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Titolo:
Tautomycetin is a novel and specific inhibitor of serine/threonine proteinphosphatase type 1, PP1
Autore:
Mitsuhashi, S; Matsuura, N; Ubukata, M; Oikawa, H; Shima, H; Kikuchi, K;
Indirizzi:
Hokkaido Univ, Inst Med Genet, Div Biochem Oncol & immunol, Kita Ku, Sapporo, Hokkaido 0600815, Japan Hokkaido Univ Sapporo Hokkaido Japan 0600815 oro, Hokkaido 0600815, Japan Toyama Prefectural Univ, Biotechnol Res Ctr, Lab Biofunct Chem, Toyama 9390398, Japan Toyama Prefectural Univ Toyama Japan 9390398 Chem, Toyama 9390398, Japan Hokkaido Univ, Fac Agr, Dept Biosci & Chem, Kita Ku, Sapporo, Hokkaido 0608589, Japan Hokkaido Univ Sapporo Hokkaido Japan 0608589 oro, Hokkaido 0608589, Japan
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 2, volume: 287, anno: 2001,
pagine: 328 - 331
SICI:
0006-291X(20010921)287:2<328:TIANAS>2.0.ZU;2-8
Fonte:
ISI
Lingua:
ENG
Soggetto:
CATALYTIC SUBUNIT; OKADAIC ACID; RETINOBLASTOMA PROTEIN; SERINE THREONINE; CALYCULIN-A; IDENTIFICATION; APOPTOSIS; BINDING; MEMBERS; POTENT;
Keywords:
tautomycetin; tautomycin; PP1; PP2A; inhibitor; activity; antibiotic; spiroketal;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Kikuchi, K Hokkaido Univ, Inst Med Genet, Div Biochem Oncol & immunol, Kita Ku, Kita-15,Nishi 7, Sapporo, Hokkaido 0600815, Japan Hokkaido Univ Kita-15,Nishi 7 Sapporo Hokkaido Japan 0600815 an
Citazione:
S. Mitsuhashi et al., "Tautomycetin is a novel and specific inhibitor of serine/threonine proteinphosphatase type 1, PP1", BIOC BIOP R, 287(2), 2001, pp. 328-331

Abstract

Here we isolated tautomycetin, TC, and examined its phosphatase inhibitoryactivity. Recently we have reported that the left-hand moiety of tautomycin, TM, and the right one containing the spiroketal are essentially requiredfor inhibition of protein phosphatase, PP, and induction of apoptosis, respectively. TC is structurally almost identical to TM except that TC is lacking the spiroketal, which has the potential apoptosis-inducing activity. TCspecifically inhibited PP1 activity, IC50 values for purified PP1 and PP2Aenzymes being 1.6 and 62 nM, respectively, whereas the IC50 values of TM were 0.21 and 0.94 nM, respectively. These results demonstrate that TC is the most specific PPI inhibitor out of over 40 species of natural phosphataseinhibitors reported, strongly suggesting that TC is a novel powerful tool to elucidate the physiological roles of PP1 in various biological events. (C) 2001 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 01:42:01