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Titolo:
HUMAN MATRIX METALLOPROTEASE ACTIVATION BY INSULTS OF BACTERIAL-INFECTION INVOLVING PROTEASES AND FREE-RADICALS
Autore:
MAEDA H; OKAMOTO T; AKAIKE T;
Indirizzi:
KUMAMOTO UNIV,SCH MED,DEPT MICROBIOL,2-2-1 HONJO KUMAMOTO 860 JAPAN
Titolo Testata:
Biological chemistry
fascicolo: 2, volume: 379, anno: 1998,
pagine: 193 - 200
SICI:
1431-6730(1998)379:2<193:HMMABI>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
PLASMA ALPHA-1-PROTEINASE INHIBITOR; NITRIC-OXIDE; NEUTROPHIL MYELOPEROXIDASE; LEUKOCYTE COLLAGENASE; MICROBIAL PROTEASES; OXYGEN RADICALS; PATHOGENESIS; INACTIVATION; PEROXYNITRITE; PURIFICATION;
Keywords:
ALPHA(1)-PROTEASE INHIBITOR; BACTERIAL PROTEASES; PEROXYNITRITE; COLLAGENASE, PMN; MATRIX METALLOPROTEASES (MMPS); NITRIC OXIDE; REACTIVE OXYGEN SPECIES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
32
Recensione:
Indirizzi per estratti:
Citazione:
H. Maeda et al., "HUMAN MATRIX METALLOPROTEASE ACTIVATION BY INSULTS OF BACTERIAL-INFECTION INVOLVING PROTEASES AND FREE-RADICALS", Biological chemistry, 379(2), 1998, pp. 193-200

Abstract

We found that human matrix metalloproteases (MMPs) may be processed from their proenzyme forms (proMMP) to their active forms by two new and unique mechanisms: Firstly, by bacterial proteases such as Pseudomonas elastase and Vibrio cholerae protease, which cleave off the N-terminal autoinhibitory domain (so-called cysteine switch) from proMMPs, The second mechanism depends on free radical generation by activated polymorphonuclear leukocytes (PMNs). In this case, peroxynitrite (ONOO-) or nitrogen dioxide radical ((NO2)-N-.), the reaction products of either superoxide (O-2(.-)) or molecular oxygen (O-2) and nitric oxide ((NO)-N-.), are the key reactants. Both O-2(.-) and (NO)-N-. are generated by activated macrophages and PMNs as a result of immunologic responses involving various proinflammatory cytokines, (NO2)-N-. or ONOO- seems to interact with a single cysteine residue in the propeptide autoinhibitory domain, or so-called cysteine switch of proMMPs, thus transforming proMMPs into their active conformation. Furthermore, reactive oxygen species are known to inactivate the alpha(1)-protease inhibitor (alpha(1)-PI), a potent neutrophil elastase inhibitor in plasma. In addition, we found that such radicals activate MMPs which degrade and inactivate alpha(1)-PI by proteolysis. Thus, the activation of MMPs, accompanied by the inactivation of alpha(1)-PI, will bring about enhanced proteolytic damage to the matrix tissues of the infected sites by bothMMPs and elastase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 15:45:23