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Titolo:
Full-length and truncated forms of vitronectin provide insight into effects of proteolytic processing on function
Autore:
Gibson, AD; Peterson, CB;
Indirizzi:
Univ Tennessee, Dept Biochem & Cellular & Mol Biol, Knoxville, TN 37996 USA Univ Tennessee Knoxville TN USA 37996 & Mol Biol, Knoxville, TN 37996 USA
Titolo Testata:
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY
fascicolo: 1-2, volume: 1545, anno: 2001,
pagine: 289 - 304
SICI:
0167-4838(20010209)1545:1-2<289:FATFOV>2.0.ZU;2-Y
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMINOGEN-ACTIVATOR INHIBITOR; S-PROTEIN VITRONECTIN; SOMATOMEDIN-B DOMAIN; EXHIBIT SIMILAR AFFINITY; HUMAN PLASMA VITRONECTIN; HUMAN-ENDOTHELIAL CELLS; HEPARIN-BINDING DOMAIN; MULTIMERIC VITRONECTIN; SELF-ASSOCIATION; LIGAND-BINDING;
Keywords:
vitronectin; heparin; serpin; proteolytic processing;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
65
Recensione:
Indirizzi per estratti:
Indirizzo: Peterson, CB Univ Tennessee, Dept Biochem & Cellular & Mol Biol, M407 Walters Life Sci Bldg, Knoxville, TN 37996 USA Univ Tennessee M407 Walters LifeSci Bldg Knoxville TN USA 37996
Citazione:
A.D. Gibson e C.B. Peterson, "Full-length and truncated forms of vitronectin provide insight into effects of proteolytic processing on function", BBA-PROT ST, 1545(1-2), 2001, pp. 289-304

Abstract

A genetic polymorphism in the vitronectin allele directs the production oftwo 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. Thisreaction 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 the62-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 sites for two vitronectin ligands and further define regions that may be involved in multimerization of the protein. (C) 2001 Elsevier Science B.V. All rights reserved.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/09/20 alle ore 22:54:37