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Thrombospondin is the endogenous lectin of human platelets

Nature volume 295, pages 246–248 (1982)Cite this article

Abstract

Platelets activated by α-thrombin change shape from disks to spheres and aggregate. During this sequence of activation, platelets develop a membrane-bound lectin activity1,2 which is expressed after the secretion of intracellular granule contents3. This lectin activity seems to be important in mediating platelet aggregation by binding to a specific receptor on other platelets. Gartner et al.4 have recently shown that fibrinogen is the receptor for the endogenous lectin secreted by activated platelets. Thrombospondin5 (also called glycoprotein G6 and thrombin-sensitive protein7,8) is an α-granule constituent which has a molecular weight (MW) of 450,000 and is a disulphide-linked trimer of 160,000 MW subunits5,9,10. Secreted thrombospondin5–14 binds to platelet membranes in a calcium-dependent manner12. We show here that thrombospondin is the endogenous lectin of human platelets.

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Authors and Affiliations

  1. Department of Medicine, Cornell University Medical College, New York, New York, 10021, USA

    Eric A. Jaffe, Lawrence L. K. Leung, Ralph L. Nachman & Richard I. Levin

  2. Department of Medicine, University of Wisconsin, Madison, Wisconsin, 53706, USA

    Deane F. Mosher

Authors
  1. Eric A. Jaffe
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  2. Lawrence L. K. Leung
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  3. Ralph L. Nachman
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  4. Richard I. Levin
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  5. Deane F. Mosher
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Jaffe, E., Leung, L., Nachman, R. et al. Thrombospondin is the endogenous lectin of human platelets. Nature 295, 246–248 (1982). https://doi.org/10.1038/295246a0

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