Receptor‐activated phospholipase D is present in caveolin‐3‐enriched light membranes of C2C12 myotubes

FEBS Letters

Meacci, Elisabetta¹  Cencetti, Francesca¹  Farnararo, Marta¹  Bruni, Paola¹  Romiti, Elena¹  Donati, Chiara¹ 

[1] Dipartimento di Scienze Biochimiche, Università di Firenze, Viale G.B. Morgagni 50, 50134 Firenze, Italy

关键词: Phospholipase D;    Bradykinin;    Caveolin-3;    RhoA;    C2C12 myotube;    PLD;    phospholipase D;    cav;    caveolin;    cav-3;    caveolin-3;    CELM;    cav-3-enriched light membrane;    BK;    bradykinin;    PMA;    phorbol 12-myristate 13-acetate;    PtdCho;    phosphatidylcholine;    PtdOH;    phosphatidic acid;    PtdEtOH;    phosphatidylethanol;    PtdPro phosphatidylpropanol;    SPP;    sphingosine 1-phosphate;    MBS;    MES buffered saline;    PKC;    protein kinase C;   

DOI  :  10.1016/S0014-5793(00)01486-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Caveolin-3 (cav-3) is a key structural component of caveolar membrane in skeletal muscle. Cav-3-enriched light membrane (CELM) fractions obtained from C2C12 myotubes contain phospholipase D1 (PLD1) and its major regulators, RhoA and protein kinase Cα (PKCα). All these proteins were found bound to cav-3. An in vivo assay of PLD activity, which allows to localize the reaction product in CELMs, indicated that the enzyme associated to this membrane microdomain was active. Moreover, bradykinin (BK), thrombin and phorbol 12-myristate 13-acetate induced rapid stimulation of PLD activity in CELMs. The cav-3-PLD1 complex was not affected by BK treatment, whereas the agonist induced a marked increase of RhoA association with cav-3. Furthermore, BK-induced PLD activation in CELMs was dependent, at least in part, on PKCα.

【 授权许可】

Unknown