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

被引：15

作者：

Meacci, E ^{[1
]}

Donati, C ^{[1
]}

Cencetti, F ^{[1
]}

Romiti, E ^{[1
]}

Farnararo, M ^{[1
]}

Bruni, P ^{[1
]}

机构：

[1] Univ Florence, Dipartimento Sci Biochim, I-50134 Florence, Italy

来源：

FEBS LETTERS | 2000年 / 473卷 / 01期

关键词：

phospholipase D; bradykinin; caveolin-3; RhoA; C2C12; myotube;

D O I：

10.1016/S0014-5793(00)01486-1

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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 C2Cl2 myotubes contain phospholipase D1 (PLD1) and its major regulators, RhoA and protein kinase C alpha (PKC alpha). 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 PKC alpha. (C) 2000 Federation of European Biochemical Societies.

引用

页码：10 / 14

页数：5

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