ATP‐dependent regulation of phospholipase C in permeabilized 3T3 cells

FEBS Letters

Higashi, Kyoichiro¹  Ogawara, Hiroshi¹ 

[1]Department of Biochemistry, Meiji College of Pharmacy, Nozawa-1, Setagaya-ku, Tokyo 154, Japan

关键词: ATPγS;    Phospholipase C;    G-protein;    Cell permeabilization;    G-protein;    GTP-binding protein;    AppCH2p;    β3;    γ-methylene adenosine 5'-triphosphate;    AppNHp;    adenyl 5'-yl imidodiphosphate;    ATPγS;    adenosine 5'-O-[3-(thio)triphosphate];    ADPβS;    adenosine 5'-O-[2-(thio)diphosphate];    GppNHp;    guanyl-5'-yl imidodiphosphate;    GTPγS;    guanosine 5'-O-[3-(thio)triphosphate];    IP3;    inositol trisphosphate;    IP2;    inositol bisphosphate;    EGTA;    [ethylenebis(oxyethylene nitrilo)]tetraacetic acid;    PI;    phosphatidyl inositol;    PIP;    phosphatidyl inositol 4-monophosphate;    PIP2;    phosphatidyl inositol 4;    5-bisphosphate;    PBS;    phosphate-buffered saline;   

DOI  :  10.1016/0014-5793(90)80285-Q

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Regulation of phospholipase C (PLC) coupled with a G-protein was studied with Swiss 3T3 cells permeabilized by digitonin. In permeabilized cells, activation ofphospholipase C required millimolar concentrations of ATP in addition to a G-protein activator, AlF₄ ⁻ or nonhydrolysable GTP analogues. To determine the mechanism of the action of ATP, we examined the effects of ATP analogues. ATPγS directly activated phospholipase C in the presence or absence ofAlF₄ ⁻. On the other hand, neither βγ-methylene ATP nor adenyl-5'-yl imidodiphosphate nor ADPβS could support the AlF₄ ⁻-dependent activation of phospholipase C. The action of ATPγS was not through the substrate supply for phospholipase C, because ATPγS did not augment the levels of PIP₂ or PIP in permeabilized cells. These results suggested the significance of the γ-phosphate group of ATP and/or phosphorylation by ATP in the activation of phospholipase C by a putative G-protein.

【 授权许可】

Unknown