Disappearance of a Novel Protein Component of the 26S Proteasome duringXenopusOocyte Maturation |
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| Authors: | Toshinobu Tokumoto Mika Tokumoto Keiji Seto Ryo Horiguchi Yoshitaka Nagahama Shinpei Yamada Katsutoshi Ishikawa Manfred J Lohka |
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| Institution: | a Department of Biology and Geosciences, Faculty of Science, Shizuoka University, Shizuoka, 422-8529, Japan;b Laboratory of Reproductive Biology, National Institute for Basic Biology, Okazaki, 444-8585, Japan;c Department of Molecular Biomechanics, The Graduate University for Advanced Studies, Okazaki, 444-8585, Japan;d Department of Biological Sciences, Faculty of Science, University of Calgary, Calgary, Canada, T2N 1N4 |
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| Abstract: | We have prepared polyclonal antibodies againstXenopus20S proteasomes. The antibodies cross-react with several proteins that are common to 20S and 26S proteasomes and with at least two proteins that are unique to 26S proteasomes. The antibodies were used to analyze changes in the components of proteasomes during oocyte maturation and early development ofXenopus laevis.A novel protein with a molecular weight of 48 kDa, p48, was clearly detected in immature oocytes, but was found at very low levels in mature oocytes and ovulated eggs. p48 was reduced to low levels during oocyte maturation, after maturation-promoting factor was activated. The amount of p48 in eggs remained low during early embryonic development, but increased again after the midblastula transition. These results show that at least one component of 26S proteasomes changes during oocyte maturation and early development and suggest that alterations in proteasome function may be important for the regulation of developmental events, such as the rapid cell cycles, of the early embryo. |
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| Keywords: | proteasomes oocyte maturation fertilization early development cell cycle |
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