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• W38376687 abstract "Domains 3 and 5 of high-molecular-weight kininogen (HK) have been shown to bind to platelets in a zinc-dependent reaction. However, the platelet-binding proteins responsible for this interaction have not been identified. We have focused on the platelet-binding site for the heavy chain (domain 3), which we approached using a domain 3-derived peptide ligand and isolated binding proteins by affinity chromatography. The domain 3-derived peptide, thrombin, HK, factor XII, as well as antibody to glycocalicin (the N-terminal portion of the alpha chain of GPIb) recognized a protein at 74 kD. We also isolated the thrombin receptor (PAR 1) at 45 kD, however, none of the above-mentioned ligands bound to this protein. Isolation of platelet membrane proteins using a monoclonal anti-glycocalicin antibody column revealed the same HK binding protein at 74 kD, which was reactive with anti-GPIb and represents a GPIb fragment. By photoaffinity labeling, HK interacted with membrane GPIb, which was then isolated in native form (135 kD) along with gC1qR, a ligand for the HK light chain. Finally, (125)I-HK binding to platelets was significantly inhibited by the anti-GPIb antibody. These results suggest that the GPIb alpha chain, a known thrombin binding protein, is also one of the zinc-dependent platelet membrane binding sites for HK domain 3." @default.
• W38376687 created "2016-06-24" @default.
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• W38376687 date "1999-08-01" @default.
• W38376687 modified "2023-10-17" @default.
• W38376687 title "Platelet Glycoprotein Ib: A Zinc-Dependent Binding Protein for the Heavy Chain of High-Molecular-Weight Kininogen" @default.
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• W38376687 doi "https://doi.org/10.1007/bf03401982" @default.
• W38376687 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2230456" @default.
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