Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
2004-11-16
pubmed:abstractText
Heat shock protein 40 (Hsp40) family proteins are known to bind to Hsp70 through their J-domain and regulate the function of Hsp70 by stimulating its adenosine triphosphatase activity. In the endoplasmic reticulum (ER), there are 5 Hsp40 family proteins known so far, 3 of which were recently identified. In this report, one of the novel Hsp40 cochaperones, ERdj3, was characterized in terms of its subcellular localization, stress response, and stress tolerance of cells. By using ERdj3-specific polyclonal antibody, endogenous ERdj3 protein was shown to reside in the ER as gene transfer-mediated exogenous ERdj3. Analysis of the expression level of endogenous ERdj3 protein revealed its moderate induction in response to various ER stressors, indicating its possible action as a stress protein in the ER. Subsequently, we analyzed whether this molecule was involved in ER stress tolerance of cells, as was the case with the ER-resident Hsp70 family protein BiP. Although overexpression of ERdj3 by gene transfection could not strengthen ER stress tolerance of neuroblastoma cells, reduction of ERdj3 expression by small interfering ribonucleic acid decreased the tolerance of cells, indicating that ERdj3 might have just a marginal role in the ER stress resistance of neuroblastoma cells. In contrast, overexpression of ERdj3 notably suppressed vero toxin-induced cell death. These data suggest that ERdj3 might have diverse roles in the ER, including that of the molecular cochaperone of BiP and an as yet unknown protective action against vero toxin.
pubmed:commentsCorrections
http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-10221986, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-10346810, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-10395641, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-10444163, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-10543453, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-10567425, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-10587643, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-10827079, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-11147971, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-11406343, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-11504627, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-11584023, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-11836248, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-11920296, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-11935289, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-12380683, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-12380691, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-12411443, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-12446677, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-14587667, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-7875597, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-8016869, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-9585179, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-9600925, http://linkedlifedata.com/resource/pubmed/commentcorrection/15544163-9644977
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1355-8145
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
253-64
pubmed:dateRevised
2009-11-18
pubmed:meshHeading
pubmed-meshheading:15544163-Amino Acid Sequence, pubmed-meshheading:15544163-Animals, pubmed-meshheading:15544163-Cell Death, pubmed-meshheading:15544163-Cell Line, Tumor, pubmed-meshheading:15544163-Down-Regulation, pubmed-meshheading:15544163-Endoplasmic Reticulum, pubmed-meshheading:15544163-Female, pubmed-meshheading:15544163-Gene Expression Regulation, pubmed-meshheading:15544163-HSP40 Heat-Shock Proteins, pubmed-meshheading:15544163-HeLa Cells, pubmed-meshheading:15544163-Heat-Shock Proteins, pubmed-meshheading:15544163-Humans, pubmed-meshheading:15544163-Male, pubmed-meshheading:15544163-Mice, pubmed-meshheading:15544163-Molecular Chaperones, pubmed-meshheading:15544163-Molecular Sequence Data, pubmed-meshheading:15544163-RNA Interference, pubmed-meshheading:15544163-Shiga Toxins, pubmed-meshheading:15544163-Stress, Physiological, pubmed-meshheading:15544163-Thapsigargin, pubmed-meshheading:15544163-Transfection, pubmed-meshheading:15544163-Tunicamycin
pubmed:year
2004
pubmed:articleTitle
Localization and function in endoplasmic reticulum stress tolerance of ERdj3, a new member of Hsp40 family protein.
pubmed:affiliation
Department of Pathology, Sapporo Medical University School of Medicine, S-1, W-17, Chuo-ku, Sapporo 060-8556, Japan.
pubmed:publicationType
Journal Article