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This Article Full Text Full Text (PDF) 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 Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Tadokoro, S. Articles by Matsuzawa, Y. Search for Related Content PubMed PubMed Citation Articles by Tadokoro, S. Articles by Matsuzawa, Y. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  Blood, 1 February 2002, Vol. 99, No. 3, pp. 931-938 HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY Missense mutations in the 3 subunit have a different impact on the expression and function between IIb3 and v3 Seiji Tadokoro, Yoshiaki Tomiyama, Shigenori Honda, Hirokazu Kashiwagi, Satoru Kosugi, Masamichi Shiraga, Teruo Kiyoi, Yoshiyuki Kurata, and Yuji Matsuzawa From Department of Internal Medicine and Molecular Science, Graduate School of Medicine, Osaka University, Japan; and Department of Blood Transfusion, Osaka University Hospital, Japan. IIb3 and v3 belong to the 3 integrin subfamily. Although the 3 subunit is a key regulator for the biosynthesis of 3 integrins, it remains obscure whether missense mutations in 3 may induce the same defects in both IIb3 and v3. In this study, it is revealed that thrombasthenic platelets with a His280Pro mutation in 3, which is prevalent in Japanese patients with Glanzmann thrombasthenia, did contain significant amounts of v3 (about 50% of control) using sensitive enzyme-linked immunosorbent assay. Expression studies showed that the His280Pro3 mutation impaired IIb3 expression but not v3 expression in 293 cells. To extend these findings, the effects of several 3 missense mutations leading to an impaired IIb3 expression on v3 function as well as expression was examined: Leu117Trp, Ser162Leu, Arg216Gln, Cys374Tyr, and a newly created Arg216Gln/Leu292Ser mutation. Leu117Trp and Cys374Tyr 3 mutations did impair v3 expression, while Ser162Leu, Arg216Gln, and Arg216Gln/Leu292Ser mutations did not. With regard to ligand binding function, Ser162Leu mutation induced especially distinct effects between 2 3 integrins: it markedly impaired ligand binding to IIb3 but not to v3 at all. These data clearly demonstrate that the biosynthesis and the ligand binding function of IIb3 and those of v3 are regulated in part by different mechanisms. Present data would be a clue to elucidate the regulatory mechanism of expression and function of 3 integrins. © 2002 by The American Society of Hematology.   CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: T. Kiyoi, Y. Tomiyama, S. Honda, S. Tadokoro, M. Arai, H. Kashiwagi, S. Kosugi, H. Kato, Y. Kurata, and Y. Matsuzawa A naturally occurring Tyr143Hisalpha IIb mutation abolishes alpha IIbbeta 3 function for soluble ligands but retains its ability for mediating cell adhesion and clot retraction: comparison with other mutations causing ligand-binding defects Blood, May 1, 2003; 101(9): 3485 - 3491. [Abstract] [Full Text] [PDF]

	Copyright © 2002 by American Society of Hematology         Online ISSN: 1528-0020