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Titolo:
STRUCTURE-ACTIVITY RELATIONSHIP WITHIN A SERIES OF DEGRADATION PRODUCTS OF TAUTOMYCIN
Autore:
NISHIYAMA U; UBUKATA M; MAGAE J; KATAOKA T; ERDODI F; HARTSHORNE DJ; ISONO K; NAGAI K; OSADA H;
Indirizzi:
TOYAMA PREFECTURAL UNIV,BIOTECHNOL RES CTR,5180 KOSUGI MACHI TOYAMA 93903 JAPAN TOYAMA PREFECTURAL UNIV,BIOTECHNOL RES CTR TOYAMA 93903 JAPAN TOKYO INST TECHNOL,DEPT BIOENGN,MIDORI KU YOKOHAMA KANAGAWA 226 JAPAN TOKAI UNIV,DEPT MARINE SCI & TECHNOL SHIMIZU SHIZUOKA 424 JAPAN INST PHYS & CHEM RES WAKO SAITAMA 35101 JAPAN DEBRECEN UNIV MED,DEPT MED CHEM H-4032 DEBRECEN HUNGARY UNIV ARIZONA,DEPT ANIM SCI TUCSON AZ 85721
Titolo Testata:
Bioscience, biotechnology, and biochemistry
fascicolo: 1, volume: 60, anno: 1996,
pagine: 103 - 107
SICI:
0916-8451(1996)60:1<103:SRWASO>2.0.ZU;2-X
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN PHOSPHATASE INHIBITOR; HUMAN MYELOID-LEUKEMIA; OKADAIC ACID; KINASE-C;
Keywords:
TAUTOMYCIN; STRUCTURE-ACTIVITY RELATIONSHIP; BLEB FORMATION; PROTEIN PHOSPHATASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
14
Recensione:
Indirizzi per estratti:
Citazione:
U. Nishiyama et al., "STRUCTURE-ACTIVITY RELATIONSHIP WITHIN A SERIES OF DEGRADATION PRODUCTS OF TAUTOMYCIN", Bioscience, biotechnology, and biochemistry, 60(1), 1996, pp. 103-107

Abstract

Tautomycin, a protein serine/threonine phosphatase inhibitor, was chemically degraded, and five derivatives were investigated for their biological activities. None of them exerted any inhibitory effects on theactivity of protein phosphatase types 1 and 2A. However, one derivative, named TM2a, induced a significant morphological change (bleb-formation) of human myeloid leukemia K562 cells, TM2b, the trimethyl ester of TM2, did not induce bleb-formation. Thus, the maleic anhydride structure played an important role in the biological activity. The biological properties of TM2a toward K562 cells resembled those of a phorbol ester, rather than of tautomycin. The phorbol ester-induced bleb formation was abrogated by a non-specific inhibitor of protein kinases, staurosporine, and by an inhibitor of protein kinase C (PKC), H-7, but TM2a-induced bleb formation was abrogated only by staurosporine. Enhanced phosphorylation of the two proteins was observed after their exposure to TM2a. This suggest that the effect was not due to any inhibition of protein phosphatase 1 or 2A, but rather to the activation of an unidentified kinase, possibly of the PKC family, or to inhibition of a protein phosphatase other than type 1 or 2A.

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Documento generato il 10/07/20 alle ore 02:24:33