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Titolo:
AUGMENTATION BY CALMODULIN OF ADP-RIBOSYLATION FACTOR-STIMULATED PHOSPHOLIPASE-D ACTIVITY IN PERMEABILIZED RABBIT PERITONEAL NEUTROPHILS
Autore:
TAKAHASHI K; TAGO K; OKANO H; OHYA Y; 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 UNIV TOKYO,GRAD SCH SCI,DEPT PLANT SCI TOKYO 113 JAPAN UNIV TOKYO,FAC PHARMACEUT SCI,DEPT PHYSIOL CHEM TOKYO 113 JAPAN
Titolo Testata:
The Journal of immunology
fascicolo: 3, volume: 156, anno: 1996,
pagine: 1229 - 1234
SICI:
0022-1767(1996)156:3<1229:ABCOAF>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
PROTEIN-KINASE-C; GTP-BINDING PROTEIN; D ACTIVATION; HL-60 GRANULOCYTES; YEAST CALMODULIN; STREPTOLYSIN-O; CHAIN KINASE; RAT-BRAIN; PURIFICATION; CALCIUM;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
40
Recensione:
Indirizzi per estratti:
Citazione:
K. Takahashi et al., "AUGMENTATION BY CALMODULIN OF ADP-RIBOSYLATION FACTOR-STIMULATED PHOSPHOLIPASE-D ACTIVITY IN PERMEABILIZED RABBIT PERITONEAL NEUTROPHILS", The Journal of immunology, 156(3), 1996, pp. 1229-1234

Abstract

Activation of the membrane-bound phospholipase D (PLD) requires cytosolic factor(s), and ADP-ribosylation factor (ARF) has been identified as a cytosolic PLD activator. In the present study, we demonstrate that calmodulin (CaM) and ARF are both involved in PLD activation in rabbit peritoneal neutrophils. The PLD activity of streptolysin O-permeabilized, cytosol-depleted rabbit neutrophils was significantly enhanced when the permeabilized cells were reconstituted with bovine brain cytosol in the presence of guanosine 5'-O-(3-thiotriphosphate) (GTP gamma S), whereas there was little activation of the enzyme in the absence of cytosol. The GTP gamma S-stimulated PLD activity in the presence of cytosol was augmented on increasing the concentration of free Ca2+. The PLD activity stimulated by GTP gamma S and Ca2+ in this system was inhibited by the calmodulin inhibitor W-7. These findings suggest that CaM plays a role as a cytosolic PLD activator. Moreover, highly purified CaM alone, as well as partially purified ARF alone, promoted a slight stimulation of the PLD activity in permeabilized neutrophils. Interestingly, ARF-stimulated PLD activity was augmented by CaM in the presence of GTP gamma S and Ca2+. This augmentation was again inhibited byW-7, as well as by the structurally unrelated CaM inhibitor trifluoperazine. These data imply that CaM stimulates the PLD activity of rabbit neutrophils in concert with ARF.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 12:37:22