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Article: Characterization of glycoconjugates of guinea pig seminal vesicle by lectin histochemistry

TitleCharacterization of glycoconjugates of guinea pig seminal vesicle by lectin histochemistry
Authors
Issue Date1998
PublisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=1567-2379
Citation
Histochemical Journal, 1998, v. 30 n. 6, p. 447-459 How to Cite?
AbstractIn the present study, the expression of glycoconjugates in the guinea pig seminal vesicle was localized and partially characterized by lectin histochemistry using a battery of 30 different lectins specific for different carbohydrate residues. The results indicate that the glandular epithelium of the guinea pig seminal vesicle exhibits complex glycoconjugates rich in Man, β-GlcNAc, β-Gal, α/β-GalNAc, Fuc and complex NeuAc(α2,6)Gal/GalNAc residues, as shown by its positive reactions to most lectins used. The Golgi region of the luminal secretory epithelial cells expresses a complex glycoconjugate pattern, as shown by its strong reactions to Man-(PSA, GNA), β-GlcNAc-(S-WGA, PWA, DSA, UDA), βGal-(RCA-I and -II), α/β-GalNAc-(SBA, Jac, VVA, BPA) and complex NeuAc-(SNA) specific lectins, indicating that the secretory epithelial cells are active in glycosylation and secretion process. It was also shown in the present study that the basal and luminal epithelial cells are different in their glycoconjugates. The basal epithelial cells are rich in NeuAc(α2,3)Gal residues as they are stained specifically by MAA. The fibroblasts in the epithelial-smooth muscle interface and the smooth muscle cells close to the glandular epithelium are shown to express more glycoconjugates as they are stained intensely by GS-I-B4, GS-II and SBA. However, their role in the epithelial-stromal interaction in the seminal vesicle remains to be elucidated. In summary, the present study reports for the first time on the lectin binding patterns of the guinea pig seminal vesicle, and the results show that the seminal vesicle epithelium elaborates and secretes glycoconjugates in a complex pattern. Some of the lectins might be useful as histochemical markers for the secretory activity and specific structural components in the guinea pig seminal vesicle.
Persistent Identifierhttp://hdl.handle.net/10722/67346
ISSN
2004 Impact Factor: 0.928
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorChan, FLen_HK
dc.contributor.authorWong, YCen_HK
dc.date.accessioned2010-09-06T05:54:18Z-
dc.date.available2010-09-06T05:54:18Z-
dc.date.issued1998en_HK
dc.identifier.citationHistochemical Journal, 1998, v. 30 n. 6, p. 447-459en_HK
dc.identifier.issn0018-2214en_HK
dc.identifier.urihttp://hdl.handle.net/10722/67346-
dc.description.abstractIn the present study, the expression of glycoconjugates in the guinea pig seminal vesicle was localized and partially characterized by lectin histochemistry using a battery of 30 different lectins specific for different carbohydrate residues. The results indicate that the glandular epithelium of the guinea pig seminal vesicle exhibits complex glycoconjugates rich in Man, β-GlcNAc, β-Gal, α/β-GalNAc, Fuc and complex NeuAc(α2,6)Gal/GalNAc residues, as shown by its positive reactions to most lectins used. The Golgi region of the luminal secretory epithelial cells expresses a complex glycoconjugate pattern, as shown by its strong reactions to Man-(PSA, GNA), β-GlcNAc-(S-WGA, PWA, DSA, UDA), βGal-(RCA-I and -II), α/β-GalNAc-(SBA, Jac, VVA, BPA) and complex NeuAc-(SNA) specific lectins, indicating that the secretory epithelial cells are active in glycosylation and secretion process. It was also shown in the present study that the basal and luminal epithelial cells are different in their glycoconjugates. The basal epithelial cells are rich in NeuAc(α2,3)Gal residues as they are stained specifically by MAA. The fibroblasts in the epithelial-smooth muscle interface and the smooth muscle cells close to the glandular epithelium are shown to express more glycoconjugates as they are stained intensely by GS-I-B4, GS-II and SBA. However, their role in the epithelial-stromal interaction in the seminal vesicle remains to be elucidated. In summary, the present study reports for the first time on the lectin binding patterns of the guinea pig seminal vesicle, and the results show that the seminal vesicle epithelium elaborates and secretes glycoconjugates in a complex pattern. Some of the lectins might be useful as histochemical markers for the secretory activity and specific structural components in the guinea pig seminal vesicle.en_HK
dc.languageengen_HK
dc.publisherSpringer Verlag Dordrecht. The Journal's web site is located at http://springerlink.metapress.com/openurl.asp?genre=journal&issn=1567-2379en_HK
dc.relation.ispartofHistochemical Journalen_HK
dc.subject.meshAcetylgalactosamine - metabolismen_HK
dc.subject.meshAcetylglucosamine - metabolismen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshCell Membrane - metabolismen_HK
dc.subject.meshEpithelial Cells - metabolismen_HK
dc.subject.meshFucose - metabolismen_HK
dc.subject.meshGalactose - metabolismen_HK
dc.subject.meshGlucose - metabolismen_HK
dc.subject.meshGlycoconjugates - metabolismen_HK
dc.subject.meshGuinea Pigsen_HK
dc.subject.meshHistocytochemistryen_HK
dc.subject.meshLectins - metabolismen_HK
dc.subject.meshMaleen_HK
dc.subject.meshMannose - metabolismen_HK
dc.subject.meshN-Acetylneuraminic Acid - metabolismen_HK
dc.subject.meshSeminal Vesicles - metabolismen_HK
dc.titleCharacterization of glycoconjugates of guinea pig seminal vesicle by lectin histochemistryen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0018-2214&volume=30&spage=447&epage=459&date=1998&atitle=Characterization+of+glycoconjugates+of+guinea+pig+seminal+vesicle+by+lectin+histochemistryen_HK
dc.identifier.emailWong, YC:ycwong@hkucc.hku.hken_HK
dc.identifier.authorityWong, YC=rp00316en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.doi10.1023/A:1003264007923en_HK
dc.identifier.pmid10192544-
dc.identifier.scopuseid_2-s2.0-0031832504en_HK
dc.identifier.hkuros33621en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0031832504&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume30en_HK
dc.identifier.issue6en_HK
dc.identifier.spage447en_HK
dc.identifier.epage459en_HK
dc.identifier.isiWOS:000074495000008-
dc.publisher.placeNetherlandsen_HK
dc.identifier.scopusauthoridChan, FL=7202586505en_HK
dc.identifier.scopusauthoridWong, YC=7403041798en_HK

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