Integrin alpha 3 beta 1 participates in the phagocytosis of extracellular matrix molecules by human breast cancer cells.

Coopman, Peter J.; Thomas, D. A.; Gehlsen, Kurt R.; Mueller, Susette C.

doi:10.1091/mbc.7.11.1789

Cited by 78 publications

(75 citation statements)

References 53 publications

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“…Cells were microinjected with either preimmune IgG or the anti-cortactin pAb (#170-10). As previously described, these cells locally degrade an FITC matrix to leave dark areas, easily detectable by immuno¯uorescence microscopy (Coopman et al, 1996). We have demonstrated previously that the in vitro invasive behavior of cells grown on gelatin and measured by phagocytosis is similar to their behavior in this assay when grown on collagen I and Matrigel (Coopman et al, 1998).…”

Section: Microinjection Of Anti-cortactin Pabs Blocks Local Invasionsupporting

confidence: 66%

“…When invasive cells such as Rous sarcoma virustransformed chicken embryo ®broblasts or metastatic cancer cell lines are cultured on ECM, actin-containing protrusions, called invadopodia, extend into the matrix and participate in matrix degradation (Chen, 1989;Coopman et al, 1996;Monsky et al, 1994;Mueller and Chen, 1991). There is a correlation between the ability of cells to locally degrade the matrix at invadopodia, and their invasive potential as measured in other in vitro and in vivo assays for motility and invasion (Coopman et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

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An invasion-related complex of cortactin, paxillin and PKCμ associates with invadopodia at sites of extracellular matrix degradation

et al. 1999

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Invasive breast cancer cells have the ability to extend membrane protrusions, invadopodia, into the extracellular matrix (ECM). These structures are associated with sites of active matrix degradation. The amount of matrix degradation associated with the activity of these membrane protrusions has been shown to directly correlate with invasive potential. We demonstrate here that microinjection of polyclonal anti-cortactin antibodies blocks matrix degradation at invadopodia supporting the hypothesis that cortactin has a direct role in invasive behavior. MDA-MB-231, invasive breast cancer cells were sheared from the surface of a gelatin matrix to isolate invadopodia. Cortactin, paxillin and protein kinase C (PKC) m, a serine kinase, were co-immunoprecipitated as a complex from invadopodia-enriched membranes. We con®rmed the subcellular distribution of these proteins by immunolocalization and Western blotting. We also determined that, in contrast to its presence in invasive cells, this complex of proteins was not detected in lysates from non-invasive cells that do not form invadopodia. Taken together, these data suggest that the formation of this cortactin-containing complex correlates with cellular invasiveness. We hypothesize that this complex of molecules has a role in the formation and function of invadopodia during cellular invasion.

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Section: Microinjection Of Anti-cortactin Pabs Blocks Local Invasionsupporting

confidence: 66%

Section: Introductionmentioning

confidence: 99%

An invasion-related complex of cortactin, paxillin and PKCμ associates with invadopodia at sites of extracellular matrix degradation

et al. 1999

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“…Several recent reports suggest, that increased proteolytic activity might play a prominent role. a3b1 integrin was shown to participate in phagocytosis of extracellular matrix (Coopman et al, 1996). a2b1, a3b1, a4b1, and a5b1 integrin were found to be involved in the regulation of matrix metalloprotease expression (Larjava et al, 1993;Huhtala et al, 1995;Riikonen et al, 1995).…”

Section: Discussionmentioning

confidence: 99%

“…Third, integrins are necessary for basement membrane penetration, since RGD peptides interfering with ligand binding to certain integrins prevented this process in vitro (Gehlsen et al, 1988). And ®nally, integrins are involved in the regulation of protease expression and their localized activities, as demonstrated in tissue culture experiments (Huhtala et al, 1995;Riikonen et al, 1995;Brooks et al, 1996;Coopman et al, 1996;Nakahara et al, 1996). In vivo changes in the metastatic potential of tumor cells often correlated with changes of the integrin expression pattern.…”

Section: Introductionmentioning

confidence: 99%

β1 integrin promotes but is not essential for metastasis of ras-myc transformed fibroblasts

Brakebusch

Wennerberg

Krell³

et al. 1999

Oncogene

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To investigate the role of b1 integrin during tumor metastasis, we established a ras-myc transformed ®broblastoid cell line with a disrupted b1 integrin gene on both alleles (GERM 11). Stable transfection of this cell line with an expression vector encoding b1A integrin resulted in b1A integrin-expressing sublines. Tumors were induced by subcutaneous injection of GERM 11 cells and 3 independent b1 integrin expressing sublines (GERM 116, 1A10, 2F2) into syngeneic mice. After 10 days tumors were surgically removed. While average weights of GERM 11 and GERM 116 tumors were similar, tumors induced by the high expressing clones 1A10 and 2F2 were markedly smaller, suggesting an inverse correlation of tumor growth and b1 integrin expression. The metastasis potential of all three b1 integrin-expressing GERM 11 sublines tested was signi®cantly higher than that of the b1-de®cient GERM 11 cells. GERM 116 tumors led in all animals to severe metastasis in lung and liver, while GERM 11 tumors induced only a few metastatic foci in the lung. Stroma of both tumors contained nidogen and high amounts of tenascin C, but only a few very low levels of ®bronectin, laminin-1, and collagen type I. b1 integrin, therefore, increases but is not essential for metastasis of ras-myc transformed ®broblasts.

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“…The pH and the oxygen levels are low, and the degree of attachment is compromised because cells are rapidly dividing and often motile, and the NHE is more active. Various integrin isoforms are expressed differently in tumors relative to normal tissue [Schwartz et al, 1991;Coopman et al, 1996;Erdreich-Epstein et al, 2000], which could have secondary effects on localization of other cell surface molecules and activities. When extracellular pH is low, typically the sodium/proton antiporter, isoform 1 (NHE1) is activated to maintain intracellular pH in the viable range.…”

Section: Other Factors Affecting Regulation Ofmentioning

confidence: 99%

Angiostatin's molecular mechanism: Aspects of specificity and regulation elucidated

Wahl

Kenan

Gonzalez-Gronow

et al. 2005

J of Cellular Biochemistry

114

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Tumor growth requires the development of new vessels that sprout from pre-existing normal vessels in a process known as ''angiogenesis'' [Folkman (1971) N Engl J Med 285:1182-1186. These new vessels arise from local capillaries, arteries, and veins in response to the release of soluble growth factors from the tumor mass, enabling these tumors to grow beyond the diffusion-limited size of approximately 2 mm diameter. Angiostatin, a naturally occurring inhibitor of angiogenesis, was discovered based on its ability to block tumor growth in vivo by inhibiting the formation of new tumor blood vessels [O'Reilly et al. (1994a) Cold Spring Harb Symp Quant Biol 59:471-482]. Angiostatin is a proteolytically derived internal fragment of plasminogen and may contain various members of the five plasminogen ''kringle'' domains, depending on the exact sites of proteolysis. Different forms of angiostatin have measurably different activities, suggesting that much remains to be elucidated about angiostatin biology. A number of groups have sought to identify the native cell surface binding site(s) for angiostatin, resulting in at least five different binding sites proposed for angiostatin on the surface of endothelial cells (EC). This review will consider the data supporting all of the various reported angiostatin binding sites and will focus particular attention on the angiostatin binding protein identified by our group: F 1 F O ATP synthase. There have been several developments in the quest to elucidate the mechanism of action of angiostatin and the regulation of its receptor. The purpose of this review is to describe the highlights of research on the mechanism of action of angiostatin, its' interaction with ATP synthase on the EC surface, modulators of its activity, and issues that should be explored in future research related to angiostatin and other anti-angiogenic agents.

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Integrin alpha 3 beta 1 participates in the phagocytosis of extracellular matrix molecules by human breast cancer cells.

Cited by 78 publications

References 53 publications

An invasion-related complex of cortactin, paxillin and PKCμ associates with invadopodia at sites of extracellular matrix degradation

An invasion-related complex of cortactin, paxillin and PKCμ associates with invadopodia at sites of extracellular matrix degradation

β1 integrin promotes but is not essential for metastasis of ras-myc transformed fibroblasts

Angiostatin's molecular mechanism: Aspects of specificity and regulation elucidated

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