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J. Biol. Chem., Vol. 277, Issue 48, 45928-45934, November 29, 2002

This Article Full Text Full Text (PDF) All Versions of this Article: 277/48/45928    most recent M206129200v1 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 Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Navdaev, A. Articles by Clemetson, K. J. Search for Related Content PubMed PubMed Citation Articles by Navdaev, A. Articles by Clemetson, K. J. Social Bookmarking                      What's this?

Glycoprotein Ib Cross-linking/Ligation on Echicetin-coated Surfaces or Echicetin-IgM in Stirred Suspension Activates Platelets by Cytoskeleton Modulated Calcium Release^*

Alexey Navdaev and Kenneth J. Clemetson

From the Theodor Kocher Institute, University of Berne, Freiestrasse 1, Berne CH-3012, Switzerland

Cross-linking platelet GPIb with the snake C-type lectin echicetin provides a specific technique for activation via this receptor. This allows GPIb-dependent mechanisms to be studied without the necessity for shear stress-induced binding of von Willebrand factor or primary _IIb3 involvement. We already showed that platelets are activated, including tyrosine phosphorylation, by echicetin-IgM-induced GPIb cross-linking. We now investigate the mechanism further and demonstrate that platelets, without modulator reagents, spread directly on an echicetin-coated surface, by a GPIb-specific mechanism, causing exocytosis of -granule markers (P-selectin) and activation of _IIb3. This spreading requires actin polymerization and release of internal calcium stores but is not dependent on external calcium nor on src family tyrosine kinases. Cross-linking of GPIb complex molecules on platelets, either in suspension or via specific surface attachment, is sufficient to induce platelet activation.

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