SEARCH:   Advanced

This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Verkleij, M. W. Articles by Sixma, J. J. Search for Related Content PubMed PubMed Citation Articles by Verkleij, M. W. Articles by Sixma, J. J. Related Collections Hemostasis, Thrombosis, and Vascular Biology Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Simple Collagen-Like Peptides Support Platelet Adhesion Under Static But Not Under Flow Conditions: Interaction Via 21 and von Willebrand Factor With Specific Sequences in Native Collagen Is a Requirement to Resist Shear Forces Marilyn W. Verkleij, Laurence F. Morton, C. Graham Knight, Philip G. de Groot, Michael J. Barnes, and Jan J. Sixma From the Postgradual School of Biomembranes, Department of Haematology, University Hospital Utrecht, Utrecht, The Netherlands; and the Strangeways Research Laboratory, Worts Causeway, Cambridge, UK. The aim of this study was to define the need for specific collagen sequences and the role of their conformation in platelet adhesion to collagen under both static and flow conditions. We recently reported that simple triple-helical collagen-related peptides (CRPs), GCP*(GPP*)10GCP*G and GKP*(GPP*)10GKP*G (single-letter amino acid code, P* = hydroxyproline; Morton et al, Biochem J 306:337, 1995) were potent stimulators of platelet activation and were able to support the adhesion of gel-filtered platelets examined under static conditions. The present study investigated whether these same peptides were able to support platelet adhesion under more physiologic conditions by examining static adhesion with platelet-rich plasma (PRP) and adhesion under flow conditions. In the static adhesion assay, we observed 20% surface coverage with platelet aggregates. In marked contrast, there was a total lack of adhesion under flow conditions examined at shear rates of 50 and 300 s1. Thus, the interaction of platelets with the CRPs is a low-affinity interaction unable on its own to withstand shear forces. However, the addition of CRPs to whole blood, in the presence of 200 µmol/L D-arginyl-glycyl-L-aspartyl-L-tryptophan (dRGDW) to prevent platelet aggregation, caused an inhibition of about 50% of platelet adhesion to collagens I and III under flow. These results suggest that the collagen triple helix per se, as defined by these simple collagen sequences, plays an important contributory role in the overall process of adhesion to collagen under flow. The monoclonal antibody (MoAb) 176D7, directed against the 2 subunit of the integrin 21, was found to inhibit static platelet adhesion to monomeric but not fibrillar collagens I and III. However, under flow conditions, anti-2 MoAbs (176D7 anf 6F1) inhibited adhesion to both monomeric and fibrillar collagens, indicating that 21 is essential for adhesion to collagen under flow, independent of collagen conformation, whether monomeric or polymeric. To obtain further insight into the nature of the different adhesive properties of CRPs and native collagen, we investigated the relative importance of von Willebrand factor (vWF) and the integrin 21 in platelet adhesion to collagen types I and III, using the same shear rate (300 s1) as used when testing CRPs under flow conditions. Our results, together with recent data of others, support a two-step mechanism of platelet interaction with collagen under flow conditions. The first step involves adhesion via both the indirect interaction of platelet glycoprotein (GP) Ib with collagen mediated by vWF binding to specific vWF-recognition sites in collagen and the direct interaction between platelet 21 and specific 21-recognition sites in collagen. This suffices to hold platelets at the collagen surface. The second step occurs via another collagen receptor (thought to be GPVI) that binds to simple collagen sequences, required essentially to delineate the collagen triple helix. Recognition of the triple helix leads to strengthening of attachment and platelet activation. Blood, Vol. 91 No. 10 (May 15), 1998: pp. 3808-3816 © 1998 by The American Society of Hematology. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: J. S. Isenberg, M. J. Romeo, C. Yu, C. K. Yu, K. Nghiem, J. Monsale, M. E. Rick, D. A. Wink, W. A. Frazier, and D. D. Roberts Thrombospondin-1 stimulates platelet aggregation by blocking the antithrombotic activity of nitric oxide/cGMP signaling Blood, January 15, 2008; 111(2): 613 - 623. [Abstract] [Full Text] [PDF] A. von Sengbusch, P. Gassmann, K. M. Fisch, A. Enns, G. L. Nicolson, and J. Haier Focal Adhesion Kinase Regulates Metastatic Adhesion of Carcinoma Cells within Liver Sinusoids Am. J. Pathol., February 1, 2005; 166(2): 585 - 596. [Abstract] [Full Text] [PDF] P. R.-M. Siljander, S. Hamaia, A. R. Peachey, D. A. Slatter, P. A. Smethurst, W. H. Ouwehand, C. G. Knight, and R. W. Farndale Integrin Activation State Determines Selectivity for Novel Recognition Sites in Fibrillar Collagens J. Biol. Chem., November 12, 2004; 279(46): 47763 - 47772. [Abstract] [Full Text] [PDF] P. MAURICE, C. LEGRAND, and F. FAUVEL-LAFEVE Platelet adhesion and signaling induced by the octapeptide primary binding sequence (KOGEOGPK) from type III collagen FASEB J, September 1, 2004; 18(12): 1339 - 1347. [Abstract] [Full Text] [PDF] P. R.-M. Siljander, I. C. A. Munnix, P. A. Smethurst, H. Deckmyn, T. Lindhout, W. H. Ouwehand, R. W. Farndale, and J. W. M. Heemskerk Platelet receptor interplay regulates collagen-induced thrombus formation in flowing human blood Blood, February 15, 2004; 103(4): 1333 - 1341. [Abstract] [Full Text] [PDF] D. Best, Y. A. Senis, G. E. Jarvis, H. J. Eagleton, D. J. Roberts, T. Saito, S. M. Jung, M. Moroi, P. Harrison, F. R. Green, et al. GPVI levels in platelets: relationship to platelet function at high shear Blood, October 15, 2003; 102(8): 2811 - 2818. [Abstract] [Full Text] [PDF] R. Polanowska-Grabowska, J. M. Gibbins, and A. R.L. Gear Platelet Adhesion to Collagen and Collagen-Related Peptide Under Flow: Roles of the {alpha}2{beta}1 Integrin, GPVI, and Src Tyrosine Kinases Arterioscler Thromb Vasc Biol, October 1, 2003; 23(10): 1934 - 1940. [Abstract] [Full Text] [PDF] J. Lahav, E. M. Wijnen, O. Hess, S. W. Hamaia, D. Griffiths, M. Makris, C. G. Knight, D. W. Essex, and R. W. Farndale Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin {alpha}2{beta}1 Blood, September 15, 2003; 102(6): 2085 - 2092. [Abstract] [Full Text] [PDF] B. Nieswandt and S. P. Watson Platelet-collagen interaction: is GPVI the central receptor? Blood, July 15, 2003; 102(2): 449 - 461. [Abstract] [Full Text] [PDF] D. Patel, H. Vaananen, M. Jirouskova, T. Hoffmann, C. Bodian, and B. S. Coller Dynamics of GPIIb/IIIa-mediated platelet-platelet interactions in platelet adhesion/thrombus formation on collagen in vitro as revealed by videomicroscopy Blood, February 1, 2003; 101(3): 929 - 936. [Abstract] [Full Text] [PDF] D. Bouvard, C. Brakebusch, E. Gustafsson, A. Aszodi, T. Bengtsson, A. Berna, and R. Fassler Functional Consequences of Integrin Gene Mutations in Mice Circ. Res., July 30, 2001; 89(3): 211 - 223. [Abstract] [Full Text] [PDF] B. Nieswandt, W. Bergmeier, A. Eckly, V. Schulte, P. Ohlmann, J.-P. Cazenave, H. Zirngibl, S. Offermanns, and C. Gachet Evidence for cross-talk between glycoprotein VI and Gi-coupled receptors during collagen-induced platelet aggregation Blood, June 15, 2001; 97(12): 3829 - 3835. [Abstract] [Full Text] [PDF] M. Roest, J. D. Banga, D. E. Grobbee, P. G. de Groot, J. J. Sixma, M. J. Tempelman, and Y. T. van der Schouw Homozygosity for 807 T Polymorphism in {alpha}2 Subunit of Platelet {alpha}2{beta}1 Is Associated With Increased Risk of Cardiovascular Mortality in High-Risk Women Circulation, October 3, 2000; 102(14): 1645 - 1650. [Abstract] [Full Text] [PDF] M. Jandrot-Perrus, S. Busfield, A.-H. Lagrue, X. Xiong, N. Debili, T. Chickering, J.-P. L. Couedic, A. Goodearl, B. Dussault, C. Fraser, et al. Cloning, characterization, and functional studies of human and mouse glycoprotein VI: a platelet-specific collagen receptor from the immunoglobulin superfamily Blood, September 1, 2000; 96(5): 1798 - 1807. [Abstract] [Full Text] [PDF] M. Roest, J. J. Sixma, Y.-P. Wu, M. J. W. Ijsseldijk, M. Tempelman, P. J. Slootweg, P. G. de Groot, and G. H. van Zanten Platelet adhesion to collagen in healthy volunteers is influenced by variation of both alpha 2beta 1 density and von Willebrand factor Blood, August 15, 2000; 96(4): 1433 - 1437. [Abstract] [Full Text] [PDF] N. von Beckerath, W. Koch, J. Mehilli, C. Bottiger, A. Schomig, and A. Kastrati Glycoprotein Ia gene C807T polymorphism and risk for major adverse cardiac events within the first 30 days after coronary artery stenting Blood, June 1, 2000; 95(11): 3297 - 3301. [Abstract] [Full Text] [PDF] E. Monnet and F. Fauvel-Lafeve A New Platelet Receptor Specific to Type III Collagen. TYPE III COLLAGEN-BINDING PROTEIN J. Biol. Chem., April 6, 2000; 275(15): 10912 - 10917. [Abstract] [Full Text] [PDF] C. Smith, D. Estavillo, J. Emsley, L. A. Bankston, R. C. Liddington, and M. A. Cruz Mapping the Collagen-binding Site in the I Domain of the Glycoprotein Ia/IIa (Integrin alpha 2beta 1) J. Biol. Chem., February 11, 2000; 275(6): 4205 - 4209. [Abstract] [Full Text] [PDF] D. Estavillo, A. Ritchie, T. G. Diacovo, and M. A. Cruz Functional Analysis of a Recombinant Glycoprotein Ia/IIa (Integrin alpha 2beta 1) I Domain That Inhibits Platelet Adhesion to Collagen and Endothelial Matrix under Flow Conditions J. Biol. Chem., December 10, 1999; 274(50): 35921 - 35926. [Abstract] [Full Text] [PDF] P. Siljander and R. Lassila Studies of Adhesion-Dependent Platelet Activation : Distinct Roles for Different Participating Receptors Can Be Dissociated by Proteolysis of Collagen Arterioscler Thromb Vasc Biol, December 1, 1999; 19(12): 3033 - 3043. [Abstract] [Full Text] [PDF] T. Nakamura, J.-i. Kambayashi, M. Okuma, and N. N. Tandon Activation of the GP IIb-IIIa Complex Induced by Platelet Adhesion to Collagen Is Mediated by Both {alpha}2{beta}1 Integrin and GP VI J. Biol. Chem., April 23, 1999; 274(17): 11897 - 11903. [Abstract] [Full Text] [PDF] C.G. Knight, L. F Morton, D. J Onley, A. R Peachey, T. Ichinohe, M. Okuma, R. W Farndale, and M. J Barnes Collagen-platelet interaction: Gly-Pro-Hyp is uniquely specific for platelet Gp VI and mediates platelet activation by collagen Cardiovasc Res, February 1, 1999; 41(2): 450 - 457. [Abstract] [Full Text] [PDF] D. J. Onley, C. G. Knight, D. S. Tuckwell, M. J. Barnes, and R. W. Farndale Micromolar Ca2+ Concentrations Are Essential for Mg2+-dependent Binding of Collagen by the Integrin alpha 2beta 1 in Human Platelets J. Biol. Chem., August 4, 2000; 275(32): 24560 - 24564. [Abstract] [Full Text] [PDF] K. Suzuki-Inoue, Y. Ozaki, M. Kainoh, Y. Shin, Y. Wu, Y. Yatomi, T. Ohmori, T. Tanaka, K. Satoh, and T. Morita Rhodocytin Induces Platelet Aggregation by Interacting with Glycoprotein Ia/IIa (GPIa/IIa, Integrin alpha 2beta 1). INVOLVEMENT OF GPIa/IIa-ASSOCIATED Src AND PROTEIN TYROSINE PHOSPHORYLATION J. Biol. Chem., January 5, 2001; 276(2): 1643 - 1652. [Abstract] [Full Text] [PDF] M. Achison, C. M. Elton, P. G. Hargreaves, C. G. Knight, M. J. Barnes, and R. W. Farndale Integrin-independent Tyrosine Phosphorylation of p125fak in Human Platelets Stimulated by Collagen J. Biol. Chem., January 26, 2001; 276(5): 3167 - 3174. [Abstract] [Full Text] [PDF]

	Copyright © 1998 by American Society of Hematology         Online ISSN: 1528-0020