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Prepublished online as a Blood First Edition Paper on November 21, 2002; DOI 10.1182/blood-2002-05-1363. This Article Full Text (PDF) All Versions of this Article: 2002-05-1363v1 101/7/2646    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 Cho, M. J Articles by Gartner, T K. Search for Related Content PubMed PubMed Citation Articles by Cho, M. J Articles by Gartner, T K. Social Bookmarking                   What's this? Submitted May 9, 2002 Accepted November 14, 2002 The roles of IIb3-mediated outside-in signal transduction, thromboxane A2, and adenosine diphosphate in collagen-induced platelet aggregation Moon J Cho, Junling Liu, Tamara I Pestina, Shirley A Steward, Dennis W Thomas, Thomas M Coffman, Demin Wang, Carl W Jackson, and T Kent Gartner* Department of Microbiology and Molecular Cell Sciences, University of Memphis, Memphis, TN, USA Division of Experimental Hematology, St. Jude Children's Research Hospital, Memphis, TN, USA Department of Medicine, Duke University and Durham Veterans Affairs Medical Centers, Durham, NC, USA Blood Research Institute, Blood Center of S.E. Wisconsin, Milwaukee, WI, USA * Corresponding author; email: tgartner{at}memphis.edu. Collagen-induced activation of platelets in suspension leads to IIb3-mediated outside-in signaling, granule release, thromboxane A2 production and aggregation. Although much is known about collagen-induced platelet signaling, the roles of thromboxane A2 production, ADP and dense granule secretion, and IIb3-mediated outside-in signaling in this process are unclear. Here, we demonstrate that thromboxane A2 and ADP are required for collagen-induced platelet activation in response to a low, but not a high level of collagen and that IIb3-mediated outside-in signaling is required, at least in part, for this TxA2 production and ADP secretion. A high level of collagen can activate platelets deficient in PLC2, Gq, or thromboxane A2 receptors, as well as platelets treated with a protein kinase C inhibitor, Ro31-8220. Thus, activation of IIb3 in response to a high level of collagen does not require these signaling proteins. Furthermore, a high level of collagen can cause weak TxA2 and ADP-independent aggregation, but maximal aggregation induced by a high level of collagen requires TxA2 or secretion. 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