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Article: Immunocytochemical localization of cathepsin D in rat junctional epithelium.

TitleImmunocytochemical localization of cathepsin D in rat junctional epithelium.
Authors
Issue Date1993
PublisherSage Publications, Inc.. The Journal's web site is located at http://www.sagepub.com/journalsProdDesc.nav?prodId=Journal201925
Citation
Journal Of Dental Research, 1993, v. 72 n. 2, p. 502-507 How to Cite?
AbstractLocalization of cathepsin D was studied in the junctional epithelium (JE) of healthy rat gingivae by immuno-light and -electron microscopy, by means of both the avidin-biotin-peroxidase complex method and a colloidal gold IgG method. At the light-microscopic level, cathepsin D was demonstrated in the JE and oral sulcular epithelium (OSE). Cathepsin D immunoreactivity was remarkable in the coronal portion of the JE and decreased toward its apical portion. However, cathepsin D immunoreactivity in the basal cell layer of the JE was negligible or negative. In the OSE, the granular layer was positive for cathepsin D. In the adjacent connective tissue, many macrophage-like cells (not clear at this level) close to the basal cell layer showed strong immunoreactivity. At the electron microscopic level, cathepsin D was found in the primary lysosomes and trans-cisternae of Golgi apparatus in the JE cells. These lysosomes were often fused together or were fused with cathepsin D-negative intracytoplasmic vacuoles to form secondary lysosomes, which indicated that intracellular digestion may have been in progress. However, neutrophils contained few gold particles based on cathepsin D. It is likely that the amounts of cathepsin D contained in the JE cells and macrophages are larger than those of cathepsin D contained in the neutrophils. These findings provided morphological evidence that JE cells have the same endocytotic capacity as macrophages and neutrophils, and that JE cells participate in the intracellular digestion that is carried out by lysosomal enzymes such as cathepsin D. It is suggested, in addition, that maximum intracellular digestion occurs in the coronal portion of the JE.
Persistent Identifierhttp://hdl.handle.net/10722/153821
ISSN
2023 Impact Factor: 5.7
2023 SCImago Journal Rankings: 1.909
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorAyasaka, Nen_US
dc.contributor.authorGoto, Ten_US
dc.contributor.authorTsukuba, Ten_US
dc.contributor.authorKido, MAen_US
dc.contributor.authorNagata, Een_US
dc.contributor.authorKondo, Ten_US
dc.contributor.authorYamamoto, Ken_US
dc.contributor.authorTanaka, Ten_US
dc.date.accessioned2012-08-08T08:21:46Z-
dc.date.available2012-08-08T08:21:46Z-
dc.date.issued1993en_US
dc.identifier.citationJournal Of Dental Research, 1993, v. 72 n. 2, p. 502-507en_US
dc.identifier.issn0022-0345en_US
dc.identifier.urihttp://hdl.handle.net/10722/153821-
dc.description.abstractLocalization of cathepsin D was studied in the junctional epithelium (JE) of healthy rat gingivae by immuno-light and -electron microscopy, by means of both the avidin-biotin-peroxidase complex method and a colloidal gold IgG method. At the light-microscopic level, cathepsin D was demonstrated in the JE and oral sulcular epithelium (OSE). Cathepsin D immunoreactivity was remarkable in the coronal portion of the JE and decreased toward its apical portion. However, cathepsin D immunoreactivity in the basal cell layer of the JE was negligible or negative. In the OSE, the granular layer was positive for cathepsin D. In the adjacent connective tissue, many macrophage-like cells (not clear at this level) close to the basal cell layer showed strong immunoreactivity. At the electron microscopic level, cathepsin D was found in the primary lysosomes and trans-cisternae of Golgi apparatus in the JE cells. These lysosomes were often fused together or were fused with cathepsin D-negative intracytoplasmic vacuoles to form secondary lysosomes, which indicated that intracellular digestion may have been in progress. However, neutrophils contained few gold particles based on cathepsin D. It is likely that the amounts of cathepsin D contained in the JE cells and macrophages are larger than those of cathepsin D contained in the neutrophils. These findings provided morphological evidence that JE cells have the same endocytotic capacity as macrophages and neutrophils, and that JE cells participate in the intracellular digestion that is carried out by lysosomal enzymes such as cathepsin D. It is suggested, in addition, that maximum intracellular digestion occurs in the coronal portion of the JE.en_US
dc.languageengen_US
dc.publisherSage Publications, Inc.. The Journal's web site is located at http://www.sagepub.com/journalsProdDesc.nav?prodId=Journal201925en_US
dc.relation.ispartofJournal of Dental Researchen_US
dc.subject.meshAnimalsen_US
dc.subject.meshCathepsin D - Analysis - Metabolismen_US
dc.subject.meshEndocytosisen_US
dc.subject.meshEpithelial Attachment - Chemistry - Metabolism - Ultrastructureen_US
dc.subject.meshFemaleen_US
dc.subject.meshImmunohistochemistryen_US
dc.subject.meshMaleen_US
dc.subject.meshMicroscopy, Immunoelectronen_US
dc.subject.meshPhagosomes - Ultrastructureen_US
dc.subject.meshRatsen_US
dc.subject.meshRats, Wistaren_US
dc.subject.meshVacuoles - Ultrastructureen_US
dc.titleImmunocytochemical localization of cathepsin D in rat junctional epithelium.en_US
dc.typeArticleen_US
dc.identifier.emailGoto, T:gototk@hku.hken_US
dc.identifier.authorityGoto, T=rp01434en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1177/00220345930720020601-
dc.identifier.pmid8423247en_US
dc.identifier.scopuseid_2-s2.0-0027548275en_US
dc.identifier.volume72en_US
dc.identifier.issue2en_US
dc.identifier.spage502en_US
dc.identifier.epage507en_US
dc.identifier.isiWOS:A1993KK85700006-
dc.publisher.placeUnited Statesen_US
dc.identifier.scopusauthoridAyasaka, N=6602293449en_US
dc.identifier.scopusauthoridGoto, T=7403938313en_US
dc.identifier.scopusauthoridTsukuba, T=6701885833en_US
dc.identifier.scopusauthoridKido, MA=7102220426en_US
dc.identifier.scopusauthoridNagata, E=7005836211en_US
dc.identifier.scopusauthoridKondo, T=35353700200en_US
dc.identifier.scopusauthoridYamamoto, K=7407976230en_US
dc.identifier.scopusauthoridTanaka, T=7406724568en_US
dc.identifier.issnl0022-0345-

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