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Titolo:
THE PH-20 PROTEIN IN CYNOMOLGUS MACAQUE SPERMATOZOA - IDENTIFICATION OF 2 DIFFERENT FORMS EXHIBITING HYALURONIDASE ACTIVITY
Autore:
CHERR GN; MEYERS SA; YUDIN AI; VANDEVOORT CA; MYLES DG; PRIMAKOFF P; OVERSTREET JW;
Indirizzi:
UNIV CALIF DAVIS,SCH MED,BODEGA MARINE LAB DAVIS CA 95616 UNIV CALIF DAVIS,SCH MED,DEPT ENVIRONM TOXICOL DAVIS CA 95616 UNIV CALIF DAVIS,SCH MED,CALIF REG PRIMATE RES CTR DAVIS CA 95616 UNIV CALIF DAVIS,SCH MED,DEPT OBSTET & GYNECOL,DIV REPROD BIOL & MED DAVIS CA 95616 UNIV CONNECTICUT,CTR HLTH,DEPT PHYSIOL FARMINGTON CT 06030
Titolo Testata:
Developmental biology
fascicolo: 1, volume: 175, anno: 1996,
pagine: 142 - 153
SICI:
0012-1606(1996)175:1<142:TPPICM>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUINEA-PIG SPERM; ACROSOME REACTION; ZONA-PELLUCIDA; MULTIPLE FORMS; HAMSTER SPERMATOZOA; SURFACE PROTEIN; GOLDEN-HAMSTER; BULL SPERM; INVITRO; PURIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
G.N. Cherr et al., "THE PH-20 PROTEIN IN CYNOMOLGUS MACAQUE SPERMATOZOA - IDENTIFICATION OF 2 DIFFERENT FORMS EXHIBITING HYALURONIDASE ACTIVITY", Developmental biology, 175(1), 1996, pp. 142-153

Abstract

In these experiments, we have characterized the bifunctional sperm protein PH-20 in macaque sperm and studied its hyaluronidase activity. Intact sperm were evaluated before the acrosome reaction (AR), and a soluble form of PH-20 released during acrosomal exocytosis was also investigated. Western blots of SDS-PAGE of acrosome-intact sperm extracts revealed a 64-kDa form of PH-20 was recognized by a polyclonal antibody (R-10) raised in rabbits against purified, recombinant cynomolgus macaque sperm PH-20. The soluble components released during the AR whichwere recognized by the R-10 antibody included both the 64-kDa form and a 53-kDa form of PH-20. An ELISA-like procedure for determining PH-20 hyaluronidase activity indicated that acrosome-intact sperm exhibited two peaks of hyaluronidase activity near pH 4 and greater than or equal to pH 7. The majority of enzyme activity in acrosome-intact sperm extracts occurred at neutral pH, while the soluble hyaluronidase activity released at the AR was predominantly acid-active. Hyaluronidase activity of PH-20 at different pH optima was investigated using hyaluronic acid substrate gel electrophoresis, and results indicated that the 64-kDa polypeptide had a broad range, with the majority of activity atneutral pH (pH 7). The 53-kDa polypeptide in sperm extracts only exhibited activity at acid pH (pH 4), The hyaluronidase activities of bothenzymes could be inhibited by apigenin. The soluble PH-20 hyaluronidase activity released during the AR was primarily of the acid-active 53-kDa form. fine structural localization of PH-20 using Fab fragments of R-10 IgG demonstrated that PH-20 was associated not only with sperm membranes, but also with the dispersing acrosomal contents. These datasuggest that the more neutral-active form of PH-20 (64 kDa) is present on the plasma and inner acrosomal membranes and gives rise to the soluble acid-active form at the time of the AR. The generation of the soluble form of PH-20 may result from the action of acrosomal enzymes, which could include proteases, glycosidases, and phospholipases. (C) 1996 Academic Press, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/12/20 alle ore 12:44:57