FEBS Letters | |
Plasmin cleavage of vitronectin Identification of the site and consequent attenuation in binding plasminogen activator inhibitor‐1 | |
Kreizman, Tamar1  Chain, Daniel1  Shaltiel, Shmuel1  Shapira, Hadar1  | |
[1] Department of Chemical Immunology, The Weizmann Institute of Science, Rehovot, 76100, Israel | |
关键词: Fibrinolysis; PAI-1; Protein kinase-A; Heparin; Extracellular matrix; PAI-1; plasminogen activator inhibitor-1; PKA; cAMP dependent protein kinase (catalytic subunit); V; vitronectin (M r in kDa indicated by subscript); Vn; pure vitronectin as isolated from plasma (containing V75 and V65 + 10); Vn′; plasmin-clipped Vn; | |
DOI : 10.1016/0014-5793(91)80810-P | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
Plasmin is shown to specifically cleave vitronectin at the Arg361-Ser362 bond, 18 amino acid residues upstream from the site of the endogenous cleavage which gives rise to the two-chain form of vitronectin in plasma. The cleavage site is established using the exclusive phosphorylation of Ser378 with protein kinase A. As a result of the plasmin cleavage, the affinity between vitronectin and the type-1 inhibitor of plasminogen activator (PAI-1) is significantly reduced. This cleavage is stimulated by glycosaminoglycans, which are known to anchor vitronectin to the extracellular matrix. A mechanism is proposed through which plasmin can arrest its own production by feedback signalling, unleashing PAI-1 from the immobilized vitronectin found in the vascular subendothelium, which becomes exposed at the locus of a hemostatic event.
【 授权许可】
Unknown
【 预 览 】
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