Linked Life Data

18793616

Source:http://linkedlifedata.com/resource/pubmed/id/18793616

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2008-10-20
pubmed:abstractText
The stress 70 protein chaperone (STCH), a member of the heat shock protein 70 (HSP70) superfamily, is a microsomal protein that contains a N-terminal ATPase domain but lacks a C-terminal protein binding domain. Although cell-protective functions of HSP70 members are well characterized, the biological relevance of STCH remains unclear. We previously identified STCH as a candidate gene for susceptibility to stomach cancer by genetic analyses. In this study, we searched somatic mutations of STCH in human stomach cancer and identified the 668del12bp mutation in exon 4, resulting in a four amino acid deletion (del223V-226L) in the conserved ATP-binding domain. In vitro binding assays revealed that this mutant lacks ATP-binding activity. Overexpression of wild-type STCH sensitized cells to tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-induced cell death, whereas del223V-226L mutant did not show any effect. These results suggest that STCH has a role in cell survival via modulation of the TRAIL-mediated cell death pathway.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
21
pubmed:volume
376
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
499-503
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Stomach cancer-derived del223V-226L mutation of the STCH gene causes loss of sensitization to TRAIL-mediated apoptosis.
pubmed:affiliation
Department of Molecular Genetics, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka 812-8582, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't