日本生理学会大会発表要旨集
セッションID: 1P048
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S64 Cellular & molecular physiology
精子運動性の調節機構に関するリン酸化プロテオーム解析
藤ノ木 政勝川村 猛戸田 年総大竹 英樹高城 忠清水 Nobuyoshi奥野 誠山岡 貞夫
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会議録・要旨集 フリー

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In our previous study [M. Fujinoki et al. (2001) Biomed. Res. 22, 45-58], we reported that 66k-Da protein, 58k-Da protein, two types of 36k-Da protein, which were designated as 36K-A protein and 36K-B protein, obtained from hamster sperm flagella were phosphorylated at serine residues associated with motility. In the present experiments, we identified and characterized these four proteins. Two 36k-Da proteins were phosphorylated in a cAMP dependent manner. In order to identify those four phosphoproteins, they were analyzed by peptide mass finger printing and amino acid sequencing. From the results, the 66k-Da protein was identified as beta tubulin. Protein of 58kDa was identified as ATP synthase F1 beta. Both 36k-Da protein were identified as pyruvate dehydrogenase E1 beta lacked N-terminal 30 amino acids. Moreover, we examined localization of 58k-Da protein and two 36k-Da proteins. The 58k-Da protein was assumed to be existed in the equatorial segment of acrosomal region of sperm head and the middle piece and the principal piece of sperm flagellum. The 36K-A protein was localized in the principal piece. On the other hand, the 36K-B protein was localized in the middle piece. [Jpn J Physiol 54 Suppl:S76 (2004)]
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© 2004 日本生理学会
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