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Prepublished online as a Blood First Edition Paper on June 5, 2003; DOI 10.1182/blood-2002-06-1646. This Article Full Text Full Text (PDF) All Versions of this Article: 2002-06-1646v1 102/6/2085    most recent 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 Lahav, J. Articles by Farndale, R. W. Search for Related Content PubMed PubMed Citation Articles by Lahav, J. Articles by Farndale, R. W. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 15 September 2003, Vol. 102, No. 6, pp. 2085-2092 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Enzymatically catalyzed disulfide exchange is required for platelet adhesion to collagen via integrin 21 Judith Lahav, Eveline M. Wijnen, Oded Hess, Samir W. Hamaia, Delia Griffiths, Michael Makris, C. Graham Knight, David W. Essex, and Richard W. Farndale From the Coagulation Laboratory, Institute of Haematology, Rabin Medical Center–Beilinson Campus, Petah-Tiqva, Israel; Department of Biochemistry, University of Cambridge, United Kingdom; Department of Haematology, Royal Hallamshire Hospital, Sheffield, United Kingdom; and the University of Texas, Health Science Center at San Antonio. Integrin 21 is the principal adhesive receptor for collagen but platelets also adhere through glycoprotein VI (GPVI). Integrin IIb3 may augment platelet adhesion. We have shown that disulfide exchange is necessary for platelet adhesion to fibrinogen, fibronectin, and collagen. However 2 questions remained: (1) Can activated IIb3 explain the observed role of disulfide exchange in adhesion to collagen, or is this role common to other integrins? (2) Is disulfide dependence specific to the integrin receptors or shared with GPVI? To discriminate adhesive functions of 21 from those of IIb3 we used Glanzmann platelets and IIb3-specific antibodies applied to normal platelets. To resolve adhesive events mediated by 21 from those of GPVI we used synthetic peptides specific to each receptor. We addressed direct integrin ligation using purified 21 and recombinant I domain. We observed the following: adhesion to the 21-specific peptide was disulfide-exchange dependent and protein disulfide isomerase (PDI) mediated; membrane-impermeant thiol blockers inhibited 21, but not GPVI mediated, adhesion; direct blockade of PDI revealed that it is involved in adhesion through 21 but not GPVI; and purified 21, but not recombinant I domain, depended on free thiols for ligation. These data suggest that the enzymatically catalyzed adhesion-associated reorganization of disulfide bonds is common to members of the integrin family and specific to this family. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: H. E. van Nispen tot Pannerden, S. M. van Dijk, V. Du, and H. F. G. Heijnen Platelet protein disulfide isomerase is localized in the dense tubular system and does not become surface expressed after activation Blood, November 19, 2009; 114(21): 4738 - 4740. [Abstract] [Full Text] [PDF] J. 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