Identification of 36 kDa phosphoprotein in fibrous sheath of hamster spermatozoa

被引:13
作者
Fujinoki, M
Kawamura, T
Toda, T
Ohtake, H
Ishimoda-Takagi, T
Shimizu, N
Yamaoka, S
Okuno, M
机构
[1] Dokkyo Univ, Sch Med, Dept Physiol, Mibu, Tochigi 3210293, Japan
[2] Keio Univ, Sch Med, Dept Biol Mol, Shinjuku Ku, Tokyo 1608582, Japan
[3] Tokyo Metropolitan Inst Gerontol, TMIG Proteom Collaborat Ctr, Itabashi Ku, Tokyo 1730015, Japan
[4] Tokyo Gakugei Univ, Dept Biol, Koganei, Tokyo 1858501, Japan
[5] Univ Tokyo, Grad Sch Arts & Sci, Dept Life Sci, Meguro Ku, Tokyo 1530041, Japan
来源
COMPARATIVE BIOCHEMISTRY AND PHYSIOLOGY B-BIOCHEMISTRY & MOLECULAR BIOLOGY | 2004年 / 137卷 / 04期
关键词
fibrous sheath; flagellum; hamster; LC-MS/MS; peptide mass finger printing; phosphorylation; pyruvate dehydrogenase; spermatozoa;
D O I
10.1016/j.cbpc.2004.02.006
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In our previous studies (Fujinoki et al., 2001, 2003), we reported that two types of 36 kDa proteins, designated 36K-A protein and 36K-B protein, obtained from hamster sperm flagella, are associated with motility activation and phosphorylated in a cAMP-dependent manner at serine residues. In the present experiments, we focused on the hamster (Mesocricetus auratus) 36K-A protein, which was analyzed by peptide mass finger printing and amino acid sequencing. The results suggest that 36K-A protein is a pyruvate dehydrogenase E1 component beta subunit lacking the N-terminal 30 amino acids. Moreover, our results suggest that 36 K-A protein is localized in the fibrous sheath of the principal piece of hamster spermatazoa. (C) 2004 Elsevier Inc. All rights reserved.
引用
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页码:509 / 520
页数:12
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