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Titolo:
Involvement of cytosolic prolyl endopeptidase in degradation of p40-phox splice variant protein in myeloid cells
Autore:
Hasebe, T; Hua, J; Someya, A; Morain, P; Checler, F; Nagaoka, I;
Indirizzi:
Juntendo Univ, Sch Med, Dept Biochem, Bunkyo Ku, Tokyo 1138421, Japan Juntendo Univ Tokyo Japan 1138421 ochem, Bunkyo Ku, Tokyo 1138421, Japan Inst Rech Servier, Div Med Chem D, F-92150 Suresnes, France Inst Rech Servier Suresnes France F-92150 em D, F-92150 Suresnes, France CNRS, Inst Pharmacol Mol & Cellulaire, UPR411, F-06560 Valbonne, France CNRS Valbonne France F-06560 ellulaire, UPR411, F-06560 Valbonne, France
Titolo Testata:
JOURNAL OF LEUKOCYTE BIOLOGY
fascicolo: 6, volume: 69, anno: 2001,
pagine: 963 - 968
SICI:
0741-5400(200106)69:6<963:IOCPEI>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHAGOCYTE NADPH OXIDASE; MESSENGER-RNA; ACTIVATION; P40(PHOX); COMPONENT; EXPRESSION; MATURATION; SEQUENCES; COMPLEX; PHOSPHORYLATION;
Keywords:
NADPH oxidase; alternative splicing; proteolysis; HL-60;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
42
Recensione:
Indirizzi per estratti:
Indirizzo: Nagaoka, I Juntendo Univ, Sch Med, Dept Biochem, Bunkyo Ku, 2-1-1 Hongo, Tokyo 1138421, Japan Juntendo Univ 2-1-1 Hongo Tokyo Japan 1138421 o 1138421, Japan
Citazione:
T. Hasebe et al., "Involvement of cytosolic prolyl endopeptidase in degradation of p40-phox splice variant protein in myeloid cells", J LEUK BIOL, 69(6), 2001, pp. 963-968

Abstract

Our previous studies indicated that an alternatively spliced variant mRNA of p40-phox, a cytosolic component of NADPH oxidase, is expressed but its protein is hardly detected in myeloid cells such as promyelocytic HL-60 cells and neutrophils, Here, we have examined die stability of p40-phox variantprotein in undifferentiated HL-60 cells. When in vitro-translated proteinswere incubated with subcellular fractions of HL-60 cells, p40-phox variantprotein but not native p40-phox was degraded by the cytosol and granule fractions. The degradation of variant protein by the granule fraction was observed using sonicated but not intact granules, suggesting that the variant protein is unlikely to be degraded by the granules in intact cells, To identify the enzyme(s) involved, we examined the effects of various enzyme inhibitors oil the degradation of variant protein by the cytosol fraction, Degradation was completely inhibited by proline-specific serine protease (prolyl endopeptidase) inhibitors but not by proteasome, calpain, and metallprotease inhibitors. Furthermore, the variant protein was degraded by a purifiedprolyl endopeptidase, and the degradation was protected by treating HL-60 cells with a cell-permeable inhibitor (S17092-1) for prolyl endopeptidase. These observations suggest that a cytosolic prolyl endopeptidase is involved in the degradation of p40-phox variant protein in myeloid cells.

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Documento generato il 23/11/20 alle ore 21:31:24