File Download
  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Cytochemical localisation and characterisation of proteoglycans (glycosaminoglycans) in the epithelial-stromal interface of the seminal vesicle of the guinea pig

TitleCytochemical localisation and characterisation of proteoglycans (glycosaminoglycans) in the epithelial-stromal interface of the seminal vesicle of the guinea pig
Authors
Issue Date1992
PublisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JOA
Citation
Journal Of Anatomy, 1992, v. 180, p. 41-56 How to Cite?
AbstractThe proteoglycans (PGs) in the guinea pig seminal vesicle were demonstrated ultrastructurally by both cuprolinic blue (CB) and ruthenium red (RR) staining. The PGs appeared as electron-dense granules with RR, but were filamentous following CB staining using the critical electrolyte concentration method. Three major types of PGs (T1, T2, T3) have been described according to their different locations and sizes. T1 filaments were short and were found mostly on both sides of the lamina densa of the basal lamina of the glandular epithelium (40-60 nm long) and also on the basal laminae of smooth muscle cells and capillary endothelial cells (20-30 nm long). In the epithelial basal lamina they were regularly spaced at an interval of 40-60 nm. T1 filaments in the lamina densa were smaller and more randomly distributed. Cytochemical characterisation of these PGs by various GAG degrading enzymes showed that T1 PGs are rich in heparan sulphate. T2 filaments were 30-40 nm long and closely associated with the collagen fibrils. They were arranged perpendicular to the long axis of collagen fibrils, also at intervals of about 60 nm. T2 filaments were removed by chondroitinase (Ch)-ABC, Ch-ABC plus Streptomyces (S)-hyaluronidase and pronase, but resistant to nitrous acid, heparitinase, heparinase, neuraminidase and S-hyaluronidase. These show that T2 filaments are rich in dermatan sulphate. T3 filaments (60-100 nm) were widely distributed in the stroma at sites such as the interstitial spaces of the lamina propria, the reticular layer below the basal lamina, around individual collagen fibrils or bundles of such fibres, and on the cell surfaces of fibroblasts. The T3 filaments were removed by Ch-ABC, Ch-AC and pronase but were resistant to heparitinase, heparinase, S hyaluronidase, neuraminidase and nitrous acid. They are therefore rich in chondroitin sulphate.
Persistent Identifierhttp://hdl.handle.net/10722/149520
ISSN
2015 Impact Factor: 2.154
2015 SCImago Journal Rankings: 1.056
PubMed Central ID
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorChan, Len_US
dc.contributor.authorWong, YCen_US
dc.date.accessioned2012-06-26T05:54:47Z-
dc.date.available2012-06-26T05:54:47Z-
dc.date.issued1992en_US
dc.identifier.citationJournal Of Anatomy, 1992, v. 180, p. 41-56en_US
dc.identifier.issn0021-8782en_US
dc.identifier.urihttp://hdl.handle.net/10722/149520-
dc.description.abstractThe proteoglycans (PGs) in the guinea pig seminal vesicle were demonstrated ultrastructurally by both cuprolinic blue (CB) and ruthenium red (RR) staining. The PGs appeared as electron-dense granules with RR, but were filamentous following CB staining using the critical electrolyte concentration method. Three major types of PGs (T1, T2, T3) have been described according to their different locations and sizes. T1 filaments were short and were found mostly on both sides of the lamina densa of the basal lamina of the glandular epithelium (40-60 nm long) and also on the basal laminae of smooth muscle cells and capillary endothelial cells (20-30 nm long). In the epithelial basal lamina they were regularly spaced at an interval of 40-60 nm. T1 filaments in the lamina densa were smaller and more randomly distributed. Cytochemical characterisation of these PGs by various GAG degrading enzymes showed that T1 PGs are rich in heparan sulphate. T2 filaments were 30-40 nm long and closely associated with the collagen fibrils. They were arranged perpendicular to the long axis of collagen fibrils, also at intervals of about 60 nm. T2 filaments were removed by chondroitinase (Ch)-ABC, Ch-ABC plus Streptomyces (S)-hyaluronidase and pronase, but resistant to nitrous acid, heparitinase, heparinase, neuraminidase and S-hyaluronidase. These show that T2 filaments are rich in dermatan sulphate. T3 filaments (60-100 nm) were widely distributed in the stroma at sites such as the interstitial spaces of the lamina propria, the reticular layer below the basal lamina, around individual collagen fibrils or bundles of such fibres, and on the cell surfaces of fibroblasts. The T3 filaments were removed by Ch-ABC, Ch-AC and pronase but were resistant to heparitinase, heparinase, S hyaluronidase, neuraminidase and nitrous acid. They are therefore rich in chondroitin sulphate.en_US
dc.languageengen_US
dc.publisherBlackwell Publishing Ltd. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JOAen_US
dc.relation.ispartofJournal of Anatomyen_US
dc.subject.meshAnimalsen_US
dc.subject.meshBasement Membrane - Metabolismen_US
dc.subject.meshChondroitin Sulfates - Analysisen_US
dc.subject.meshDermatan Sulfate - Analysisen_US
dc.subject.meshEpithelium - Metabolismen_US
dc.subject.meshGuinea Pigsen_US
dc.subject.meshHeparitin Sulfate - Analysisen_US
dc.subject.meshHistocytochemistryen_US
dc.subject.meshIndolesen_US
dc.subject.meshMaleen_US
dc.subject.meshMicroscopy, Electronen_US
dc.subject.meshOrganometallic Compoundsen_US
dc.subject.meshProteoglycans - Analysis - Chemistryen_US
dc.subject.meshRuthenium Reden_US
dc.subject.meshSeminal Vesicles - Metabolism - Ultrastructureen_US
dc.subject.meshStaining And Labelingen_US
dc.titleCytochemical localisation and characterisation of proteoglycans (glycosaminoglycans) in the epithelial-stromal interface of the seminal vesicle of the guinea pigen_US
dc.typeArticleen_US
dc.identifier.emailWong, YC:ycwong@hkucc.hku.hken_US
dc.identifier.authorityWong, YC=rp00316en_US
dc.description.naturelink_to_OA_fulltexten_US
dc.identifier.pmid1280636-
dc.identifier.pmcidPMC1259606-
dc.identifier.scopuseid_2-s2.0-0026603632en_US
dc.identifier.volume180en_US
dc.identifier.spage41en_US
dc.identifier.epage56en_US
dc.identifier.isiWOS:A1992HN50300005-
dc.publisher.placeUnited Kingdomen_US
dc.identifier.scopusauthoridChan, L=35336076700en_US
dc.identifier.scopusauthoridWong, YC=7403041798en_US

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats