Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen

Santoro, Samuel A.

doi:10.1016/0092-8674(86)90073-5

Cited by 386 publications

(261 citation statements)

References 29 publications

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“…In the presence of Mg2+ and Ca2+, similar to the in vivo situation, the affinity of alp1 for collagen IV was five-times higher than for a2pl. Similar inhibitory or regulatory effects of Ca2+ were observed for the adhesion of platelets to collagen and the binding of a2p1 to collagen ligands (Santoro, 1986;Grzesiak et al, 1992). alp1 and a2pl are described as typical collagen and laminin receptors (Tomaselli et al, 1988;Kramer and Marks, 1989;Clyman et al, 1990;Staats et al, 1989;Ignatius et al, 1990;Hynes, 1987;Hall et al, 1990;Languino et al, 1989).…”

Section: Discussionmentioning

confidence: 70%

Interaction of type IV collagen with the isolated integrins α1β1 and α2β1

Kern

Eble

Golbik

et al. 1993

European Journal of Biochemistry

199

188

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The triple-helical cyanogen-bromide-derived fragment CB3 [IV] of collagen IV, located 100 nm from the N-terminus of the molecule, contains the binding sites for the integrins alp1 and a2pl. To investigate the interaction of these integrins and collagen IV, we performed solid-phase and inhibition assays using as receptor isolated alp1 and a2pl. The ligands used were the binding-site-bearing trimeric peptide CB3 [IV] and its shorter tryptic fragments Fl-F4. Using titration curves, in which the binding of soluble receptors to coated ligands and the binding of soluble ligands to coated receptors were analyzed, the binding sites for alp1 and a2pl were in different but adjacent areas of CB3 [IV]. Triple-helical conformation and distinct primary structures were required for the interaction. Dissociation constants (Kd), for the affinity of integrins for collagen IV, were determined in the 1-nM range in the presence of Mn2+ and Mg". In the absence of Mn2+, the Kd values indicated a 30-60-fold decrease in the affinities, which for a2pl was further reduced by adding Ca". In the presence of Ca2+ and Mg2+ the affinity of collagen IV for alp1 was four-times higher than for a2pl.

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Section: Discussionmentioning

confidence: 70%

Interaction of type IV collagen with the isolated integrins α1β1 and α2β1

Kern

Eble

Golbik

et al. 1993

European Journal of Biochemistry

199

188

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“…A possible explanation is that due to their triple-helical nature, these RGD sequences are not accessible to integrins. However, cell adhesion to collagen IV is predominantly dependent on triple-helical state of collagen IV, since reduction of disulfide bonds followed by heat-denaturation dramatically decreases cell binding and spreading (Aumailley and Timpl, 1986;Perris et al, 1993;Santoro, 1986).…”

Section: Integrin Receptorsmentioning

confidence: 99%

“…This interaction is critical for a variety of biological processes, including cell adhesion, migration, survival, proliferation, and differentiation. Cell culture studies have shown that collagen IV is the binding substrate for a large number of cell types including platelets (Santoro, 1986;Staatz et al, 1990), hepatocytes (Rubin et al, 1981), keratinocytes (Murray et al, 1979), endothelial (Cheng and Kramer, 1989;Herbst et al, 1988), mesangial (Setty et al, 1998), pancreatic (Kaido et al, 2004), and tumor cells such as breast and prostate carcinoma (Abecassis et al, 1987;Dedhar et al, 1993), melanoma (Chelberg et al, 1989), fibrosarcoma, and glioma (Aumailley and Timpl, 1986;Knight et al, 2000). Cell attachment to collagen IV is mediated by multiple binding sites within both triple-helical and NC1 domains, suggesting involvement of several adhesion receptors (Chelberg et al, 1989;Herbst et al, 1988;Wayner and Carter, 1987).…”

Section: Interaction To Cell Surface Receptorsmentioning

confidence: 99%

Mammalian collagen IV

Khoshnoodi

Pedchenko

Hudson

2008

Microscopy Res & Technique

554

487

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Four decades have passed since the first discovery of collagen IV by Kefalides in 1966. Since then collagen IV has been investigated extensively by a large number of research laboratories around the world. Advances in molecular genetics have resulted in identification of six evolutionary related mammalian genes encoding six different polypeptide chains of collagen IV. The genes are differentially expressed during the embryonic development, providing different tissues with specific collagen IV networks each having unique biochemical properties. Newly translated α-chains interact and assemble in the endoplasmic reticulum in a chain-specific fashion and form unique heterotrimers. Unlike most collagens, type IV collagen is an exclusive member of the basement membranes and through a complex inter-and intramolecular interactions form supramolecular networks that influence cell adhesion, migration, and differentiation. Collagen IV is directly involved in a number of genetic and acquired disease such as Alport's and Goodpasture's syndromes. Recent discoveries have also highlighted a new and direct role for collagen IV in the development of rare genetic diseases such as cerebral hemorrhage and porencephaly in infants and hemorrhagic stroke in adults. Years of intensive investigations have resulted in a vast body of information about the structure, function, and biology of collagen IV. In this review article, we will summarize essential findings on the structural and functional relationships of different collagen IV chains and their roles in health and disease.

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“…Despite this central role, its molecular basis of action remains unclear and its receptor is not defined although several candidates have been proposed. Among those put forward as the collagen receptor are the integrin M2A1 (Niewenhuis et al, 1985;Santoro, 1986;Coller et al, 1989), glycoprotein IV (CD36) (Tandon et al, 1989), Clq (or collectin) receptor (Peerschke et al, 1993) and several uncharacterized surface proteins including p62 (Sugiyama et al, 1987), p47 (Chiang et al, 1993) and p65 (Chiang & Kang, 1982). None of these is known to possess the seven-transmembrane domain architecture associated with G protein-coupled receptors.…”

Section: Introductionmentioning

confidence: 99%

Regulation of cytosolic calcium by collagen in single human platelets

Poole

Watson

1995

British J Pharmacology

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There is controversy in the literature as to whether collagen is able to induce directly a rise in cytosolic calcium concentration ([Ca2+]i) in human platelets. We have addressed this question by observing the cytosolic calcium response of single fura‐2‐loaded human platelets settling onto a collagen‐coated surface using dynamic fluorescence ratio imaging. Following a short lag phase after adherence to collagen fibres, platelets underwent a rapid rise in cytosolic calcium from basal values of 80 ± 13 nM (n = 24) to a peak of 475 ± 42 nM (n = 24) which was sustained for the remaining period of the experiment. The tyrphostin protein tyrosine kinase inhibitor, ST271, reduced substantially the proportion of platelets which exhibited a rise in [Ca2+]i on adherence to collagen and transformed the response in remaining cells to one of oscillations. In contrast, and as a control for collagen, laminin‐coated surfaces induced adherence of human platelets without elevating intracellular [Ca2+]; the cells however remained responsive to ADP. We conclude that collagen directly induces a rise in cytosolic calcium in single human platelets through a tyrosine kinase‐mediated pathway.

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Identification of a 160,000 dalton platelet membrane protein that mediates the initial divalent cation-dependent adhesion of platelets to collagen

Cited by 386 publications

References 29 publications

Interaction of type IV collagen with the isolated integrins α1β1 and α2β1

Interaction of type IV collagen with the isolated integrins α1β1 and α2β1

Mammalian collagen IV

Regulation of cytosolic calcium by collagen in single human platelets

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