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Titolo:
GLYCOSYLATION IN GOLGI-APPARATUS OF EARLY SPERMATIDS OF RAT - A HIGH-RESOLUTION LECTIN CYTOCHEMICAL STUDY
Autore:
MARTINEZMENARGUEZ JA; AVILES M; MADRID JF; CASTELLS MT; BALLESTA J;
Indirizzi:
UNIV MURCIA,SCH MED,DEPT CELL BIOL,HISTOL & GEN EMBRYOL LAB E-30071 MURCIA SPAIN UNIV MURCIA,SCH MED,DEPT CELL BIOL,HISTOL & GEN EMBRYOL LAB E-30071 MURCIA SPAIN UNIV PAIS VASCO,SCH MED,DEPT CELL BIOL & MORPHOL SCI BILBAO SPAIN
Titolo Testata:
European journal of cell biology
fascicolo: 1, volume: 61, anno: 1993,
pagine: 21 - 33
SICI:
0171-9335(1993)61:1<21:GIGOES>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
ASPARAGINE-LINKED OLIGOSACCHARIDES; BETA-N-ACETYLGLUCOSAMINIDASE; COMPLEX-TYPE OLIGOSACCHARIDES; DATURA-STRAMONIUM LECTIN; HORSERADISH-PEROXIDASE; ELECTRON-MICROSCOPY; CONCANAVALIN-A; ULTRASTRUCTURAL-LOCALIZATION; SUBCELLULAR ORGANIZATION; THIAMINE PYROPHOSPHATASE;
Keywords:
RAT SPERMATIDS; GOLGI APPARATUS; GLYCOSYLATION; LECTIN CYTOCHEMISTRY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
69
Recensione:
Indirizzi per estratti:
Citazione:
J.A. Martinezmenarguez et al., "GLYCOSYLATION IN GOLGI-APPARATUS OF EARLY SPERMATIDS OF RAT - A HIGH-RESOLUTION LECTIN CYTOCHEMICAL STUDY", European journal of cell biology, 61(1), 1993, pp. 21-33

Abstract

In the present study, lectin cytochemistry in combination with enzymeand chemical treatments and ultrastructural immunocytochemistry were applied to investigate the formation of acrosomal glycoproteins in endoplasmic reticulum (ER) and Golgi apparatus (GA) of early rat spermatids. In addition, the vesicles involved in glycoprotein traffic were investigated using a monoclonal antibody against clathrin. The results obtained suggest the occurrence of high mannose and complex type N-linked oligosaccharides and mucin type O-linked oligosaccharides. In N-linked glycoproteins, Man residues are incorporated into the nascent oligosaccharide in the ER, Fuc residues of the inner core of the oligosaccharide in the cis region of GA, GlcNAc in medial cisternae of GA and Gal residues in the transmost cisternae of GA. In O-linked glycoproteins, the addition of GalNAc occurs in cis and trans cisternae of GA. Galbeta 1,3GalNAc sequence was detected in medial and trans cisternae ofGA. Sialic acid was detected in both N- and O-linked oligosaccharidesin medial and trans cisternae of GA but not in acrosomes. Immunoreactivity to clathrin was observed in the intermediate zone between ER andGA and in vesicles of the trans side of GA.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 12/07/20 alle ore 12:48:19