A-Kinase Anchor Protein 1 (AKAP1) Regulates cAMP-Dependent Protein Kinase (PKA) Localization and Is Involved in Meiotic Maturation of Porcine Oocytes

被引:12
作者
Nishimura, Takanori [1 ]
Sugiura, Koji [1 ]
Naito, Kunihiko [1 ]
机构
[1] Univ Tokyo, Lab Appl Genet, Grad Sch Agr & Life Sci, Tokyo 1138657, Japan
基金
日本学术振兴会;
关键词
cyclic adenosine monophosphate (cAMP); gamete biology; kinases; oocyte maturation; porcine/pig; HIGH-AFFINITY BINDING; MOLECULAR CHARACTERIZATION; SUBUNIT RII; ASSOCIATION; ACTIVATION; MECHANISM; MEIOSIS; EZRIN;
D O I
10.1095/biolreprod.112.106351
中图分类号
Q [生物科学];
学科分类号
07 ; 0710 ; 09 ;
摘要
In mammalian oocytes, cAMP-dependent protein kinase (PKA) has critical functions in meiotic arrest and meiotic maturation. Although subcellular localization of PKA is regulated by A-kinase anchor proteins (AKAPs) and PKA compartmentalization is essential for PKA functions, the role of AKAPs in meiotic regulation has not been fully elucidated. In the present study, we performed far-Western blot analysis using porcine PRKAR2A for detection of AKAPs and found, to our knowledge, several novel signals in porcine oocytes. Among these signals, a 150-kDa AKAP showed the major expression and was the product of porcine AKAP1. Overexpression of AKAP1 changed the PKA localization and promoted meiotic resumption of porcine oocytes even in the presence of a high concentration of cAMP, which inhibits meiotic resumption by inducing high PKA activity. On the contrary, knockdown of AKAP1 showed inhibitory effects on meiotic resumption and oocyte maturation. In addition, the expression level of AKAP1 in porcine growing oocytes, which show meiotic incompetence and PKA mislocalization, was significantly lower than that in fully grown oocytes. However, AKAP1 insufficiency was not the primary cause of the meiotic incompetence of the growing oocytes. These results suggest that the regulation of PKA localization by AKAP1 may be involved in meiotic resumption and oocyte maturation but not in meiotic incompetence of porcine growing oocytes.
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页数:9
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