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Titolo:
SYNERGISTIC ACTIVATION OF RAT-BRAIN PHOSPHOLIPASE-D BY ADP-RIBOSYLATION FACTOR AND RHOA P21, AND ITS INHIBITION BY CLOSTRIDIUM-BOTULINUM C3EXOENZYME
Autore:
KURIBARA H; TAGO K; YOKOZEKI T; SASAKI T; TAKAI Y; MORII N; NARUMIYA S; KATADA T; KANAHO Y;
Indirizzi:
TOKYO INST TECHNOL,DEPT LIFE SCI YOKOHAMA KANAGAWA 226 JAPAN TOKYO INST TECHNOL,DEPT LIFE SCI YOKOHAMA KANAGAWA 226 JAPAN OSAKA UNIV,SCH MED,DEPT MOLEC BIOL & BIOCHEM SUITA OSAKA 565 JAPAN KYOTO UNIV,FAC MED,DEPT PHARMACOL,SAKYO KU KYOTO 606 JAPAN UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL SCI TOKYO 113 JAPAN
Titolo Testata:
The Journal of biological chemistry
fascicolo: 43, volume: 270, anno: 1995,
pagine: 25667 - 25671
SICI:
0021-9258(1995)270:43<25667:SAORPB>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
REGULATORY PROTEIN; GTP; CELLS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
23
Recensione:
Indirizzi per estratti:
Citazione:
H. Kuribara et al., "SYNERGISTIC ACTIVATION OF RAT-BRAIN PHOSPHOLIPASE-D BY ADP-RIBOSYLATION FACTOR AND RHOA P21, AND ITS INHIBITION BY CLOSTRIDIUM-BOTULINUM C3EXOENZYME", The Journal of biological chemistry, 270(43), 1995, pp. 25667-25671

Abstract

An activator of rat brain phospholipase D (PLD) that is distinct fromthe already identified PLD activator, ADP-ribosylation factor (ARF), was partially purified from bovine brain cytosol by a series of chromatographic steps. The partially purified preparation contained a 22-kDasubstrate for Clostridium botulinum C3 exoenzyme ADP-ribosyltransferase, which strongly reacted with anti-rhoA p21 antibody, but not with anti-rac1 p21 or anti-cdc42Hs p21 antibody. Treatment of the partially purified PLD-activating factor with both C3 exoenzyme and NAD significantly inhibited the PLD-stimulating activity. These results suggest that rhoA p21 is, at least in part, responsible for the PLD-stimulating activity in the preparation. Recombinant isoprenylated rhoA p21 expressed in and purified from Sf9 cells activated rat brain PLD in a concentration- and GTP gamma S (guanosine 5'-O-(3-thiotriphosphate))-dependent manner. In contrast, recombinant non-isoprenylated rhoA pal (fused to glutathione S-transferase) expressed in Escherichia coil failed to activate the PLD. This difference cannot be explained by a lower affinity of non-isoprenylated rhoA p21 for GTP gamma S, as the rates of [S-35]GTP gamma S binding were very similar for both recombinant preparations and the GTP gamma S-bound form of non-isoprenylated rhoA p21 did not induce PLD activation. Interestingly, recombinant isoprenylated rhoA p21 and ARF synergistically activated rat brain PLD; a similar pattern was seen with the partially purified PLD-activating factor. The synergistic activation was inhibited by C3 exoenzyme-catalyzed ADP-ribosylation of recombinant isoprenylated rhoA p21 in a NAD-dependent manner. Inhibition correlated with the extent of ADP-ribosylation. These findings suggest that rhoA pal regulates rat brain PLD in concert with ARF, and that isoprenylation of rhoA p21 is essential for PLD regulation in vitro.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 00:35:12