Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
2001-7-16
pubmed:abstractText
The present study was addressed on the effect of 3,3',4,4',5-pentachlorobiphenyl (PenCB) to the expression of molecular chaperon proteins, glucose regulated protein (GRP) 78, GRP94, calreticulin and calnexin in liver endoplasmic reticulum of rat by treatment with acute exposure. Male Wistar rats received PenCB in corn oil at once a dose of 10 mg/kg i.p., then at 5 days after treatment the microsomes were prepared. Free-fed and pair-fed control groups were given the vehicle. The microsomal proteins were separated on SDS-PAGE, transferred to membrane and blotted using antibody towards respective chaperone proteins. The protein levels of GRP78, GRP94, calreticulin and calnexin were significantly decreased with the acute exposure. In addition, albumin level in the microsomes was also significantly reduced by the PenCB treatment. The transferrin level was significantly higher than pair-fed but not from free-fed group. These chaperone proteins have important physiological functions against synthesized and/or denatured proteins, which include assembling, folding of proteins. PenCB-treatment may alter the extent of biosynthesis of secretory protein such as albumin through the decreasing levels of chaperone proteins in endoplasmic reticulum. Interestingly, reduced GRP78 protein level by PenCB was not due to decreased mRNA level. Our results suggested that a part of the toxicity of PenCB is associated to significant decrease of the chaperone proteins in the endoplasmic reticulum.
pubmed:language
jpn
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
http://linkedlifedata.com/resource/pubmed/chemical/3,4,5,3',4'-pentachlorobiphenyl, http://linkedlifedata.com/resource/pubmed/chemical/Calcium-Binding Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Calnexin, http://linkedlifedata.com/resource/pubmed/chemical/Calreticulin, http://linkedlifedata.com/resource/pubmed/chemical/Carrier Proteins, http://linkedlifedata.com/resource/pubmed/chemical/HSP70 Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Heat-Shock Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Molecular Chaperones, http://linkedlifedata.com/resource/pubmed/chemical/Polychlorinated Biphenyls, http://linkedlifedata.com/resource/pubmed/chemical/Ribonucleoproteins, http://linkedlifedata.com/resource/pubmed/chemical/glucose-regulated proteins, http://linkedlifedata.com/resource/pubmed/chemical/molecular chaperone GRP78
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0016-254X
pubmed:author
pubmed:issnType
Print
pubmed:volume
92
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
201-16
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
2001
pubmed:articleTitle
[Suppression of stress proteins, GRP78, GRP94, calreticulin and calnexin in liver endoplasmic reticulum of rat treated with a highly toxic coplanar PCB].
pubmed:affiliation
Graduate School of Pharmaceutical Sciences, Kyushu University, Fukuoka 812-8582.
pubmed:publicationType
Journal Article, English Abstract