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Prepublished online as a Blood First Edition Paper on April 24, 2003; DOI 10.1182/blood-2003-02-0591. This Article Full Text (PDF) All Versions of this Article: 2003-02-0591v1 102/4/1355    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 Naik, U. P Articles by Naik, M. U Search for Related Content PubMed PubMed Citation Articles by Naik, U. P Articles by Naik, M. U Social Bookmarking                   What's this? Submitted February 24, 2003 Accepted April 8, 2003 Association of CIB with GPIIb/IIIa during outside-in signaling is required for platelet spreading on fibrinogen Ulhas P Naik* and Meghna U Naik Department of Biological Sciences, University of Delaware, Newark, DE, USA * Corresponding author; email: unaik{at}udel.edu. Platelet spreading on immobilized fibrinogen (Fg) involves progression through a number of morphological stages, which, although distinctive, are not mechanistically well-understood. Here we demonstrate that an association between GPIIb/IIIa and calcium- and integrin-binding protein (CIB) is required for the process of platelet spreading. Upon platelet adhesion to immobilized Fg, CIB localizes to the transiently formed filopodia, and then redistributes diffusely along the membrane periphery of spread platelets. Immunoprecipitation analyses indicate that CIB and GPIIb/IIIa interact with each other as platelets adhere to immobilized Fg, and together they associate with the platelet cytoskeleton. Introduction of anti-CIB antibody or GPIIb cytoplasmic peptide into platelets blocks lamellipodia but not filopodia formation. GPIIb peptide-induced inhibition of platelet spreading is recovered by the incorporation of recombinant CIB protein, suggesting that interaction between CIB and GPIIb/IIIa is required for progression from filopodial to spread morphologies. Further, anti-CIB or GPIIb peptide-induced inhibition of platelet spreading can be overcome by the addition of exogenous adenosine diphosphate (ADP). These data suggest that formation of the CIB-GPIIb/IIIa complex may be necessary for initiation of downstream signaling events such as ADP secretion, which lead to platelet spreading. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? 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