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Title 

Protein modification by phosphorylation during the process of nuclear membrane dissolution in puromycin-treated mouse oocytes

Authors 

Hae Mook KangChung Hee ChoKyung Kwang LeeHyuk Bang KwonKyung Jin KimWan Kyoo Cho

Publisher 

Society for the Study of Reproduction

Issue Date 

1991

Citation 

Biology of Reproduction, vol. 44, no. 0, pp. 590-598

Keywords 

puromycincell nucleus membranemouseoocytephosphorylationprotein synthesis inhibitionMiceMice, Inbred ICRNuclear EnvelopeOocytes

Abstract 

The present study was undertaken to elucidate the mechanism of nuclear membrane dissolution (NMD) in puromycin-treated mouse oocytes. Treatment of germinal vesicle breakdown (GVBD) oocytes with puromycin (50 μg/ml) induced chromosome decondensation with formation of a polar body; these are designated nuclear membrane (NM) oocytes. After withdrawal of puromycin, NM oocytes underwent NMD (approximately 70%) during a 12-h culture period. Either dibutyryl cyclic AMP (dbcAMP, 25-100 μg/ml) or isobutylmethylxanthine (IBMX, 0.1-1.0 mM) inhibited the process of NMD in a dose-dependent manner, suggesting the involvement of cAMP in the process of NMD. To determine which protein(s) participated in the transition from interphase to metaphase II during NMD, NM oocytes were labeled with [35S]methionine, and one- and two-dimensional gel electrophoresis were performed. Although the synthesis of stage-specific proteins during NMD was not found, two specific proteins of M(r) 27 000 and 46 000, which were synthesized at interphase following removal of puromycin, were modified during NMD. Phosphatase treatment and 32PO4-labeling experiments indicated that phosphorylation was responsible for these modifications, which were inhibited by either dbcAMP or IBMX. Therefore, it appears that phosphorylation of specific proteins may play an important role in the transition from interphase to metaphase II.

ISSN 

0006-3363

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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