Human platelets and glomerular basal lamina interaction.
Collagen is one of the major constituents of glomerular basal lamina. Its thrombogenecity has been systematically studied in our laboratory by aggregometry, adenine nucleotide release assay, and electron microscopy. The purified human glomerular basal lamina (HGBL) preparation does not induce platelet degranulation, nucleotide release, or aggregation, although adhesion and spreading of platelets on HGBL are observed. Isolated monomeric HGBL collagen or insoluble HGBL collagen in its native state of organization are similarly inactive. Modification of carbohydrate moieties by sialase, alpha-glucosidase, or sodium periodate oxidation has no effect on HGBL's inability to induce platelet release reaction or aggregation. Therefore, HGBL collagen is not thrombogenic as has been suspected. Adhesion and spreading of platelets on HGBL, which require the noncollagen constituents of HGBL and divalent cations, represent a temporary capillary pavement for endothelial defect distinct from thrombogenic activity of platelets.
D000227:Adenine Nucleotides / Q000378:metabolism; D001485:Basement Membrane / Q000502:physiology*; D001777:Blood Coagulation; D001792:Blood Platelets / Q000502:physiology*; D003094:Collagen / Q000032:analysis / Q000502:physiology*; D006801:Humans; D007678:Kidney Glomerulus / Q000098:blood supply*; D046911:Macromolecular Substances; D008859:Microscopy, Polarization; D010973:Platelet Adhesiveness; D010974:Platelet Aggregation; D012107:Research Design
D000227:Adenine Nucleotides; D046911:Macromolecular Substances; D003094:Collagen