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Article: The expression of secreted aspartyl proteinases of Candida species in human whole saliva

TitleThe expression of secreted aspartyl proteinases of Candida species in human whole saliva
Authors
Issue Date1999
PublisherSociety for General Microbiology. The Journal's web site is located at http://jmm.sgmjournals.org
Citation
Journal Of Medical Microbiology, 1999, v. 48 n. 8, p. 711-720 How to Cite?
AbstractThe expression of secreted aspartyl proteinases (Saps) by clinical isolates of Candida albicans, C. tropicalis and C. parapsilosis in human saliva supplemented with glucose and in a proteinase-inducing medium (YCB-BSA), was investigated. Also, yeast growth, pH fluctuation and total protein concentration of the saliva cultures during incubation were measured. Sap expression was assessed by evaluating the enzyme activity as well as the antigen concentration. Saps were expressed well in human saliva supplemented with glucose by all three Candida species, although greater expressions was found in YCB-BSA medium. C. albicans isolates were significantly more proteolytic than the non-albicans isolates. In general, for all three species, the rate of yeast growth, pH fluctuation and percentage reduction of total salivary protein concentration concurred with the degree of expression of Saps. These data strongly suggest that Saps of C. albicans, C. tropicalis and C. parapsilosis may play an active role in the progression of oral candidoses, particularly with regard to the abundance of low pH micro-environments in the oral cavity, which are regularly replenished with dietary carbohydrates.
Persistent Identifierhttp://hdl.handle.net/10722/66105
ISSN
2015 Impact Factor: 2.269
2015 SCImago Journal Rankings: 1.060
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorWu, Ten_HK
dc.contributor.authorSamaranayake, LPen_HK
dc.date.accessioned2010-09-06T05:43:37Z-
dc.date.available2010-09-06T05:43:37Z-
dc.date.issued1999en_HK
dc.identifier.citationJournal Of Medical Microbiology, 1999, v. 48 n. 8, p. 711-720en_HK
dc.identifier.issn0022-2615en_HK
dc.identifier.urihttp://hdl.handle.net/10722/66105-
dc.description.abstractThe expression of secreted aspartyl proteinases (Saps) by clinical isolates of Candida albicans, C. tropicalis and C. parapsilosis in human saliva supplemented with glucose and in a proteinase-inducing medium (YCB-BSA), was investigated. Also, yeast growth, pH fluctuation and total protein concentration of the saliva cultures during incubation were measured. Sap expression was assessed by evaluating the enzyme activity as well as the antigen concentration. Saps were expressed well in human saliva supplemented with glucose by all three Candida species, although greater expressions was found in YCB-BSA medium. C. albicans isolates were significantly more proteolytic than the non-albicans isolates. In general, for all three species, the rate of yeast growth, pH fluctuation and percentage reduction of total salivary protein concentration concurred with the degree of expression of Saps. These data strongly suggest that Saps of C. albicans, C. tropicalis and C. parapsilosis may play an active role in the progression of oral candidoses, particularly with regard to the abundance of low pH micro-environments in the oral cavity, which are regularly replenished with dietary carbohydrates.en_HK
dc.languageengen_HK
dc.publisherSociety for General Microbiology. The Journal's web site is located at http://jmm.sgmjournals.orgen_HK
dc.relation.ispartofJournal of Medical Microbiologyen_HK
dc.subject.meshAnimalsen_HK
dc.subject.meshAspartic Acid Endopeptidases - metabolism - secretionen_HK
dc.subject.meshBlotting, Westernen_HK
dc.subject.meshCandida - drug effects - enzymology - growth & developmenten_HK
dc.subject.meshCandida albicans - drug effects - enzymology - growth & developmenten_HK
dc.subject.meshCattleen_HK
dc.subject.meshCulture Media - pharmacologyen_HK
dc.subject.meshCulture Media, Conditioned - chemistry - metabolismen_HK
dc.subject.meshGlucose - pharmacologyen_HK
dc.subject.meshHumansen_HK
dc.subject.meshHydrogen-Ion Concentrationen_HK
dc.subject.meshSalivaen_HK
dc.subject.meshSalivary Proteins and Peptides - metabolismen_HK
dc.subject.meshSerum Albumin, Bovine - pharmacologyen_HK
dc.titleThe expression of secreted aspartyl proteinases of Candida species in human whole salivaen_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://library.hku.hk:4550/resserv?sid=HKU:IR&issn=2150-1203&volume=48&spage=711&epage=720&date=1999&atitle=The+expression+of+secreted+aspartyl+proteinases+of+Candida+species+in+human+whole+salivaen_HK
dc.identifier.emailSamaranayake, LP:lakshman@hku.hken_HK
dc.identifier.authoritySamaranayake, LP=rp00023en_HK
dc.description.naturelink_to_subscribed_fulltext-
dc.identifier.pmid10450994-
dc.identifier.scopuseid_2-s2.0-0032859994en_HK
dc.identifier.hkuros42684en_HK
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032859994&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume48en_HK
dc.identifier.issue8en_HK
dc.identifier.spage711en_HK
dc.identifier.epage720en_HK
dc.identifier.isiWOS:000081722100002-
dc.publisher.placeUnited Kingdomen_HK
dc.identifier.scopusauthoridWu, T=9237315300en_HK
dc.identifier.scopusauthoridSamaranayake, LP=7102761002en_HK

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