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Identification of Tspan9 as a novel platelet tetraspanin and the collagen receptor GPVI as a component of tetraspanin microdomains

Protty, Majd B. and Watkins, Nicholas A and Colombo, Dario and Thomas, Steven G and Heath, Victoria L and Herbert, John and Bicknell, Roy and Senis, Yotis A. and Ashman, Leonie K and Berditchevski, Fedor and Ouwehand, Willem H and Watson, Steve P and Tomlinson, Michael G. (2008) Identification of Tspan9 as a novel platelet tetraspanin and the collagen receptor GPVI as a component of tetraspanin microdomains. Biochemical Journal, 417. pp. 391-400. ISSN 0264-6021

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URL of Published Version: http://www.biochemj.org/bj/417/0391/4170391.pdf

Identification Number/DOI: 10.1042/BJ20081126

Platelets are essential for wound healing and inflammatory processes, but can also play a deleterious role by causing heart attack and stroke. Normal platelet activation is dependent on tetraspanins, a superfamily of glycoproteins that function as ‘organisers’ of cell membranes by recruiting other receptors and signalling proteins into tetraspanin-enriched microdomains. However, our understanding of how tetraspanin microdomains regulate platelets is hindered by the fact that only four of the 33 mammalian tetraspanins have been identified in platelets. This is because of a lack of antibodies to most tetraspanins and difficulties in measuring mRNA, due to low levels in this anucleate cell. To identify potentially platelet-expressed tetraspanins, mRNA was measured in their nucleated progenitor cell, the megakaryocyte, using serial analysis of gene expression and DNA microarrays. Amongst 19 tetraspanins identified in megakaryocytes, Tspan9,a previously uncharacterized tetraspanin, was relatively specific to these cells. Through generating the first Tspan9 antibodies, Tspan9 expression was found to be tightly regulated in platelets. The relative levels of CD9, CD151, Tspan9 and CD63 were 100, 14, 6 and 2, respectively. Since CD9 was expressed at 49000 cell surface copies per platelet, this suggested a copy number of 2800 Tspan9 molecules. Finally, Tspan9 was shown to be a component of tetraspanin microdomains that included the collagen receptor GPVI and integrin α6β1, but not the von Willebrand receptor GPIbα or the integrins αIIbβ3 or α2β1. These findings suggest a role for Tspan9 in regulating platelet function in concert with other platelet tetraspanins and their associated proteins.

Type of Work:Article
Date:16 September 2008 (Publication)
School/Faculty:Schools (1998 to 2008) > School of Medicine
Department:Institute of Biomedical Research, Institute of Cancer Studies
Subjects:R Medicine (General)
Institution:University of Birmingham
Copyright Holders:Portland Press
ID Code:130
Refereed:YES
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