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Exploring The Role Played By Hsp90β Isoform In Chapering GR Signal Pathway

Posted on:2007-08-09Degree:DoctorType:Dissertation
Country:ChinaCandidate:Y W JiFull Text:PDF
GTID:1104360185488133Subject:Pharmacology
Abstract/Summary:PDF Full Text Request
Glucocorticoid receptors (GR) is very important signaling molecular that mediates wide biological and pharmalogical effects after its binding with Glucocoticoids. The eukaryotic Hsp90s are essential molecular chaperones with key roles in assembly of a range of co-chaperones typically involved in GR signal transduction. There are two major cytoplasmic isoforms of Hsp90,Hsp90α(Hsp86 in mice correspondingly) and Hsp90β(Hsp84 in mice correspondingly).The genes of these two isoforms locates in different chromosomes, and the sequence similarity of the isoforms from homosapiens or from mice is lower than that of the same isoform between homosapiens and mice. We propose Hsp90αandβplay different role in chaperoning GR signaling and Hsp90β,notα, is the isoform that matters in GR conformation maturation.Our laboratory has found that two strains of C57BL/6 and BALB/c mice have different endurance capacity and mortal rate in systemic blast injury and acute pancreatitis. We also found GR function of these two strains is discrepant in the aspects of GR translocating into nucleus and binding the chromatin. The Hsp84 mRNA of C57BL/6 mice has been sequenced by our...
Keywords/Search Tags:glucocorticoid receptor, Hsp90βisoform, RNAi, eukaryotic expression, SNP
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