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Histidine-proline-rich glycoprotein binding to platelets mediated by transition metals.

Authors
  • Horne, M K 3rd
  • Merryman, P K
  • Cullinane, A M
Type
Published Article
Journal
Thrombosis and haemostasis
Publication Date
May 01, 2001
Volume
85
Issue
5
Pages
890–895
Identifiers
PMID: 11372684
Source
Medline
License
Unknown

Abstract

Histidine-proline-rich glycoprotein (HPRG) binds zinc, which in turn promotes HPRG binding to lymphocytes and monocytes. We examined the possibility that zinc and other transition metals also promote HPRG binding to platelets. Only non-specific, unsaturable association of HPRG with resting or activated platelets was observed in the absence of transition metals. However, nickel, cobalt, copper, cadmium, and zinc greatly increased HPRG association with the cells. In the presence of zinc, specific, saturable binding of HPRG to platelets was demonstrated. The cell binding capacity for HPRG could be increased by increasing the zinc saturation of HPRG from 10% to 30% as well as by activating the platelets with thrombin. Because platelets contain relatively high concentrations of secretable zinc, it is possible that significant amounts of HPRG bind to activated platelets at sites of blood clotting and that this has a physiologic function.

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