated Fibroblasts Is Strongly Related to Human Epidermal Growth Factor Receptor 2 Status in Invasive Breast Carcinoma. Mol. Clin. Oncol. 2016;4:375-378.
Not in our library10.3892/mco.2015.721
288.
Del Casar J.M., González L.O., Alvarez E., Junquera S., Marín L., González L., Bongera M., Vázquez J., Vizoso F.J. Comparative Analysis and Clinical Value of the Expression of Metalloproteases and Their Inhibitors by Intratumor Stromal Fibroblasts and Those at the Invasive Front of Breast Carcinomas. Breast Cancer Res. Treat. 2009;116:39-52.
Not in our library10.1007/s10549-009-0351-z
289.
Eck S.M., Côté A.L., Winkelman W.D., Brinckerhoff C.E. CXCR4 and Matrix Metalloproteinase-1 Are Elevated in Breast Carcinoma-Associated Fibroblasts and in Normal Mammary Fibroblasts Exposed to Factors Secreted by Breast Cancer Cells. Mol. Cancer Res. 2009;7:1033-1044.
Not in our library10.1158/1541-7786.mcr-09-0015
290.
Panagopoulos V., Leach D.A., Zinonos I., Ponomarev V., Licari G., Liapis V., Ingman W.V., Anderson P., DeNichilo M.O., Evdokiou A. Inflammatory Peroxidases Promote Breast Cancer Progression in Mice via Regulation of the Tumour Microenvironment. Int. J. Oncol. 2017;50:1191-1200.
Not in our library10.3892/ijo.2017.3883
291.
Jackson B.C., Nebert D.W., Vasiliou V. Update of Human and Mouse Matrix Metalloproteinase Families. Hum. Genomics. 2010;4:194-201.
Not in our library10.1186/1479-7364-4-3-194
292.
Cui N., Hu M., Khalil R.A. Biochemical and Biological Attributes of Matrix Metalloproteinases. Prog. Mol. Biol. Transl. Sci. 2017;147:1-73.
Not in our library10.1016/bs.pmbts.2017.02.005
293.
Harper E., Bloch K.J., Gross J. The Zymogen of Tadpole Collagenase. Biochemistry. 1971;10:3035-3041.
Not in our library10.1021/bi00792a008
294.
Becker J.W., Marcy A.I., Rokosz L.L., Axel M.G., Burbaum J.J., Fitzgerald P.M., Cameron P.M., Esser C.K., Hagmann W.K., Hermes J.D. Stromelysin-1: Three-Dimensional Structure of the Inhibited Catalytic Domain and of the C-Truncated Proenzyme. Protein Sci. 1995;4:1966-1976.
Not in our library10.1002/pro.5560041002
295.
Pei D., Weiss S.J. Transmembrane-Deletion Mutants of the Membrane-Type Matrix Metalloproteinase-1 Process Progelatinase A and Express Intrinsic Matrix-Degrading Activity. J. Biol. Chem. 1996;271:9135-9140.
Not in our library10.1074/jbc.271.15.9135
296.
Van Wart H.E., Birkedal-Hansen H. The Cysteine Switch: A Principle of Regulation of Metalloproteinase Activity with Potential Applicability to the Entire Matrix Metalloproteinase Gene Family. Proc. Natl. Acad. Sci. USA. 1990;87:5578-5582.
Not in our library10.1073/pnas.87.14.5578
297.
Ferrari R., Martin G., Tagit O., Guichard A., Cambi A., Voituriez R., Vassilopoulos S., Chavrier P. MT1-MMP Directs Force-Producing Proteolytic Contacts That Drive Tumor Cell Invasion. Nat. Commun. 2019;10:4886.
Not in our library10.1038/s41467-019-12930-y
298.
Franchi M., Piperigkou Z., Karamanos K.-A., Franchi L., Masola V. Extracellular Matrix-Mediated Breast Cancer Cells Morphological Alterations, Invasiveness, and Microvesicles/Exosomes Release. Cells. 2020;9:2031.
Not in our library10.3390/cells9092031
299.
Nakahara H., Howard L., Thompson E.W., Sato H., Seiki M., Yeh Y., Chen W.T. Transmembrane/Cytoplasmic Domain-Mediated Membrane Type 1-Matrix Metalloprotease Docking to Invadopodia Is Required for Cell Invasion. Proc. Natl. Acad. Sci. USA. 1997;94:7959-7964.
Not in our library10.1073/pnas.94.15.7959
300.
Watanabe A., Hoshino D., Hosino D., Koshikawa N., Seiki M., Suzuki T., Ichikawa K. Critical Role of Transient Activity of MT1-MMP for ECM Degradation in Invadopodia. PLoS Comput. Biol. 2013;9:e1003086.
Not in our library10.1371/annotation/b41ed85a-11d1-483a-a7ac-9d06f0c8669a
301.
Gould C.M., Courtneidge S.A. Regulation of Invadopodia by the Tumor Microenvironment. Cell Adh. Migr. 2014;8:226-235.
Not in our library10.4161/cam.28346
302.
Peláez R., Pariente A., Pérez-Sala Á., Larrayoz I.M. Integrins: Moonlighting Proteins in Invadosome Formation. Cancers. 2019;11:615.
Not in our library10.3390/cancers11050615
303.
Alexander N.R., Branch K.M., Parekh A., Clark E.S., Iwueke I.C., Guelcher S.A., Weaver A.M. Extracellular Matrix Rigidity Promotes Invadopodia Activity. Curr. Biol. 2008;18:1295-1299.
Not in our library10.1016/j.cub.2008.07.090
304.
Jerrell R.J., Parekh A. Matrix Rigidity Differentially Regulates Invadopodia Activity through ROCK1 and ROCK2. Biomaterials. 2016;84:119-129.
Not in our library10.1016/j.biomaterials.2016.01.028
305.
Knapinska A.M., Fields G.B. The Expanding Role of MT1-MMP in Cancer Progression. Pharmaceuticals. 2019;12:77.
Not in our library10.3390/ph12020077
306.
Artym V.V., Zhang Y., Seillier-Moiseiwitsch F., Yamada K.M., Mueller S.C. Dynamic Interactions of Cortactin and Membrane Type 1 Matrix Metalloproteinase at Invadopodia: Defining the Stages of Invadopodia Formation and Function. Cancer Res. 2006;66:3034-3043.
Not in our library10.1158/0008-5472.can-05-2177
307.
Yu X., Zech T., McDonald L., Gonzalez E.G., Li A., Macpherson I., Schwarz J.P., Spence H., Futó K., Timpson P., et al. N-WASP Coordinates the Delivery and F-Actin-Mediated Capture of MT1-MMP at Invasive Pseudopods. J. Cell Biol. 2012;199:527-544.
Not in our library10.1083/jcb.201203025
308.
Williams K.C., McNeilly R.E., Coppolino M.G. SNAP23, Syntaxin4, and Vesicle-Associated Membrane Protein 7 (VAMP7) Mediate Trafficking of Membrane Type 1-Matrix Metalloproteinase (MT1-MMP) during Invadopodium Formation and Tumor Cell Invasion. Mol. Biol. Cell. 2014;25:2061-2070.
Not in our library10.1091/mbc.e13-10-0582
309.
Castro-Castro A., Marchesin V., Monteiro P., Lodillinsky C., Rossé C., Chavrier P. Cellular and Molecular Mechanisms of MT1-MMP-Dependent Cancer Cell Invasion. Annu. Rev. Cell Dev. Biol. 2016;32:555-576.
Not in our library10.1146/annurev-cellbio-111315-125227
310.
Ohuchi E., Imai K., Fujii Y., Sato H., Seiki M., Okada Y. Membrane Type 1 Matrix Metalloproteinase Digests Interstitial Collagens and Other Extracellular Matrix Macromolecules. J. Biol. Chem. 1997;272:2446-2451.
Not in our library10.1074/jbc.272.4.2446
311.
d’Ortho M.P., Will H., Atkinson S., Butler G., Messent A., Gavrilovic J., Smith B., Timpl R., Zardi L., Murphy G. Membrane-Type Matrix Metalloproteinases 1 and 2 Exhibit Broad-Spectrum Proteolytic Capacities Comparable to Many Matrix Metalloproteinases. Eur. J. Biochem. 1997;250:751-757.
Not in our library10.1111/j.1432-1033.1997.00751.x
312.
Strongin A.Y., Collier I., Bannikov G., Marmer B.L., Grant G.A., Goldberg G.I. Mechanism of Cell Surface Activation of 72-KDa Type IV Collagenase. Isolation of the Activated Form of the Membrane Metalloprotease. J. Biol. Chem. 1995;270:5331-5338.
Not in our library10.1074/jbc.270.10.5331
313.
Tokuraku M., Sato H., Murakami S., Okada Y., Watanabe Y., Seiki M. Activation of the Precursor of Gelatinase A/72 KDa Type IV Collagenase/MMP-2 in Lung Carcinomas Correlates with the Expression of Membrane-Type Matrix Metalloproteinase (MT-MMP) and with Lymph Node Metastasis. Int. J. Cancer. 1995;64:355-359.
Not in our library10.1002/ijc.2910640513
314.
Sato H., Takino T. Coordinate Action of Membrane-Type Matrix Metalloproteinase-1 (MT1-MMP) and MMP-2 Enhances Pericellular Proteolysis and Invasion. Cancer Sci. 2010;101:843-847.
Not in our library10.1111/j.1349-7006.2010.01498.x
315.
Henriet P., Emonard H. Matrix Metalloproteinase-2: Not (Just) a “Hero” of the Past. Biochimie. 2019;166:223-232.
Not in our library10.1016/j.biochi.2019.07.019
316.
Matrix Metalloproteinase-9 (MMP-9) as a Cancer Biomarker and MMP-9 Biosensors: Recent Advances · 2018
No notice
317.
Aufderklamm S., Hennenlotter J., Rausch S., Bock C., Erne E., Schwentner C., Stenzl A. Oncological Validation of Bone Turnover Markers C-Terminal Telopeptide of Type I Collagen (1CTP) and Peptides n-Terminal Propeptide of Type I Procollagen (P1NP) in Patients with Prostate Cancer and Bone Metastases. Transl. Androl. Urol. 2021;10:4000-4008.
Not in our library10.21037/tau-20-1120
318.
Lipton A., Leitzel K., Ali S.M., Polimera H.V., Nagabhairu V., Marks E., Richardson A.E., Krecko L., Ali A., Koestler W., et al. High Turnover of Extracellular Matrix Reflected by Specific Protein Fragments Measured in Serum Is Associated with Poor Outcomes in Two Metastatic Breast Cancer Cohorts. Int. J. Cancer. 2018;143:3027-3034.
Not in our library10.1002/ijc.31627
319.
Kehlet S.N., Sanz-Pamplona R., Brix S., Leeming D.J., Karsdal M.A., Moreno V. Excessive Collagen Turnover Products Are Released during Colorectal Cancer Progression and Elevated in Serum from Metastatic Colorectal Cancer Patients. Sci. Rep. 2016;6:30599.
Not in our library10.1038/srep30599
320.
Maquart F.-X., Pasco S., Ramont L., Hornebeck W., Monboisse J.-C. An Introduction to Matrikines: Extracellular Matrix-Derived Peptides Which Regulate Cell Activity. Implication in Tumor Invasion. Crit. Rev. Oncol. Hematol. 2004;49:199-202.
Not in our library10.1016/j.critrevonc.2003.06.007
321.
Maquart F.X., Siméon A., Pasco S., Monboisse J.C. Regulation of cell activity by the extracellular matrix: The concept of matrikines. J. Soc. Biol. 1999;193:423-428.
Not in our library10.1051/jbio/1999193040423
322.
Davis G.E., Bayless K.J., Davis M.J., Meininger G.A. Regulation of Tissue Injury Responses by the Exposure of Matricryptic Sites within Extracellular Matrix Molecules. Am. J. Pathol. 2000;156:1489-1498.
Not in our library10.1016/s0002-9440(10)65020-1
323.
Ricard-Blum S., Vallet S.D. Fragments Generated upon Extracellular Matrix Remodeling: Biological Regulators and Potential Drugs. Matrix Biol. 2019;75–76:170-189.
Not in our library10.1016/j.matbio.2017.11.005
324.
Han X., Caron J.M., Brooks P.C. Cryptic Collagen Elements as Signaling Hubs in the Regulation of Tumor Growth and Metastasis. J. Cell Physiol. 2020;235:9005-9020.
Not in our library10.1002/jcp.29752
325.
Kisling A., Lust R.M., Katwa L.C. What Is the Role of Peptide Fragments of Collagen I and IV in Health and Disease? Life Sci. 2019;228:30-34.
Not in our library10.1016/j.lfs.2019.04.042
326.
Heinz A., Jung M.C., Duca L., Sippl W., Taddese S., Ihling C., Rusciani A., Jahreis G., Weiss A.S., Neubert R.H.H., et al. Degradation of Tropoelastin by Matrix Metalloproteinases—Cleavage Site Specificities and Release of Matrikines. FEBS J. 2010;277:1939-1956.
Not in our library10.1111/j.1742-4658.2010.07616.x
327.
Wells J.M., Gaggar A., Blalock J.E. MMP Generated Matrikines. Matrix Biol. 2015;44–46:122-129.
Not in our library10.1016/j.matbio.2015.01.016
328.
Fujita M., Suzuki H., Fukai F. Involvement of Integrin-Activating Peptides Derived from Tenascin-C in Colon Cancer Progression. World J. Gastrointest. Oncol. 2021;13:980-994.
Not in our library10.4251/wjgo.v13.i9.980
329.
Fujita M., Sasada M., Iyoda T., Fukai F. Involvement of Integrin-Activating Peptides Derived from Tenascin-C in Cancer Aggression and New Anticancer Strategy Using the Fibronectin-Derived Integrin-Inactivating Peptide. Molecules. 2020;25:3239.
Not in our library10.3390/molecules25143239
330.
Joshi R., Goihberg E., Ren W., Pilichowska M., Mathew P. Proteolytic Fragments of Fibronectin Function as Matrikines Driving the Chemotactic Affinity of Prostate Cancer Cells to Human Bone Marrow Mesenchymal Stromal Cells via the A5β1 Integrin. Cell Adh. Migr. 2017;11:305-315.
Not in our library10.1080/19336918.2016.1212139
331.
Pagano M., Reboud-Ravaux M. Cryptic Activities of Fibronectin Fragments, Particularly Cryptic Proteases. Front. Biosci. (Landmark Ed.). 2011;16:698-706.
Not in our library10.2741/3713
332.
Adair-Kirk T.L., Atkinson J.J., Broekelmann T.J., Doi M., Tryggvason K., Miner J.H., Mecham R.P., Senior R.M. A Site on Laminin Alpha 5, AQARSAASKVKVSMKF, Induces Inflammatory Cell Production of Matrix Metalloproteinase-9 and Chemotaxis. J. Immunol. 2003;171:398-406.
Not in our library10.4049/jimmunol.171.1.398
333.
Papadas A., Arauz G., Cicala A., Wiesner J., Asimakopoulos F. Versican and Versican-Matrikines in Cancer Progression, Inflammation, and Immunity. J. Histochem. Cytochem. 2020;68:871-885.
Not in our library10.1369/0022155420937098
334.
Tumor Microenvironment: Extracellular Matrix Alterations Influence Tumor Progression · 2020
No notice
335.
Aikio M., Alahuhta I., Nurmenniemi S., Suojanen J., Palovuori R., Teppo S., Sorsa T., López-Otín C., Pihlajaniemi T., Salo T., et al. Arresten, a Collagen-Derived Angiogenesis Inhibitor, Suppresses Invasion of Squamous Cell Carcinoma. PLoS ONE. 2012;7:e51044.
Not in our library10.1371/journal.pone.0051044
336.
Hwang-Bo J., Park J.-H., Bae M.G., Chung I.S. Recombinant Canstatin Inhibits VEGF-A-Induced Lymphangiogenesis and Metastasis in an Oral Squamous Cell Carcinoma SCC-VII Animal Model. Cancer Med. 2016;5:2977-2988.
Not in our library10.1002/cam4.866
337.
Ma Y., Wu T., Zhou H., He G., Li Y., Wang B., Guo Q., Chen B., Li W. Canstatin Represses Glioma Growth by Inhibiting Formation of VM-like Structures. Transl. Neurosci. 2021;12:309-319.
Not in our library10.1515/tnsci-2020-0176
338.
Okada M., Yamawaki H. A Current Perspective of Canstatin, a Fragment of Type IV Collagen Alpha 2 Chain. J. Pharmacol. Sci. 2019;139:59-64.
Not in our library10.1016/j.jphs.2018.12.001
339.
Li K., Shi M., Qin S. Current Status and Study Progress of Recombinant Human Endostatin in Cancer Treatment. Oncol. Ther. 2018;6:21-43.
Not in our library10.1007/s40487-017-0055-1
340.
Liu X., Nie W., Xie Q., Chen G., Li X., Jia Y., Yin B., Qu X., Li Y., Liang J. Endostatin Reverses Immunosuppression of the Tumor Microenvironment in Lung Carcinoma. Oncol. Lett. 2018;15:1874-1880.
Not in our library10.3892/ol.2017.7455
341.
Walia A., Yang J.F., Huang Y.-H., Rosenblatt M.I., Chang J.-H., Azar D.T. Endostatin’s Emerging Roles in Angiogenesis, Lymphangiogenesis, Disease, and Clinical Applications. Biochim. Biophys. Acta. 2015;1850:2422-2438.
Not in our library10.1016/j.bbagen.2015.09.007
342.
Koskimaki J.E., Karagiannis E.D., Tang B.C., Hammers H., Watkins D.N., Pili R., Popel A.S. Pentastatin-1, a Collagen IV Derived 20-Mer Peptide, Suppresses Tumor Growth in a Small Cell Lung Cancer Xenograft Model. BMC Cancer. 2010;10:29.
Not in our library10.1186/1471-2407-10-29
343.
Li Y., Li J., Woo Y.M., Shen Z., Yao H., Cai Y., Lin M.C.-M., Poon W.S. Enhanced Expression of Vastatin Inhibits Angiogenesis and Prolongs Survival in Murine Orthotopic Glioblastoma Model. BMC Cancer. 2017;17:126.
Not in our library10.1186/s12885-017-3125-8
344.
Shen Z., Yao C., Wang Z., Yue L., Fang Z., Yao H., Lin F., Zhao H., Sun Y.-J., Bian X.-W., et al. Vastatin, an Endogenous Antiangiogenesis Polypeptide That Is Lost in Hepatocellular Carcinoma, Effectively Inhibits Tumor Metastasis. Mol. Ther. 2016;24:1358-1368.
Not in our library10.1038/mt.2016.56
345.
Kim M., Lee C., Seo D.Y., Lee H., Horton J.D., Park J., Scherer P.E. The Impact of Endotrophin on the Progression of Chronic Liver Disease. Exp. Mol. Med. 2020;52:1766-1776.
Not in our library10.1038/s12276-020-00520-8
346.
Cai M., Onoda K., Takao M., Kyoko I.-Y., Shimpo H., Yoshida T., Yada I. Degradation of Tenascin-C and Activity of Matrix Metalloproteinase-2 Are Associated with Tumor Recurrence in Early Stage Non-Small Cell Lung Cancer. Clin. Cancer Res. 2002;8:1152-1156.
Not in our library
347.
Mai J., Sameni M., Mikkelsen T., Sloane B.F. Degradation of Extracellular Matrix Protein Tenascin-C by Cathepsin B: An Interaction Involved in the Progression of Gliomas. Biol. Chem. 2002;383:1407-1413.
Not in our library10.1515/bc.2002.159
348.
Kusagawa H., Onoda K., Namikawa S., Yada I., Okada A., Yoshida T., Sakakura T. Expression and Degeneration of Tenascin-C in Human Lung Cancers. Br. J. Cancer. 1998;77:98-102.
Not in our library10.1038/bjc.1998.15
349.
Saito Y., Imazeki H., Miura S., Yoshimura T., Okutsu H., Harada Y., Ohwaki T., Nagao O., Kamiya S., Hayashi R., et al. A Peptide Derived from Tenascin-C Induces Beta1 Integrin Activation through Syndecan-4. J. Biol. Chem. 2007;282:34929-34937.
Not in our library10.1074/jbc.m705608200
350.
Tanaka R., Seki Y., Saito Y., Kamiya S., Fujita M., Okutsu H., Iyoda T., Takai T., Owaki T., Yajima H., et al. Tenascin-C-Derived Peptide TNIIIA2 Highly Enhances Cell Survival and Platelet-Derived Growth Factor (PDGF)-Dependent Cell Proliferation through Potentiated and Sustained Activation of Integrin A5β1. J. Biol. Chem. 2014;289:17699-17708.
Not in our library10.1074/jbc.m113.546622
351.
Fujita M., Sasada M., Iyoda T., Nagai R., Kudo C., Yamamoto T., Osada S., Kodama H., Fukai F. Anoikis Resistance Conferred by Tenascin-C-Derived Peptide TNIIIA2 and Its Disruption by Integrin Inactivation. Biochem. Biophys. Res. Commun. 2021;536:14-19.
Not in our library10.1016/j.bbrc.2020.12.050
352.
Fujita M., Yamamoto T., Iyoda T., Fujisawa T., Sasada M., Nagai R., Kudo C., Otsuka K., Kamiya S., Kodama H., et al. Aggressive Progression in Glioblastoma Cells through Potentiated Activation of Integrin A5β1 by the Tenascin-C-Derived Peptide TNIIIA2. Mol. Cancer Ther. 2019;18:1649-1658.
Not in our library10.1158/1535-7163.mct-18-1251
353.
Fujita M., Yamamoto T., Iyoda T., Fujisawa T., Nagai R., Kudo C., Sasada M., Kodama H., Fukai F. Autocrine Production of PDGF Stimulated by the Tenascin-C-Derived Peptide TNIIIA2 Induces Hyper-Proliferation in Glioblastoma Cells. Int. J. Mol. Sci. 2019;20:3183.
Not in our library10.3390/ijms20133183
354.
Iyoda T., Fujita M., Fukai F. Biologically Active TNIIIA2 Region in Tenascin-C Molecule: A Major Contributor to Elicit Aggressive Malignant Phenotypes From Tumors/Tumor Stroma. Front. Immunol. 2020;11:610096.
Not in our library10.3389/fimmu.2020.610096
355.
Suzuki H., Sasada M., Kamiya S., Ito Y., Watanabe H., Okada Y., Ishibashi K., Iyoda T., Yanaka A., Fukai F. The Promoting Effect of the Extracellular Matrix Peptide TNIIIA2 Derived from Tenascin-C in Colon Cancer Cell Infiltration. Int. J. Mol. Sci. 2017;18:181.
Not in our library10.3390/ijms18010181
356.
Fukai F., Hasebe S., Ueki M., Mutoh M., Ohgi C., Takahashi H., Takeda K., Katayama T. Identification of the Anti-Adhesive Site Buried within the Heparin-Binding Domain of Fibronectin. J. Biochem. 1997;121:189-192.
Not in our library
357.
Shapiro S.D., Endicott S.K., Province M.A., Pierce J.A., Campbell E.J. Marked Longevity of Human Lung Parenchymal Elastic Fibers Deduced from Prevalence of D-Aspartate and Nuclear Weapons-Related Radiocarbon. J. Clin. Investig. 1991;87:1828-1834.
Not in our library10.1172/jci115204
358.
Heinz A. Elastases and Elastokines: Elastin Degradation and Its Significance in Health and Disease. Crit. Rev. Biochem. Mol. Biol. 2020;55:252-273.
Not in our library10.1080/10409238.2020.1768208
359.
Ntayi C., Labrousse A.-L., Debret R., Birembaut P., Bellon G., Antonicelli F., Hornebeck W., Bernard P. Elastin-Derived Peptides Upregulate Matrix Metalloproteinase-2-Mediated Melanoma Cell Invasion through Elastin-Binding Protein. J. Investig. Dermatol. 2004;122:256-265.
Not in our library10.1046/j.0022-202x.2004.22228.x
360.
Blood C.H., Sasse J., Brodt P., Zetter B.R. Identification of a Tumor Cell Receptor for VGVAPG, an Elastin-Derived Chemotactic Peptide. J. Cell Biol. 1988;107:1987-1993.
Not in our library10.1083/jcb.107.5.1987
361.
Da Silva J., Lameiras P., Beljebbar A., Berquand A., Villemin M., Ramont L., Dukic S., Nuzillard J.-M., Molinari M., Gautier M., et al. Structural Characterization and in Vivo Pro-Tumor Properties of a Highly Conserved Matrikine. Oncotarget. 2018;9:17839-17857.
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Toupance S., Brassart B., Rabenoelina F., Ghoneim C., Vallar L., Polette M., Debelle L., Birembaut P. Elastin-Derived Peptides Increase Invasive Capacities of Lung Cancer Cells by Post-Transcriptional Regulation of MMP-2 and UPA. Clin. Exp. Metastasis. 2012;29:511-522.
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