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Titolo:
Serine phosphorylation of flagellar proteins associated with the motility activation of hamster spermatozoa
Autore:
Fujinoki, M; Ohtake, H; Okuno, M;
Indirizzi:
Dokkyo Univ, Sch Med, Dept Physiol, Mibu, Tochigi 3210293, Japan Dokkyo Univ Mibu Tochigi Japan 3210293 siol, Mibu, Tochigi 3210293, Japan Univ Tokyo, Grad Sch Arts & Sci, Dept Biol, Tokyo 1530041, Japan Univ Tokyo Tokyo Japan 1530041 ts & Sci, Dept Biol, Tokyo 1530041, Japan
Titolo Testata:
BIOMEDICAL RESEARCH-TOKYO
fascicolo: 1, volume: 22, anno: 2001,
pagine: 45 - 58
SICI:
0388-6107(200102)22:1<45:SPOFPA>2.0.ZU;2-U
Fonte:
ISI
Lingua:
ENG
Soggetto:
MAMMALIAN SPERM MOTILITY; TYROSINE PHOSPHORYLATION; MOUSE SPERM; GEL-ELECTROPHORESIS; ADENYLATE-CYCLASE; SEMINAL PLASMA; KINASE; CAPACITATION; INITIATION; HYPERACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
40
Recensione:
Indirizzi per estratti:
Indirizzo: Fujinoki, M Dokkyo Univ, Sch Med, Dept Physiol, Mibu, Tochigi 3210293, Japan Dokkyo Univ Mibu Tochigi Japan 3210293 Tochigi 3210293, Japan
Citazione:
M. Fujinoki et al., "Serine phosphorylation of flagellar proteins associated with the motility activation of hamster spermatozoa", BIOMED RES, 22(1), 2001, pp. 45-58

Abstract

It has been widely accepted that the motility of spermatozoa is regulated by phosphorylation of flagellar proteins. In order to understand the regulatory mechanisms of the motility of mammalian spermatozoa, we investigated protein phosphorylation associated with motility activation. For precise analyses, we designated four steps in motility activation. They were pre-initiation (immotile spermatozoa), initiation (calcium-independent activation), activation (calcium-dependent activation), and hyperactivation. We detected66K, 58K, and 36K proteins as the phosphoproteins related to the motility of spermatozoa. Among them, 36K proteins were separated into two different isoelectric proteins. When the motility of the spermatozoa was changed frompre-initiation to initiation, which is independent of calcium, 66K and 58Kproteins were exclusively phosphorylated. When the spermatozoa were activated from the initiation by extracellular calcium, two types of 36K proteinswere phosphorylated. All these proteins were phosphorylated at the serine residues. On the basis of the present results, we propose that the motilityof hamster spermatozoa may be regulated through at least two pathways of protein phosphorylation. Proteins of 66K and 58K are involved in a calcium-independent path way to initiate the motility of spermatozoa. On the other hand, two types of 36K proteins are involved in a calcium-dependent pathway to activate the motile spermatozoa.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/11/20 alle ore 18:57:11