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001-es BibID:BIBFORM028871
Első szerző:Nishiyama, Uichi
Cím:Structure-activity relationship within a series of degradation products of tautomycin / Uichi Nishiyama, Makoto Ubukata, Junji Magae, Takao Kataoka, Ferenc Erdődi, David J. Hartshorne, Kiyoshi Isono, Kazuo Nagai, Hiroyuki Osada
Dátum:1996
ISSN:0916-8451
Megjegyzések: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 the activity 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.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
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Megjelenés:Bioscience Biotechnology And Biochemistry. - 60 : 1 (1996), p. 103-107. -
További szerzők:Ubukata, Makoto Magae, Junji Kataoka, Takao Hartshorne, David J. Isono, Kiyoshi Nagai, Kazuo Osada, Hiroyuki Erdődi Ferenc (1953-) (biokémikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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