PMID: 2114094Jun 1, 1990Paper

Platelet adhesion to collagen. Factors affecting Mg2(+)-dependent and bivalent-cation-independent adhesion

The Biochemical Journal
L S ZijenahM J Barnes

Abstract

Platelet adhesion to collagens immobilized on plastic has been measured, with the following results. (1) Human, but not rabbit, platelets adhered readily to pepsin-extracted monomeric collagens in an Mg2(+)-dependent manner. (2) Rabbit platelets adhered to a monomeric collagen extracted without pepsin by a process that was cation-independent; human platelet adhesion to this collagen exhibited a cation-independent element. (3) Human platelet adhesion to polymeric collagens, including intact native fibres and those reconstituted from pepsin-extracted monomeric collagens, exhibited appreciable cation-independence; adhesion of rabbit platelets to these collagens occurred only by a cation-independent process; pepsin treatment of the intact fibres caused a reduction in cation-independent binding. Two mechanisms of adhesion can therefore be distinguished, one Mg2(+)-dependent, expressed by human, but not rabbit, platelets, the other cation-independent and exhibited by platelets of both species. Mg2(+)-dependent and cation-independent adhesion sites are located within the triple helix of collagen, but the latter sites are only expressed in collagen in polymeric form. In neither case is the helical conformation of the sites essential fo...Continue Reading

Citations

Jul 26, 2002·Blood Coagulation & Fibrinolysis : an International Journal in Haemostasis and Thrombosis·P A Whiss, R G G Andersson
Mar 15, 1997·Journal of Biomedical Materials Research·G A SkarjaJ L Brash
Feb 29, 2008·Blood·Gavin E JarvisRichard W Farndale
Jul 1, 1996·Arteriosclerosis, Thrombosis, and Vascular Biology·M Diaz-RicartG A Jamieson
May 10, 1996·Journal of Immunological Methods·M ChibaU Specks
Nov 15, 1993·Thrombosis Research·L F MortonM J Barnes

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