Plasmin cleavage of vitronectin Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1

46Citations
Citations of this article
7Readers
Mendeley users who have this article in their library.

Abstract

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. © 1991.

Cite

CITATION STYLE

APA

Chain, D., Kreizman, T., Shapira, H., & Shaltiel, S. (1991). Plasmin cleavage of vitronectin Identification of the site and consequent attenuation in binding plasminogen activator inhibitor-1. FEBS Letters, 285(2), 251–256. https://doi.org/10.1016/0014-5793(91)80810-P

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free