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Article: Localization of prostatic glycoconjugates by the lectin-gold method

TitleLocalization of prostatic glycoconjugates by the lectin-gold method
Authors
Issue Date1992
Citation
Acta Anatomica, 1992, v. 143 n. 1, p. 27-40 How to Cite?
AbstractThe glycoconjugates of the lateral prostate were examined ultrastructurally by lectin-gold histochemistry in combination with a low-temperature embedding technique using Lowicryl K4M. The binding patterns of concanavalin A, wheat germ agglutinin, Griffonia simplicifolia, soybean agglutinin, peanut agglutinin, Ricinus communis agglutinin isolectin I, Griffonia simplicifolia isolectin B 4, Ulex europaeus isolectin I and Phaseolus vulgaris agglutinin P have been documented in the subcellular compartments of the lateral prostate. The results show that the granular endoplasmic reticulum (GER) is rich in glycoproteins with mannosyl residues while the Golgi cisternae, secretory granules and microvilli are less so. The mannose (Man) and N-acetylgucosamine (GlcNAc) residues present in the GER of the epithelial cells may be associated with the initial assembly of the N-linked oligosaccharides of glycoproteins. The secretory granules exhibited different reactivities to lectins. Most of the lectin-binding sites confined to the limiting membranes may play a role in the transport of plasmalemma glycoconjugates to the apical plasma membrane. The epithelial Golgi stack is rich in GlcNAc, galactose (Gal), N-acetylgalactosamine (GalNAc) and sialic acid residues, and a compartmental organization of the Golgi stack is apparent which might be associated with the sequential addition of sugar residues to the oligosaccharides. The plasma membrane contains abundant Man, GlcNAc, Gal, GalNAc and complex carbohydrates, especially in the microvilli, and a differential lectin labelling was noted between the apical and basolateral plasma membrane. The present study showed that fucose-containing glycoconjugates were detected in the apical plasma membrane of the lateral prostate. The stromal extracellular matrices as well as the epithelial basement membranes demonstrated weak lectin reaction. Man, GlcNAc, Gal residues and complex sugars were also noted in the stromal tissues of the lateral prostate including the extracellular matrix, capillaries and smooth muscle.
Persistent Identifierhttp://hdl.handle.net/10722/149519
ISSN
2000 Impact Factor: 2.435
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, Len_US
dc.contributor.authorWong, YCen_US
dc.date.accessioned2012-06-26T05:54:46Z-
dc.date.available2012-06-26T05:54:46Z-
dc.date.issued1992en_US
dc.identifier.citationActa Anatomica, 1992, v. 143 n. 1, p. 27-40en_US
dc.identifier.issn0001-5180en_US
dc.identifier.urihttp://hdl.handle.net/10722/149519-
dc.description.abstractThe glycoconjugates of the lateral prostate were examined ultrastructurally by lectin-gold histochemistry in combination with a low-temperature embedding technique using Lowicryl K4M. The binding patterns of concanavalin A, wheat germ agglutinin, Griffonia simplicifolia, soybean agglutinin, peanut agglutinin, Ricinus communis agglutinin isolectin I, Griffonia simplicifolia isolectin B 4, Ulex europaeus isolectin I and Phaseolus vulgaris agglutinin P have been documented in the subcellular compartments of the lateral prostate. The results show that the granular endoplasmic reticulum (GER) is rich in glycoproteins with mannosyl residues while the Golgi cisternae, secretory granules and microvilli are less so. The mannose (Man) and N-acetylgucosamine (GlcNAc) residues present in the GER of the epithelial cells may be associated with the initial assembly of the N-linked oligosaccharides of glycoproteins. The secretory granules exhibited different reactivities to lectins. Most of the lectin-binding sites confined to the limiting membranes may play a role in the transport of plasmalemma glycoconjugates to the apical plasma membrane. The epithelial Golgi stack is rich in GlcNAc, galactose (Gal), N-acetylgalactosamine (GalNAc) and sialic acid residues, and a compartmental organization of the Golgi stack is apparent which might be associated with the sequential addition of sugar residues to the oligosaccharides. The plasma membrane contains abundant Man, GlcNAc, Gal, GalNAc and complex carbohydrates, especially in the microvilli, and a differential lectin labelling was noted between the apical and basolateral plasma membrane. The present study showed that fucose-containing glycoconjugates were detected in the apical plasma membrane of the lateral prostate. The stromal extracellular matrices as well as the epithelial basement membranes demonstrated weak lectin reaction. Man, GlcNAc, Gal residues and complex sugars were also noted in the stromal tissues of the lateral prostate including the extracellular matrix, capillaries and smooth muscle.en_US
dc.languageengen_US
dc.relation.ispartofActa Anatomicaen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCapillaries - Chemistryen_US
dc.subject.meshCell Nucleus - Chemistryen_US
dc.subject.meshEndoplasmic Reticulum - Chemistryen_US
dc.subject.meshGlycoconjugates - Analysisen_US
dc.subject.meshGolden_US
dc.subject.meshGolgi Apparatus - Chemistryen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshLectinsen_US
dc.subject.meshMaleen_US
dc.subject.meshMicrovilli - Chemistryen_US
dc.subject.meshProstate - Chemistry - Ultrastructureen_US
dc.subject.meshStaining And Labelingen_US
dc.titleLocalization of prostatic glycoconjugates by the lectin-gold methoden_US
dc.typeArticleen_US
dc.identifier.emailWong, YC:ycwong@hkucc.hku.hken_US
dc.identifier.authorityWong, YC=rp00316en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.pmid1374993-
dc.identifier.scopuseid_2-s2.0-0026533637en_US
dc.identifier.volume143en_US
dc.identifier.issue1en_US
dc.identifier.spage27en_US
dc.identifier.epage40en_US
dc.identifier.isiWOS:A1992HL87900005-
dc.identifier.scopusauthoridChan, L=35336076700en_US
dc.identifier.scopusauthoridWong, YC=7403041798en_US

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