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

页码：509 / 520

页数：12

共 56 条

[21] Motility-associated and cyclic AMP-dependent protein phosphorylation in the sperm of the chum salmon, Oncorhynchus keta [J].