File Download

There are no files associated with this item.

  Links for fulltext
     (May Require Subscription)
Supplementary

Article: Human oral keratinocyte E-cadherin degradation by Candida albicans and Candida glabrata

TitleHuman oral keratinocyte E-cadherin degradation by Candida albicans and Candida glabrata
Authors
Issue Date2010
PublisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JOPM
Citation
Journal Of Oral Pathology And Medicine, 2010, v. 39 n. 3, p. 275-278 How to Cite?
AbstractBackground: E-cadherin (E-Cad) is a 120-kDa adhesive protein found in adherens junctions of the digestive tract epithelium. We tested the ability of two Candida strains to degrade human E-Cad in the Candida virulence factor perspective. Materials and methods: We set out to study oral mucosal E-Cad degradation by clinical and reference strains of Candida albicans and Candida glabrata. We also included hyphal and secreted aspartic proteinase (Sap) mutants of C. albicans to test the effect of yeast/hyphal transition on the ability to degrade E-Cad. The tests were performed at pH 4 and pH 6 to determine the effect of local tissue acidity on the activation of Saps. The C. albicans strains used were: CCUG 32723; clinical strain SC5314 which is known to be strongly invasive; hyphal mutants of SC5314: HLC52 (efg1/efg1), HLC54 (cph1/cph1 efg1/efg1) and JKC19 (cph1/cph1); clinical strain B1134; Sap 1-3 and Sap 4-6 mutants of SC5314. The C. glabrata strains used were ATCC 90030, and the clinical strains 5WT and G212. Results: The sonicated yeast cells of C. albicans JKC19 and SC5314, both in hyphal form, degraded E-Cad at pH 4. The 10× concentrated growth media of the strains HLC-52, HLC-54, 32723 and B1134; all in yeast form, caused degradation at pH 4, HLC-52 and HLC-54 also at pH 6. The C. glabrata strains did not degrade E-Cad. Conclusions: pH is a strain dependent triggering factor in activating yeast or hyphal form related Candida Saps in degrading epithelial cell associated E-Cads. © 2010 John Wiley & Sons A/S.
Persistent Identifierhttp://hdl.handle.net/10722/154598
ISSN
2015 Impact Factor: 1.859
2015 SCImago Journal Rankings: 0.731
ISI Accession Number ID
Funding AgencyGrant Number
Helsinki University Central Hospital EVOT1020Y0003
Funding Information:

We wish to thank Ms Pipsa Kaipainen and Ms Marja-Leena Piironen for experienced technical assistance and tissue culturing and The Finnish Womens' Dental Association for a grant to this study. Special thanks to University lecturer Pirjo Nikula-Ijas, Department of Biochemistry, University of Helsinki, for assisting in the proteinase activity calculations. Laboratory facilities were funded by the Helsinki University Central Hospital EVO-grant (T1020Y0003).

References

 

DC FieldValueLanguage
dc.contributor.authorPärnänen, Pen_US
dc.contributor.authorMeurman, JHen_US
dc.contributor.authorSamaranayake, Len_US
dc.contributor.authorVirtanen, Ien_US
dc.date.accessioned2012-08-08T08:26:25Z-
dc.date.available2012-08-08T08:26:25Z-
dc.date.issued2010en_US
dc.identifier.citationJournal Of Oral Pathology And Medicine, 2010, v. 39 n. 3, p. 275-278en_US
dc.identifier.issn0904-2512en_US
dc.identifier.urihttp://hdl.handle.net/10722/154598-
dc.description.abstractBackground: E-cadherin (E-Cad) is a 120-kDa adhesive protein found in adherens junctions of the digestive tract epithelium. We tested the ability of two Candida strains to degrade human E-Cad in the Candida virulence factor perspective. Materials and methods: We set out to study oral mucosal E-Cad degradation by clinical and reference strains of Candida albicans and Candida glabrata. We also included hyphal and secreted aspartic proteinase (Sap) mutants of C. albicans to test the effect of yeast/hyphal transition on the ability to degrade E-Cad. The tests were performed at pH 4 and pH 6 to determine the effect of local tissue acidity on the activation of Saps. The C. albicans strains used were: CCUG 32723; clinical strain SC5314 which is known to be strongly invasive; hyphal mutants of SC5314: HLC52 (efg1/efg1), HLC54 (cph1/cph1 efg1/efg1) and JKC19 (cph1/cph1); clinical strain B1134; Sap 1-3 and Sap 4-6 mutants of SC5314. The C. glabrata strains used were ATCC 90030, and the clinical strains 5WT and G212. Results: The sonicated yeast cells of C. albicans JKC19 and SC5314, both in hyphal form, degraded E-Cad at pH 4. The 10× concentrated growth media of the strains HLC-52, HLC-54, 32723 and B1134; all in yeast form, caused degradation at pH 4, HLC-52 and HLC-54 also at pH 6. The C. glabrata strains did not degrade E-Cad. Conclusions: pH is a strain dependent triggering factor in activating yeast or hyphal form related Candida Saps in degrading epithelial cell associated E-Cads. © 2010 John Wiley & Sons A/S.en_US
dc.languageengen_US
dc.publisherBlackwell Munksgaard. The Journal's web site is located at http://www.blackwellpublishing.com/journals/JOPMen_US
dc.relation.ispartofJournal of Oral Pathology and Medicineen_US
dc.subject.meshAspartic Acid Endopeptidases - Metabolismen_US
dc.subject.meshCadherins - Metabolismen_US
dc.subject.meshCandida Albicans - Classification - Metabolism - Pathogenicityen_US
dc.subject.meshCandida Glabrata - Classification - Metabolism - Pathogenicityen_US
dc.subject.meshCell Adhesionen_US
dc.subject.meshCell Lineen_US
dc.subject.meshEpithelial Cells - Metabolism - Microbiologyen_US
dc.subject.meshFungal Proteins - Metabolismen_US
dc.subject.meshHumansen_US
dc.subject.meshHydrogen-Ion Concentrationen_US
dc.subject.meshHyphae - Metabolismen_US
dc.subject.meshKeratinocytes - Metabolism - Microbiologyen_US
dc.subject.meshMouth Mucosa - Cytology - Microbiologyen_US
dc.subject.meshVirulence - Physiologyen_US
dc.titleHuman oral keratinocyte E-cadherin degradation by Candida albicans and Candida glabrataen_US
dc.typeArticleen_US
dc.identifier.emailSamaranayake, L:lakshman@hku.hken_US
dc.identifier.authoritySamaranayake, L=rp00023en_US
dc.description.naturelink_to_subscribed_fulltexten_US
dc.identifier.doi10.1111/j.1600-0714.2009.00866.xen_US
dc.identifier.pmid20359311en_US
dc.identifier.scopuseid_2-s2.0-77249166684en_US
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-77249166684&selection=ref&src=s&origin=recordpageen_US
dc.identifier.volume39en_US
dc.identifier.issue3en_US
dc.identifier.spage275en_US
dc.identifier.epage278en_US
dc.identifier.isiWOS:000274668700013-
dc.publisher.placeDenmarken_US
dc.identifier.scopusauthoridPärnänen, P=24344880300en_US
dc.identifier.scopusauthoridMeurman, JH=7006469347en_US
dc.identifier.scopusauthoridSamaranayake, L=7102761002en_US
dc.identifier.scopusauthoridVirtanen, I=7102648106en_US
dc.identifier.citeulike6801855-

Export via OAI-PMH Interface in XML Formats


OR


Export to Other Non-XML Formats