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Titolo:
CYTOCHEMICAL CHARACTERIZATION OF OLIGOSACCHARIDE SIDE-CHAINS OF THE GLYCOPROTEINS OF RAT ZONA-PELLUCIDA - AN ULTRASTRUCTURAL-STUDY
Autore:
AVILES M; MARTINEZMENARGUEZ JA; CASTELLS MT; MADRID JF; BALLESTA J;
Indirizzi:
UNIV MURCIA,SCH MED,DEPT CELL BIOL,HISTOL & GEN EMBRYOL SECT E-30071 MURCIA SPAIN UNIV MURCIA,SCH MED,DEPT CELL BIOL,HISTOL & GEN EMBRYOL SECT E-30071 MURCIA SPAIN UNIV BASQUE COUNTRY,SCH MED & DENT,DEPT CELL BIOL & MORPHOLOG SCI VIZCAYA SPAIN
Titolo Testata:
The Anatomical record
fascicolo: 2, volume: 239, anno: 1994,
pagine: 137 - 149
SICI:
0003-276X(1994)239:2<137:CCOOSO>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPERM SURFACE GALACTOSYLTRANSFERASE; ASPARAGINE-LINKED GLYCOPEPTIDES; CARBOHYDRATE-BINDING-PROPERTIES; COMPLEX-TYPE OLIGOSACCHARIDES; RICINUS-COMMUNIS AGGLUTININ; DATURA-STRAMONIUM LECTIN; ACETYL-D-GALACTOSAMINE; OVARIAN FOLLICLES; CONCANAVALIN-A; ELECTRON-MICROSCOPY;
Keywords:
CYTOCHEMISTRY; LECTIN; RAT ZONA PELLUCIDA; OOCYTE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
77
Recensione:
Indirizzi per estratti:
Citazione:
M. Aviles et al., "CYTOCHEMICAL CHARACTERIZATION OF OLIGOSACCHARIDE SIDE-CHAINS OF THE GLYCOPROTEINS OF RAT ZONA-PELLUCIDA - AN ULTRASTRUCTURAL-STUDY", The Anatomical record, 239(2), 1994, pp. 137-149

Abstract

Background: The zona pellucida (ZP), an extracellular matrix which surrounds mammalian oocytes, is formed by different glycoproteins. Several studies have revealed that carbohydrate residues present in glycoproteins of ZP play a key role in the sperm-egg recognition. However, the origin and the biochemical composition of ZP remain to be completelyresolved. Methods: ZP glycoproteins from rat ovarian follicles were investigated at light and electron microscopic level by the applicationof lectins conjugated to peroxidase, digoxigenin, and colloidal gold in combination with enzyme and chemical treatment. A quantitative analysis was also performed. Results: ZP shows reactivity to WGA, DSA, LFA, AAA, RCA I, and MAA. SBA and PNA showed a variable reactivity ranging from negative to strongly positive. A uniform pattern of binding throughout ZP was observed with DSA, Con A, AAA, MAA, and LFA. However, labeling by RCA I and SBA was higher in the outer ZP while PNA and WGA showed a higher binding in the inner ZP. Lectin reactivity was detected in cortical granules, endoplasmic reticulum, Golgi apparatus, vesicles, and multivesicular bodies of oocytes. Conclusions: ZP contained the terminal disaccharides Gal beta 1,4GlcNAc, Gal beta 1,3GalNAc, and GalNAc beta 1,3Gal and the trisaccharides Neu5Ac alpha 2, 3Gal beta 1,4GlcNAc, Neu5Ac-Gal beta 1,3GalNAc, and Neu5Ac-GalNAc beta 1,3Gal sequences. The occurrence of Fucose residues a 1,6 linked to the inner coreregion of N-linked glycoproteins of ZP was demonstrated by the use ofseveral fucose-specific lectins. Methylation-saponification treatmentin combination with lectin cytochemistry reveals that Gal, GalNAc, and polyl-lactosamine residues of rat ZP glycoproteins contain sulphatedgroups. The reactivity observed in ooplasmic vesicles was similar to that of ZP, thus suggesting that the oocyte is the site of synthesis of ZP glycoproteins. (C) 1994 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 07/07/20 alle ore 06:03:57