Isolation and characterization of a platelet surface collagen binding complex related to VLA-2

Santoro, Samuel A.; Rajpara, Sanjay; Staatz, William D.; Woods, Virgil L.

doi:10.1016/s0006-291x(88)81211-7

Cited by 139 publications

(62 citation statements)

References 14 publications

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“…Primary breast cancer cell-matrix adhesion of nodenegative women was significantly reduced compared with control wells using the paired Wilcoxon test (Figure 5). Inhibition of breast cancer cell adhesion by monoclonal antibodies in nodenegative women was consistent with previous knowledge of integrin receptor-ligand interactions (Hynes, 1992 (Languino et al, 1989) and collagen (Santoro et al, 1988 to be clarified. The mechanism by which integrin receptors are able to recognize multiple ligands is as yet uncertain.…”

Section: Discussionsupporting

confidence: 89%

Altered cell-matrix contact: a prerequisite for breast cancer metastasis?

Gui

Puddefoot²,

Vinson³

et al. 1997

Br J Cancer

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Summary The integrins are receptors that regulate interaction between epithelial cells and the extracellular matrix. Previous studies have shown that a reduction in the expression of the a2p1, a3p3l, a6p1, av31 and avP5 integrins in primary breast cancer is associated with positive nodal status. In order to assess the functional significance of altered integrin expression, primary breast cancer cells were derived from individual patients with known tumour characteristics using immunomagnetic separation. Purified human fibronectin, vitronectin, laminin and type IV collagen were used to represent the principal extracellular matrix proteins in an in vitro adhesion assay. Primary breast cancer cells from lymph node-positive patients were significantly less adhesive to each of the matrix proteins studied (P<0.001, Mann-Whitney Utest). Matrix adhesion of primary breast cancer cells from node-negative patients was inhibited by appropriate integrin monoclonal antibodies (P<0.001, paired Wilcoxon test). Adhesion to fibronectin, vitronectin and laminin, but not type IV collagen, was influenced by the inhibitor arginine-glycine-aspartate, suggesting that breast cancer cell recognition of collagen IV is mediated through alternative epitopes. Weak matrix adhesion correlated with loss of integrin expression in tissue sections from corresponding patients assessed using immunohistochemistry. This study demonstrates a link between altered integrin expression and function in primary breast cancers predisposed to metastasize.

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Section: Discussionsupporting

confidence: 89%

Altered cell-matrix contact: a prerequisite for breast cancer metastasis?

Gui

Puddefoot²,

Vinson³

et al. 1997

Br J Cancer

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“…Given the observation that SLP-76 is a substrate of tyrosine kinases activated after collagen receptor ligation, these data suggest that SLP-76 functions to couple proximal activation of tyrosine kinases with PLC-γ2 phosphorylation in platelets. Major platelet surface receptors for collagen include the α 2 β 1 integrin (glycoprotein Ia/IIa) and glycoprotein VI (21)(22)(23)(24). While the α 2 β 1 integrin is required for the initial recruitment and adherence of the platelet to the collagen surface, glycoprotein VI has emerged as one of the primary candidates for initiating intracellular signaling after collagen binding (25,26).…”

Section: Resultsmentioning

confidence: 99%

Fetal hemorrhage and platelet dysfunction in SLP-76–deficient mice

Clements¹,

Lee²,

Gross³

et al. 1999

J. Clin. Invest.

165

132

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“…Integrin α2β1 was the first platelet collagen receptor to be identified and binds to collagen in a Mg 2+ -dependent manner (Kunicki et al, 1988;Nieuwenhuis et al, 1985;Santoro, 1986;Santoro et al, 1988;Sixma et al, 1995;Sixma et al, 1997). Integrin α2β1 does not stimulate tyrosine kinase activity, which is required for collagen-induced platelet activation.…”

Section: Integrin α2β1mentioning

confidence: 99%

Platelet adhesion signalling and the regulation of thrombus formation

Gibbins

2004

Journal of Cell Science

257

232

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Platelets perform a central role in haemostasis and thrombosis. They adhere to subendothelial collagens exposed at sites of blood vessel injury via the glycoprotein (GP) Ib-V-IX receptor complex, GPVI and integrin α2β1. These receptors perform distinct functions in the regulation of cell signalling involving non-receptor tyrosine kinases (e.g. Src, Fyn, Lyn, Syk and Btk), adaptor proteins, phospholipase C and lipid kinases such as phosphoinositide 3-kinase. They are also coupled to an increase in cytosolic calcium levels and protein kinase C activation, leading to the secretion of paracrine/autocrine platelet factors and an increase in integrin receptor affinities. Through the binding of plasma fibrinogen and von Willebrand Factor to integrin αIIbβ3, a platelet thrombus is formed. Although increasing evidence indicates that each of the adhesion receptors GPIb-V-IX and GPVI and integrins α2β1 and αIIbβ3 contribute to the signalling that regulates this process, the individual roles of each are only beginning to be dissected. By contrast, adhesion receptor signalling through platelet endothelial cell adhesion molecule 1 (PECAM-1) is implicated in the inhibition of platelet function and thrombus formation in the healthy circulation. Recent studies indicate that understanding of platelet adhesion signalling mechanisms might enable the development of new strategies to treat and prevent thrombosis.

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Isolation and characterization of a platelet surface collagen binding complex related to VLA-2

Cited by 139 publications

References 14 publications

Altered cell-matrix contact: a prerequisite for breast cancer metastasis?

Altered cell-matrix contact: a prerequisite for breast cancer metastasis?

Fetal hemorrhage and platelet dysfunction in SLP-76–deficient mice

Platelet adhesion signalling and the regulation of thrombus formation

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