Inhibition of glycosphingolipid synthesis induces p34cdc2 activation in Xenopus oocyte

FEBS Letters

Jessus, Catherine¹  De Smedt, Véronique²  Ozon, René¹  Rime, Hélène¹ 

[1] Laboratoire de Physiologie de la Reproduction, URA-CNRS 1449/INRA, Université Pierre et Marie Curie, Boîte 13, 4 place Jussieu, 75252 Paris Cedex 05, France;Unité de Biologie de la Fécondation, Station de Physiologie Animale, INRA, 78352 Jouy-en-Josas, France

关键词: p34cdc2 kinase;    Xenopos oocyte;    Ceramide;    Glucosylceramide synthase;    Sphingomyelin;    ER;    endoplasmic reticulum;    GVBD;    germinal vesicle breakdown;    IBMX;    3-isobutyl-1-methylxantine;    MAP kinase;    mitogen-activated protein kinase;    MPF;    M-phase promoting factor;    PDMP;    dl-threo-1-phenyl-2-decanoylamino-3-morpholino-1-propanol;    SMase;    sphingomyelinase;   

DOI  :  10.1016/0014-5793(95)01183-F

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In Xenopus prophase-blocked oocytes, it is assumed that progesterone interacts with the plasma membrane to initiate a signalling cascade that ultimately leads to MPF activation. Progesterone regulates negatively the cAMP pathway through an inhibition of adenylate cyclase. However, the mechanisms linking the initial action of the hormone with adenylate cyclase activity remain to be elucidated. Here, we demonstrate that PDMP, an inhibitor of glucosphingolipid synthesis, triggers oocyte meiotic maturation in a cAMP- and cycloheximide-dependent manner, whereas exogenous ceramide is unefficient. We propose that sphingolipid metabolism and targeting represent an important regulatory process of oocyte meiosis.

【 授权许可】

Unknown