Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
MATRILYSIN IS MUCH MORE EFFICIENT THAN OTHER MATRIX METALLOPROTEINASES IN THE PROTEOLYTIC INACTIVATION OF ALPHA(1)-ANTITRYPSIN
Autore:
SIRES UI; MURPHY G; BARAGI VM; FLISZAR CJ; WELGUS HG; SENIOR RM;
Indirizzi:
WASHINGTON UNIV,JEWISH HOSP ST LOUIS,SCH MED,DEPT MED,DIV DERMATOL,216 S KINGSHIGHWAY ST LOUIS MO 63110 WASHINGTON UNIV,JEWISH HOSP ST LOUIS,SCH MED,DEPT MED,DIV RESP & CRITCARE ST LOUIS MO 63110 WASHINGTON UNIV,ST LOUIS CHILDRENS HOSP,SCH MED,DEPT PEDIAT ST LOUIS MO 63110 WARNER LAMBERT PARKE DAVIS,PARKE DAVIS PHARMACEUT RES DIV,DEPT IMMUNOPATHOL ANN ARBOR MI 00000 STRANGEWAYS RES LAB CAMBRIDGE ENGLAND
Titolo Testata:
Biochemical and biophysical research communications
fascicolo: 2, volume: 204, anno: 1994,
pagine: 613 - 620
SICI:
0006-291X(1994)204:2<613:MIMMET>2.0.ZU;2-B
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA ALPHA-1-PROTEINASE INHIBITOR; ALPHA-1 PROTEINASE-INHIBITOR; HUMAN MONONUCLEAR PHAGOCYTES; SKIN FIBROBLAST COLLAGENASE; HUMAN STROMELYSIN; HUMAN-MONOCYTES; IV COLLAGENASE; EXPRESSION; PURIFICATION; MACROPHAGES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
U.I. Sires et al., "MATRILYSIN IS MUCH MORE EFFICIENT THAN OTHER MATRIX METALLOPROTEINASES IN THE PROTEOLYTIC INACTIVATION OF ALPHA(1)-ANTITRYPSIN", Biochemical and biophysical research communications, 204(2), 1994, pp. 613-620

Abstract

alpha(1)-antitrypsin, the primary physiologic inhibitor of human leukocyte elastase, is proteolytically inactivated by several matrix metalloproteinases including interstitial collagenase, stromelysin and 92 kDa gelatinase. In this report, we describe the catalytic effects of matrilysin, a recently identified metalloproteinase, upon alpha(1)-antitrypsin. Matrilysin was found to be approximately 30-fold more effective than 92 kDa gelatinase, 70-fold more effective than collagenase, and180-fold more effective than stromelysin. Cleavage of alpha(1)-antitrypsin by matrilysin produced two fragments of approximately 50 kDa and4 kDa. The single cleavage occurred at the Phe(352).Leu(353) peptide bond, a locus within alpha(1)-antitrypsin's active-site loop. These results suggest that apart from its activity against extracellular matrix, matrilysin provides a mechanism for the regulation of leukocyte elastase activity through its capacity to degrade alpha(1)-AT. (C) 1994 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/12/20 alle ore 08:13:45