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Titolo:
Inhibitory effect of glycyrrhizin on the phosphorylation and DNA-binding abilities of high mobility group proteins 1 and 2 in vitro
Autore:
Sakamoto, R; Okano, M; Takena, H; Ohtsuki, K;
Indirizzi:
Kitasato Univ, Grad Sch Med Sci, Lab Genet Biochem, Sagamihara, Kanagawa 2288555, Japan Kitasato Univ Sagamihara Kanagawa Japan 2288555 , Kanagawa 2288555, Japan
Titolo Testata:
BIOLOGICAL & PHARMACEUTICAL BULLETIN
fascicolo: 8, volume: 24, anno: 2001,
pagine: 906 - 911
SICI:
0918-6158(200108)24:8<906:IEOGOT>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
CASEIN KINASE-II; IN-VITRO; BIOCHEMICAL-CHARACTERIZATION; AFFINITY; HMG1; CHROMATOGRAPHY; STIMULATION; SEQUENCE; ENHANCE; RELEASE;
Keywords:
casein kinase 1; DNA-binding ability; glycyrrhizin; GL-binding proteins; high mobility group protein; protein kinase;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: Ohtsuki, K Kitasato Univ, Grad Sch Med Sci, Lab Genet Biochem, 1-15-1 Kitasato, Sagamihara, Kanagawa 2288555, Japan Kitasato Univ 1-15-1 Kitasato Sagamihara Kanagawa Japan 2288555
Citazione:
R. Sakamoto et al., "Inhibitory effect of glycyrrhizin on the phosphorylation and DNA-binding abilities of high mobility group proteins 1 and 2 in vitro", BIOL PHAR B, 24(8), 2001, pp. 906-911

Abstract

The physiological correlation between glycyrrhizin (GL) and high mobility group proteins 1 and 2 (HMG1/2) and the inhibitory effect of GL on their phosphorylation by three protein kinases (CK-I, CK-II and PKC) were investigated biochemically in vitro. It was found that GL binds directly to HMG1/2, because (i) HMG1/2 have a high affinity with a GL-affinity column; and (ii)GL induces the conformational changes in HMG1/2. Both purified HMG1/2 functioned as phosphate acceptors for these two protein kinases (CK-1 and PKC),but not phosphorylated by, CK-II. Phosphorylation of HMG1/2 by two proteinkinases (CK-1 and PKC) was completely inhibited by a glycyrrhetinic acid derivative (oGA) at one-tenth the concentration of GL. Also, the DNA-bindingabilities of HMG1/2 were reduced by GL in a dose-dependent manner. These results show that the binding of GL to HMG1/2 results in the inhibition of their physiological activities (DNA-binding ability and phosphorylation by PKC or CK-1) in vitro. The GL-induced inhibition of the physiological activities of HMG1/2 may be involved in the anti-inflammatory effect of GL in vivo.

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Documento generato il 29/11/20 alle ore 18:29:03