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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 (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 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 Social Bookmarking                   What's this? Submitted June 18, 2002 Accepted April 28, 2003 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 Hemostasis Laboratory, Rabin Medical Center-Beilinson Campus, Petah Tikva, Israel Department of Biochemistry, University of Cambridge, Cambridge, United Kingdom Royal Hallamshire Hospital, Department of Hematology, Sheffield, United Kingdom Health Science Center, The University of Texas, San Antonio, TX, USA * Corresponding author; email: jlahav{at}netvision.net.il. Integrin 21 is the principal adhesive receptor for collagen, but platelets also adhere through GPVI. Integrin IIb3 may augment platelet adhesion. We have shown that disulfide exchange is necessary for platelet adhesion to fibrinogen, fibronectin and collagen. However two questions remained: Can activated IIb3 explain the observed role of disulfide exchange in adhesion to collagen, or is this role common to other integrins? and 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: Adhesion to the 21-specific peptide was disulfide-exchange-dependent and 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, purified 21 but not recombinant I-domain depended on free thiols for ligation. 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