| Autor: |
Chain, Daniel, Kreizman, Tamar, Shapira, Hadar, Shaltiel, Shmuel |
| Zdroj: |
FEBS Letters; January 1991, Vol. 285 Issue: 2 p251-256, 6p |
| Abstrakt: |
Plasmin is shown to specifically cleave vitronectin at the Arg 361-Ser 362bond, 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 Ser 378with 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. |
| Databáze: |
Supplemental Index |
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