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Titolo:
STRUCTURE AND FUNCTION OF PLASMINOGEN-ACTIVATOR INHIBITOR-2 - AN INTRACELLULAR SERINE PROTEINASE-INHIBITOR MODULATING APOPTOSIS (REVIEW)
Autore:
JENSEN PH;
Indirizzi:
AARHUS UNIV,DEPT MED BIOCHEM DK-8000 AARHUS C DENMARK
Titolo Testata:
International journal of oncology
fascicolo: 3, volume: 11, anno: 1997,
pagine: 557 - 570
SICI:
1019-6439(1997)11:3<557:SAFOPI>2.0.ZU;2-D
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL CARCINOMA ANTIGEN; INTERLEUKIN-1-BETA CONVERTING-ENZYME; EPITHELIUM-DERIVED FACTOR; RECEPTOR-RELATED PROTEIN; CATALYZED CROSS-LINKING; ICE-LIKE PROTEASES; MOLECULAR CHARACTERIZATION; UROKINASE RECEPTOR; HUMAN-PLACENTA; CHROMOSOMAL LOCALIZATION;
Keywords:
PLASMINOGEN ACTIVATOR INHIBITOR-2; SERINE PROTEINASE INHIBITOR; APOPTOSIS;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
163
Recensione:
Indirizzi per estratti:
Citazione:
P.H. Jensen, "STRUCTURE AND FUNCTION OF PLASMINOGEN-ACTIVATOR INHIBITOR-2 - AN INTRACELLULAR SERINE PROTEINASE-INHIBITOR MODULATING APOPTOSIS (REVIEW)", International journal of oncology, 11(3), 1997, pp. 557-570

Abstract

Serine proteinase inhibitors (serpins) are well known regulators of extracellular proteolytic pathways. A recently identified group of intracellular serpins of mammalian and viral origin, designated ovalbumine-like serpins, modify intracellular proteolytic pathways involved in the regulation of apoptosis and inflammation. This review focuses on plasminogen activator inhibitor-2 (PAI-2) in terms of the molecular structure-function relationships and its intracellular functions, in particular in relation to apoptosis. PAI-2 inhibits apoptosis in cell lineschallenged with tumor necrosis factor or certain viruses. The intracellular proteinases which PAI-2 act upon are still unknown. During myeloid apoptosis, PAI-2 proteolytically modified to a smaller but still proteinase inhibitory form. PAI-2 is unique among the serpins with respect to its large CD-domain localized between alpha-helices C and D. Recent data show that two domains in PAI-2 are required for its antiapoptotic activity, the CD-domain and the proteinase reactive site. We have shown the CD-domain is involved in covalent and reversible interactions with cytosolic proteins, e.g. the annexins. These intracellular PAI-2-reactive proteins might represent participants in signalling pathways involved in the regulation of cell survival.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 13:27:19