HSP90B1

(redirected from GRP94)

HSP90B1

A gene on chromosome 12q24.2-q24.3 that encodes a molecular chaperone of the HSP 90 family which has ATPase activity and functions in the processing and transport of secreted proteins. HSP90B1 plays a role in endoplasmic reticulum associated degradation.
References in periodicals archive ?
The upstream sequences of horse BiP, GRP94, and homocysteine-responsive endoplasmic reticulum-resident ubiquitin-like domain member 1 protein (Herpud1) were retrieved to search the binding sites of XBP1.
The second asset is an antibody-interferon fusion molecule directed against GRP94, a target for which currently there are no existing approved therapies.
There, it binds to stress response elements of the ER to activate target genes, such as GRP94 and CHOP (9-11).
reported the upregulation of GRP94, CHOP (ER stress components) in myocardial depression of septic rats, and ER stress inhibition protected the myocardium [18].
Previous study has found HCV could upregulate ER proteins such as GRp78 and GRp94 in the liver [17].
Schmidt demonstrated that mutant A-1-AT ZZ forms interact with the Grp78, Grp94, and Grp170 chaperones, calnexin, and UGGT [8].
Based on these findings, the two proteins were designated glucose-regulated proteins (GRP78 and GRP94) in 1977, as their expression levels are regulated by glucose in medium.
The use of HSPs as tumor vaccines wasfirst reported by Srivastava et al ., who showed that HSPs, in particular GRP94, bind peptides that are immunogenic in vitro and in vivo .
Effect of laminarin on the expression of GRP78 and GRP94 in rat after unilateral ureteral obstruction.
Previous studies indicated that plasma of T1 diabetic subjects contains elevated concentrations of the heat shock protein (HSP) glucose-regulated protein94 (Grp94) [1, 2].
Decreased protein and mRNA expression of ER stress proteins GRP78 and GRP94 in HepG2 cells over-expressing CYP2E1.