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Inhibition of glycosphingolipid synthesis induces p34 cdc2 activation in Xenopus oocyte
Author(s) -
De Smedt Véronique,
Rime Hélène,
Jessus Catherine,
Ozon René
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)01183-f
Subject(s) - oocyte , xenopus , cyclase , adenylate kinase , cycloheximide , microbiology and biotechnology , prophase , chemistry , puromycin , meiosis , biology , protein biosynthesis , biochemistry , receptor , embryo , gene
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.

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