Literature DB >> 3024762

Divalent cation-dependent and independent surface expression of thrombospondin on thrombin-stimulated human platelets.

M L Aiken, M H Ginsberg, E F Plow.   

Abstract

Thrombospondin (TSP), a platelet alpha-granule protein, becomes expressed on the surface of thrombin-stimulated platelets. The surface expression of this protein occurs through two distinct mechanisms. At low platelet concentrations (1 X 10(8)/mL), a divalent ion-dependent, low-capacity mechanism predominates. At higher cell concentrations, a divalent ion-dependent, higher capacity mechanism prevails that can account for greater than 90% of all the TSP surface expression measured. This mechanism requires the presence of both calcium and magnesium (Ca + Mg). The dependence of the divalent ion-dependent surface expression on platelet concentration suggests that release of the molecule from the cell followed by its binding to the cell surface mediates this component of the endogenous TSP-platelet interaction. These data are consistent with a two-receptor model for the platelet-surface expression of the endogenous TSP pool.

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Year:  1987        PMID: 3024762

Source DB:  PubMed          Journal:  Blood        ISSN: 0006-4971            Impact factor:   22.113


  7 in total

Review 1.  Thrombospondin as a mediator of cancer cell adhesion in metastasis.

Authors:  D A Walz
Journal:  Cancer Metastasis Rev       Date:  1992-11       Impact factor: 9.264

2.  Immunoelectron-microscopic studies of human platelet thrombospondin, von Willebrand factor, and fibrinogen redistribution during clot formation.

Authors:  S C Watkins; V Raso; H S Slayter
Journal:  Histochem J       Date:  1990-09

3.  Thrombospondin-platelet interactions. Role of divalent cations, wall shear rate, and platelet membrane glycoproteins.

Authors:  F R Agbanyo; J J Sixma; P G de Groot; L R Languino; E F Plow
Journal:  J Clin Invest       Date:  1993-07       Impact factor: 14.808

4.  Developmentally regulated expression of a 78 kDa erythroblast membrane glycoprotein immunologically related to the platelet thrombospondin receptor.

Authors:  N Kieffer; A Bettaieb; C Legrand; L Coulombel; W Vainchenker; L Edelman; J Breton-Gorius
Journal:  Biochem J       Date:  1989-09-15       Impact factor: 3.857

5.  Molecular and functional differences induced in thrombospondin-1 by the single nucleotide polymorphism associated with the risk of premature, familial myocardial infarction.

Authors:  Natalya V Narizhneva; Vicky J Byers-Ward; Martin J Quinn; Frank J Zidar; Edward F Plow; Eric J Topol; Tatiana V Byzova
Journal:  J Biol Chem       Date:  2004-03-08       Impact factor: 5.157

6.  Human platelet glycoprotein IIIb binds to thrombospondin fragments bearing the C-terminal region, and/or the type I repeats (CSVTCG motif), but not to the N-terminal heparin-binding region.

Authors:  B Catimel; L Leung; H el Ghissasi; N Mercier; J McGregor
Journal:  Biochem J       Date:  1992-05-15       Impact factor: 3.857

7.  Cell attachment to thrombospondin: the role of ARG-GLY-ASP, calcium, and integrin receptors.

Authors:  J Lawler; R Weinstein; R O Hynes
Journal:  J Cell Biol       Date:  1988-12       Impact factor: 10.539

  7 in total

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