Thrombospondin is the endogenous lectin of human platelets Academic Article Article uri icon

Overview

MeSH Major

  • Blood Platelets
  • Blood Vessels
  • Purpura
  • Thrombocytopenia

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 activity which is expressed after the secretion of intracellular granule contents. This lectin activity seems to be important in mediating platelet aggregation by binding to a specific receptor on other platelets. Gartner et al. have recently shown that fibrinogen is the receptor for the endogenous lectin secreted by activated platelets. Thrombospondin (also called glycoprotein G and thrombin-sensitive protein) is an α-granule constituent which has a molecular weight (MW) of 450,000 and is a disulphide-linked trimer of 160,000 MW subunits. Secreted thrombospondin binds to platelet membranes in a calcium-dependent manner. We show here that thrombospondin is the endogenous lectin of human platelets.

publication date

  • November 3, 1982

Research

keywords

  • Academic Article

Identity

Digital Object Identifier (DOI)

  • 10.1038/295246a0

PubMed ID

  • 7057888

Additional Document Info

start page

  • 246

end page

  • 8

volume

  • 295

number

  • 5846