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Blood, 15 October 2005, Vol. 106, No. 8, pp. 2744-2749. Prepublished online as a Blood First Edition Paper on July 12, 2005; DOI 10.1182/blood-2005-04-1454. This Article Full Text Full Text (PDF) All Versions of this Article: 2005-04-1454v1 106/8/2744    most recent 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 Kunicki, T. J. Articles by Furihata, K. Search for Related Content PubMed PubMed Citation Articles by Kunicki, T. J. Articles by Furihata, K. Related Collections Hemostasis, Thrombosis, and Vascular Biology Cell Adhesion and Motility Signal Transduction Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY The influence of N-linked glycosylation on the function of platelet glycoprotein VI Thomas J. Kunicki, Yann Cheli, Masaaki Moroi, and Kenichi Furihata From the Division of Experimental Hemostasis and Thrombosis, Department of Molecular and Experimental Medicine, The Scripps Research Institute, La Jolla, CA; and Department of Protein Biochemistry, Institute of Life Science, Kurume University, Kurume, Fukuoka, Japan. Using recombinant human glycoprotein VI (GPVI), we evaluated the effect of N-linked glycosylation at the consensus site Asparagine92-Glycine-Serine94 (N92GS94) on binding of this platelet-specific receptor to its ligands, human type I collagen, collagen-related peptide (CRP), and the snake venom C-type lectin convulxin (CVX). In COS-7 cells transiently transfected with GPVI, deglycosylation with peptide-N-glycosidase F (PNGase F; specific for complex N-linked glycans) or tunicamycin decreases the molecular weight of GPVI and reduces transfected COS-7 cell binding to both CRP and CVX. In stably transfected Dami cells, the substitutions N92A or S94A, but not L95H, resulted in a 30% to 40% decrease in adhesion to CVX, but a 90% or greater decrease in adhesion to CRP and a 65% to 70% decrease in adhesion to type I collagen. Treatment with PNGase F, but not Endoglycosidase H (Endo H) (specific for high-mannose N-linked glycans), produced an equivalent decrease in molecular weight. Neither N92A nor S94A affected the expression of GPVI, based on the direct binding of murine anti–human GPVI monoclonal antibody 204-11 to transfected Dami cells. These findings indicate that N-linked glycosylation at N92 in human GPVI is not required for surface expression, but contributes to maximal adhesion to type I collagen, CRP and, to a lesser extent, CVX. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: A. B. Herr and R. W. Farndale Structural Insights into the Interactions between Platelet Receptors and Fibrillar Collagen J. Biol. Chem., July 24, 2009; 284(30): 19781 - 19785. [Abstract] [Full Text] [PDF] K. Horii, M. L. Kahn, and A. B. Herr Structural basis for platelet collagen responses by the immune-type receptor glycoprotein VI Blood, August 1, 2006; 108(3): 936 - 942. [Abstract] [Full Text] [PDF]

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