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Titolo:
HUMAN SPERM SURFACE GLYCOPROTEIN INVOLVED IN SPERM ZONA-PELLUCIDA INTERACTION
Autore:
BATOVA IN; IVANOVA MD; MOLLOVA MV; KYURKCHIEV SD;
Indirizzi:
BULGARIAN ACAD SCI,DEPT IMMUNOBIOL,INST BIOL & IMMUNOL,AVE TSARIGRADSKO SHOSSE 73 BU-1113 SOFIA BULGARIA BULGARIAN ACAD SCI,DEPT MOL IMMUNOL,INST BIOL & IMMUNOL BU-1113 SOFIABULGARIA
Titolo Testata:
International journal of andrology
fascicolo: 3, volume: 21, anno: 1998,
pagine: 141 - 153
SICI:
0105-6263(1998)21:3<141:HSSGII>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
GUINEA-PIG SPERM; PLASMA-MEMBRANE ANTIGEN; MOUSE SPERM; MONOCLONAL-ANTIBODIES; MAMMALIAN FERTILIZATION; ACROSOME REACTION; INVITRO CAPACITATION; BOAR SPERMATOZOA; RAT SPERMATOZOA; BINDING-PROTEIN;
Keywords:
EPIDIDYMIS; FERTILIZATION; HUMAN SPERM GLYCOPROTEIN; INHIBITION; MONOCLONAL ANTIBODY; SEMINAL PLASMA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
64
Recensione:
Indirizzi per estratti:
Citazione:
I.N. Batova et al., "HUMAN SPERM SURFACE GLYCOPROTEIN INVOLVED IN SPERM ZONA-PELLUCIDA INTERACTION", International journal of andrology, 21(3), 1998, pp. 141-153

Abstract

To identify peptide-specific antibodies which define sperm surface antigens, hybridomas were derived from the splenocytes of mice immunizedwith swollen human spermatozoa which had been subjected to limited proteolytic cleavage under reducing conditions prior to immunization. A total of 13.7% of the hybrid clones secreted antibodies which reacted with deglycosylated human seminal plasma glycoproteins when screened by an ELISA. A monoclonal antibody, designated mAb 4A8 sp., specifying a peptide epitope of human epididymal and a sperm surface glycoproteinwas selected which inhibited human sperm-egg binding in a dose-dependent manner, and totally blocked sperm penetration in vitro. This inhibition did not result from an effect of the antibody on the motility ofspermatozoa, nor was it due to premature induction of the acrosome reaction. Exclusion of oligosaccharide chains by chemical hydrolysis with trifluoromethane sulphonic acid (TFMS), enzymatic degradation and binding of lectins, did not abrogate the reactivity of mAb 4A8 to the cognate epitope whereas antibody binding was precluded upon digestion with proteolytic enzymes. In Western immunoblots of human seminal plasmaglycoproteins, the antigen presented as a set of immunoreactive polypeptides, a major glycoprotein of M-r 78 kDa and less prominent bands of M-r 56 and 44 kDa. Immunocytochemical staining of a number of human reproductive and somatic tissues revealed strong immunostaining of theluminal epithelium of the epididymis as well as of spermatozoa in thelumen. Immunolocalization to the plasma membrane of ejaculated human spermatozoa was demonstrated by immunofluorescence, although on undigested spermatozoa the antigen epitope was less accessible. Upon capacitation the antigen persisted on the sperm surface and was present on the head of capacitated acrosome-intact spermatozoa. The pronounced peripheral immunostaining of the sperm head was accentuated after DTT/trypsin treatment, implicating the dynamic accessibility of the epitope onthe plasma membrane of capacitated spermatozoa. It is suggested that the protein in question appears on the sperm membrane as a consequenceof its modification in the epididymis (insertion and processing), andmay be involved in the processes leading to sperm attachment and interaction with the human zona pellucida.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/11/20 alle ore 02:49:35