Identification of 36 kDa phosphoprotein in fibrous sheath of hamster spermatozoa

• Published in: Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology Vol. 137; no. 4; pp. 509 - 520
• Main Authors: Fujinoki, Masakatsu, Kawamura, Takeshi, Toda, Toshifusa, Ohtake, Hideki, Ishimoda-Takagi, Tadashi, Shimizu, Nobuyoshi, Yamaoka, Sadao, Okuno, Makoto
• Format: Journal Article
• Language: English
• Published: England Elsevier Inc 01.04.2004
• Subjects: Amino Acid Sequence; Animals; Cricetinae; Cyclic AMP - metabolism; Fibrous sheath; Flagellum; Hamster; LC-MS/MS; Male; Molecular Sequence Data; Molecular Weight; Peptide mass finger printing; Peptides - analysis; Peptides - chemistry; Phosphoproteins - chemistry; Phosphoproteins - isolation & purification; Phosphorylation; Protein Subunits - analysis; Protein Subunits - chemistry; Protein Subunits - metabolism; Pyruvate dehydrogenase; Pyruvate Dehydrogenase (Lipoamide) - metabolism; Serine - chemistry; Sperm Tail - chemistry; Sperm Tail - enzymology; Sperm Tail - metabolism; Spermatozoa; Spermatozoa - chemistry; LC-MS/MS; Phosphorylation; Spermatozoa; Fibrous sheath; Flagellum; Peptide mass finger printing; Pyruvate dehydrogenase; Hamster
• ISSN: 1096-4959; 1879-1107
• DOI: 10.1016/j.cbpc.2004.02.006

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 β 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.