VEGF165 requires extracellular matrix components to induce mitogenic effects and migratory response in breast cancer cells

Miralem, Tihomir; Steinberg, Robert A.; Price, Dan R.G.; Avraham, Hava

doi:10.1038/sj.onc.1204753

Cited by 56 publications

(42 citation statements)

References 78 publications

(96 reference statements)

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“…Osteoblast binding to extracellular matrix proteins such as FN through integrins induces c-Fos and c-Jun expression via protein kinase C and phosphotyrosine kinase signaling pathways (61). FN is required for vascular endothelial growth factor-induced c-Fos induction, mitogenic response, and cell migration in T47D breast cancer cells (62). We found that the inhibitors of ERK, PD98095, of PI3K, wortmannin, and of AP-1, NDGA, blocked FN-induced c-Fos protein expression.…”

Section: Discussionmentioning

confidence: 99%

Fibronectin Increases Matrix Metalloproteinase 9 Expression through Activation of c-Fos via Extracellular-regulated Kinase and Phosphatidylinositol 3-Kinase Pathways in Human Lung Carcinoma Cells

Han

Ritzenthaler

Sitaraman

et al. 2006

Journal of Biological Chemistry

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Matrix metalloproteinases (MMPs) 2 are a family of zinc enzymes responsible for degradation of extracellular matrix components including basement membrane collagen, interstitial collagens, fibronectin (FN), and various proteoglycans during normal remodeling and repair processes (1, 2). The potent proteolytic activities of MMPs are mainly regulated by the concomitant expression of specific tissue inhibitors of matrix metalloproteinases (3). Excessive or inappropriate expression of MMPs may contribute to the pathogenesis of tissue destructive processes in a wide variety of diseases including lung disorders like bronchial asthma, chronic obstructive pulmonary disease, acute lung injury, pulmonary hypertension, and interstitial lung diseases (2, 4). In addition, MMPs have been implicated in the progression and metastases of different tumors including lung cancer (see later in text).One member of the MMP family is the 92-kDa type IV collagenase MMP-9. The MMP-9 gene is encoded on chromosome 20 and its expression is under the control of a 2.2-kb upstream regulatory sequence harboring binding sites for AP-1, NF-B, Sp1, and others (5). MMP-9 expression is increased in malignant cancers when compared with benign tumors and non-invasive ones, and there is compelling in vitro and in vivo evidence for a role of MMP-9 in tumor invasion and angiogenesis (6, 7). Its dramatic overexpression in cancer and various inflammatory conditions suggest that this protease is a potential target for the development of novel therapeutic interventions (8).Because of its perceived importance, our research focuses on the factors that increase MMP-9 expression in the lung. Our search led us to FN, a matrix glycoprotein highly expressed in tobacco-related lung disease that has been shown to stimulate lung carcinoma cell growth through several mechanisms (9 -11). Cell adhesion to FN results in MMP secretion in normal and tumor cell systems (12)(13)(14). These studies suggest that tumor cell interactions with FN might lead to MMP-9 expression thereby promoting cancer cell migration, invasion, and related processes. However, the mechanisms by which FN stim-* This work was supported by American Lung Association Bioresearch Grant RG-10215N (to S. W. H.) and by a Merit Review Grant from the Department of Veterans Affairs (to J. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C.

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Section: Discussionmentioning

confidence: 99%

Fibronectin Increases Matrix Metalloproteinase 9 Expression through Activation of c-Fos via Extracellular-regulated Kinase and Phosphatidylinositol 3-Kinase Pathways in Human Lung Carcinoma Cells

Han

Ritzenthaler

Sitaraman

et al. 2006

Journal of Biological Chemistry

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“…62,63 Although it is not known if LN␣4-containing isoforms bind, retain, and present growth factors to the cell, it is possible that lack of LN␣4 reduces or abolishes the effect of PDGF-BB on MC/ pericyte proliferation, migration, or differentiation. We have shown that PDGF-BB-induced MC migration requires interaction with the LN␣4 chain of LN411.…”

Section: Discussionmentioning

confidence: 99%

Laminin α4-Null Mutant Mice Develop Chronic Kidney Disease with Persistent Overexpression of Platelet-Derived Growth Factor

Abrass

Hansen

Patton

2010

The American Journal of Pathology

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Each extracellular matrix compartment in the kidney has a unique composition, with regional specificity in the expression of various laminin isoforms. Although null mutations in the majority of laminin chains lead to specific developmental abnormalities in the kidney, Lama4؊/؊ mice have progressive glomerular and tubulointerstitial fibrosis. These mice have a significant increase in expression of platelet-derived growth factor (PDGF)-BB, PDGF-DD, and PDGF receptor ␤ in association with immature glomerular and peritubular capillaries. In addition, mesangial cell exposure to ␣4-containing laminins, but not other isoforms, results in down-regulation of PDGF receptor mRNA and protein, suggesting a direct effect of LN411/LN421 on vessel maturation. Given the known role of overexpression of PDGF-BB and PDGF-DD on glomerular and tubulointerstitial fibrosis , these data suggest that failure of laminin ␣4-mediated down-regulation of PDGF activity contributes to the progressive renal lesions in this animal model. Given the recent demonstration that individuals with laminin ␣4 mutations develop cardiomyopathy , these findings may be relevant to kidney disease in humans.

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“…Most studies addressing the autocrine functions of VEGF in breast cancer cells used the MDA-MB-231 cell line, which expresses mainly the VEGF165 and VEGF121 isoforms. VEGF blockade (anti-VEGF antibodies or use of anti-sense VEGF RNA) in breast cancer cells results in direct apoptosis of tumor cells under normoxia 11,12,15,16 or hypoxia. 34 However, these experiments cannot discriminate between VEGF isoforms.…”

Section: Discussionmentioning

confidence: 99%

“…VEGF165 contributes to the two major characteristics of invasive breast carcinoma: survival and migration of breast cancer cells, [11][12][13][14][15][16] independently of angiogenesis. Several findings supported the hypothesis that carcinoma progression selects for cells that depend on VEGF165 as an autocrine survival factor (11, 13 and 16).…”

Section: Overexpression Of Vegf189 In Breast Cancer Cells Induces Apomentioning

confidence: 99%

Overexpression of VEGF189 in breast cancer cells induces apoptosis via NRP1 under stress conditions

Vintonenko¹,

Pelaez-Garavito²,

Buteau-Lozano³

et al. 2011

Cell Adhesion & Migration

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VEGF165 requires extracellular matrix components to induce mitogenic effects and migratory response in breast cancer cells

Cited by 56 publications

References 78 publications

Fibronectin Increases Matrix Metalloproteinase 9 Expression through Activation of c-Fos via Extracellular-regulated Kinase and Phosphatidylinositol 3-Kinase Pathways in Human Lung Carcinoma Cells

Fibronectin Increases Matrix Metalloproteinase 9 Expression through Activation of c-Fos via Extracellular-regulated Kinase and Phosphatidylinositol 3-Kinase Pathways in Human Lung Carcinoma Cells

Laminin α4-Null Mutant Mice Develop Chronic Kidney Disease with Persistent Overexpression of Platelet-Derived Growth Factor

Overexpression of VEGF189 in breast cancer cells induces apoptosis via NRP1 under stress conditions

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