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Inhibitory effects of cAMP and protein kinase C on meiotic maturation and MAP kinase phosphorylation in porcine oocytes
Author(s) -
Fan HengYu,
Li ManYu,
Tong Chao,
Chen DaYuan,
Xia GuoLiang,
Song XiangFen,
Schatten Heide,
Sun QingYuan
Publication year - 2002
Publication title -
molecular reproduction and development
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.745
H-Index - 105
eISSN - 1098-2795
pISSN - 1040-452X
DOI - 10.1002/mrd.10194
Subject(s) - protein kinase c , staurosporine , biology , activator (genetics) , forskolin , calphostin c , protein kinase a , phosphorylation , okadaic acid , microbiology and biotechnology , mitogen activated protein kinase kinase , map kinase kinase kinase , phosphatase , meiosis ii , kinase , ask1 , oocyte , biochemistry , endocrinology , stimulation , embryo , gene
The regulation of MAP kinase phosphorylation by cAMP and protein kinase C (PKC) modulators during pig oocyte maturation was studied by Western immunoblotting. We showed that both forskolin and IBMX inhibited MAP kinase phosphorylation and meiosis resumption in a dose‐dependent manner, and this inhibitory effect was overcome by the protein phosphatase inhibitor, okadaic acid. Pharmacological PKC activator phorbol myristate acetate or physiological PKC activator diC8 also delayed MAP kinase phosphorylation and meiosis resumption, and their effect was abrogated by PKC inhibitors, staurosporine, and calphostin C. The results suggest that meiotic resumption is inhibited by elevation of cAMP or delayed by activation of PKC probably via down‐regulation of MAP kinase activation, which is mediated by protein phosphatase, during pig oocyte maturation. Mol. Reprod. Dev. 63: 480–487, 2002. © 2002 Wiley‐Liss, Inc.