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Titolo:
SPERMINE SUPPRESSES THE ACTIVATION OF HUMAN NEUTROPHIL NADPH OXIDASE IN CELL-FREE AND SEMI-RECOMBINANT SYSTEMS
Autore:
OGATA K; NISHIMOTO N; UHLINGER DJ; IGARASHI K; TAKESHITA M; TAMURA M;
Indirizzi:
EHIME UNIV,FAC ENGN,DEPT APPL CHEM MATSUYAMA EHIME 790 JAPAN EHIME UNIV,FAC ENGN,DEPT APPL CHEM MATSUYAMA EHIME 790 JAPAN OITA MED UNIV,DEPT BIOCHEM HASAMA OITA 87955 JAPAN EMORY UNIV,SCH MED,DEPT BIOCHEM ATLANTA GA 30322 CHIBA UNIV,FAC PHARMACEUT SCI YAYOI CHIBA 263 JAPAN
Titolo Testata:
Biochemical journal
, volume: 313, anno: 1996,
parte:, 2
pagine: 549 - 554
SICI:
0264-6021(1996)313:<549:SSTAOH>2.0.ZU;2-1
Fonte:
ISI
Lingua:
ENG
Soggetto:
ELECTROPERMEABILIZED HUMAN NEUTROPHILS; PIG POLYMORPHONUCLEAR LEUKOCYTES; CHARGE-DEPENDENT REGULATION; RESPIRATORY BURST OXIDASE; SUPEROXIDE GENERATION; PLASMA-MEMBRANE; POLYAMINES; PHAGOCYTES; INVOLVEMENT; PROTEINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
36
Recensione:
Indirizzi per estratti:
Citazione:
K. Ogata et al., "SPERMINE SUPPRESSES THE ACTIVATION OF HUMAN NEUTROPHIL NADPH OXIDASE IN CELL-FREE AND SEMI-RECOMBINANT SYSTEMS", Biochemical journal, 313, 1996, pp. 549-554

Abstract

Spermine, a cellular polyamine, down-regulates O-2(-) generation in human neutrophils stimulated by receptor-linked agonist [Ogata, Tamura and Takeshita (1992) Biochem. Biophys. Res. Commun. 182, 20-26]. In this study, to elucidate the mechanism for the inhibition, the effect ofspermine on cell-free activation of the O-2(-) generating enzyme (NADPH oxidase) was examined. Spermine suppressed the SDS-induced activation of NADPH oxidase in a dose-dependent manner with an IC50 of 18 mu M. The inhibition was specific for spermine over its precursor amines, spermidine and putrescine. Spermine did not alter the K-m for NADPH orthe optimal concentration of SDS for activation. The amine was inhibitory only when added before activation, indicating that it affects theactivation process rather than the enzyme's activity. An increased concentration of cytosol partly prevented the inhibition by spermine. Insemi-recombinant cell-free system, spermine inhibited the activation of NADPH oxidase as effectively as in the cell-free system (IC50 = 13 mu M). Pretreatment of each recombinant cytosolic component with spermine revealed that they (especially p67phox) are sensitive to spermine. These results suggest that spermine interacts with cytosolic component(s) and impairs the assembly of NADPH oxidase.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 13:10:29