PMID: 11342054May 9, 2001Paper

Full-length and truncated forms of vitronectin provide insight into effects of proteolytic processing on function

Biochimica Et Biophysica Acta
A Gibson, C B Peterson

Abstract

A genetic polymorphism in the vitronectin allele directs the production of two distinct forms of the 459 amino acid glycoprotein. A methionine present at position 381 favors production of the single-chain form of vitronectin, while threonine at this position increases the susceptibility of vitronectin to cleavage just beyond its heparin-binding domain at residue 379. This reaction gives rise to a disulfide-bonded, two-chain form of vitronectin. In order to investigate the functional significance of the vitronectin polymorphism, the baculovirus system has been used to express recombinant full-length vitronectin and a truncated form of the molecule that represents the 62-kDa fragment of two-chain vitronectin. Both forms of vitronectin bind and neutralize heparin anticoagulant activity. The proteins also bind PAI-1 and stabilize its active conformation. These experiments suggest that the C-terminal 80 amino acids do not confer a functional difference in the two allelic variants. Immunoassays and gel filtration experiments indicate that both full-length and truncated recombinant forms of vitronectin are multimeric. Together with other reports from this laboratory, these results provide information regarding the primary binding site...Continue Reading

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Citations

Dec 2, 2020·Investigative Ophthalmology & Visual Science·Fabiola BiasellaUlrike Friedrich
Dec 7, 2007·Comparative Biochemistry and Physiology. Part B, Biochemistry & Molecular Biology·Manish Mahawar, Paritosh Joshi

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