Linked Life Data

12670688

Source:http://linkedlifedata.com/resource/pubmed/id/12670688

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-4-2
pubmed:abstractText
The antifungal mechanism of salivary histatin has been studied in Candida albicans and involves binding to a specific receptor, translocation across the membrane and targeting intracellularly. Cell death correlates with non-lytic release of ATP that may function as a cytotoxic mediator extracellularly. By sequential exposure to increasing concentrations of histatin 3, we generated histatin-resistant derivatives of C. albicans strain CA132A that show five-fold less killing at physiological concentrations of histatin 3. Protection against histatin killing in histatin-resistant derivatives is not due to alterations in binding, internalisation or degradation of histatin or efflux of ATP. These results indicate that protective mechanisms activated by exposure to histatin 3 may involve unidentified pathways downstream of binding and internalisation events.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Mar
pubmed:issn
0378-1097
pubmed:author
pubmed:issnType
Print
pubmed:day
28
pubmed:volume
220
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
247-53
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Binding, internalisation and degradation of histatin 3 in histatin-resistant derivatives of Candida albicans.
pubmed:affiliation
Department of Restorative Dentistry, School of Dental Science and Dublin Dental Hospital, University of Dublin, Trinity College, Dublin 2, Ireland. deirdre.fitzgerald@dental.tcd.ie
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't