HSPA9

(redirected from Mortalin)

HSPA9

A gene on chromosome 5q31.1 that encodes a member of the heat shock protein 70 (HSP70) family which localises to the mitochondria as well as the endoplasmic reticulum, plasma membrane and cytoplasmic vesicles. HSPA9 plays a role in cell proliferation, stress response and maintenance of mitochondria; it may play a role in controlling cell proliferation and ageing and act as a chaperone.
References in periodicals archive ?
Mortalin, a member of the heat shock protein 70 family, was first identified as a human mitochondrial heat shock protein, playing important roles in stress response and glucose regulation (22).
In general, apoptosis in IUGR neonates' small intestinal mucosa is increased [5, 22, 26]; that is why high mortalin expression in homogenized intestinal tissues crappings in IUGRs was expected.
Reinartz et al., "TP53 status regulates ACSL5-induced expression of mitochondrial mortalin in enterocytes and colorectal adenocarcinomas," Cell and Tissue Research, vol.
Furthermore, mutations in the mitochondrial Hsp70, HSPA9 (mortalin), were recently suggested to promote the development of PD [42-44]; however, other groups suggest mutations in HSPA9 are not a frequent cause of early-onset PD as they are also found in patient controls [45].
Chen et al., "Inhibition of mitochondrial permeability transition pore opening is involved in the protective effects of mortalin overexpression against beta-amyloid-induced apoptosis in SH-SY5Y cells," Neuroscience Research, vol.
On the brotherhood of the mitochondrial chaperones mortalin and heat shock protein 60.
Induction of mutant p53-dependent apoptosis in human hepatocellular carcinoma by targeting stress protein mortalin. Int J Cancer.
A proteomic approach showed that mtHsp70 or Mortalin interacts with DJ1--a protein involved in oxidative stress related to Parkinson's disease.
Patterns of p53, p73 and mortalin gene expression associated with hemocyte polyploidy in the soft-shell clam, Mya arenaria.
Presence of HSPA 9 in omental preadipocytes may protect them from apoptosis, because HSPA9 also called as mortalin and is known to have antiapoptotic role.
Osorio and co-workers used 2-D DIGE to identify four proteins that were differentially regulated by the human APOE genotype in targeted replacement (TR) mice.3 The proteins were subsequently identified by mass spectrometry (MALDI MS/MS) as isoforms of mortalin (a Mr 74,000 protein that belongs to the heat shock protein 70 [Hsp70] family of chaperone proteins), with significant differences in regulation and phosphorylation among the isoforms.