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Titolo:
New insights into the origin, structure and role of CD52: A major component of the mammalian sperm glycocalyx
Autore:
Kirchhoff, C; Schroter, S;
Indirizzi:
Univ Hamburg, Inst Hormon & Fortpflanzungsforsch, D-22529 Hamburg, GermanyUniv Hamburg Hamburg Germany D-22529 ngsforsch, D-22529 Hamburg, Germany
Titolo Testata:
CELLS TISSUES ORGANS
fascicolo: 1-2, volume: 168, anno: 2001,
pagine: 93 - 104
SICI:
1422-6405(2001)168:1-2<93:NIITOS>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
RAT SPERMATOZOA; MONOCLONAL-ANTIBODIES; GENE-EXPRESSION; MEMBRANE-GLYCOPROTEINS; EPIDIDYMAL MATURATION; CAMPATH-1 ANTIGEN; PEPTIDE BACKBONE; PLASMA-MEMBRANE; DOG EPIDIDYMIS; CDW52 ANTIGEN;
Keywords:
CD52; sperm antigen HE5; glycans, N-linked; glycosylphosphatidyl-inositol anchor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Kirchhoff, C Univ Hamburg, Inst Hormon & Fortpflanzungsforsch, Grandweg 64, D-22529 Hamburg, Germany Univ Hamburg Grandweg 64 Hamburg Germany D-22529 rg, Germany
Citazione:
C. Kirchhoff e S. Schroter, "New insights into the origin, structure and role of CD52: A major component of the mammalian sperm glycocalyx", CELLS T ORG, 168(1-2), 2001, pp. 93-104

Abstract

The sperm glycocalyx represents the primary interface between the male gamete and its environment, and gamete interaction inevitably involves interaction with this structure. Thus, it has potential significance as a target for a nti bod ies that inhibit sperm function. Still, little is known about the components and biological role of the sperm glycocalyx. Despite the apparent complexity of the sperm membrane, surface carbohydrate labelling experiments show a high selectivity suggesting that carbohydrate side chains ofCD52, an unusually short, bipolar glycopeptide of epididymal origin, form major components of the sperm glycocalyx in all mammalian species investigated. Acquisition of the highly sialylated, lipid-anchored CD52 antigen is one of the few well-defined modifications that occur to the sperm membrane during epididymal passage. It would explain changes in lectin-binding patterns and also the remarkable surface charge differences occurring during epididymal transit, most probably attributable to its terminal sialic acid residues, CD52 seems to be immunodominant on human spermatozoa, and antibodies directed against it can agglutinate and completely immobilize human sperm in the presence of complement. Expression of the same peptide backbone in lymphocytes had largely discounted its consideration as a candidate for contraceptive development. However, the recent proof of male-specific modifications indicates the feasibility of this approach. Copyright (C) 2001 S. Karger AG, Basel.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 08:39:25