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Validated All-in-One™ qPCR Primer for HSPD1(NM_199440.2) Search again
Product ID:
HQP155372
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
CPN60, GROEL, HLD4, HSP-60, HSP60, HSP65, HuCHA60, SPG13
Gene Description:
heat shock protein family D (Hsp60) member 1
Target Gene Accession:
NM_199440.2(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
This gene encodes a member of the chaperonin family. The encoded mitochondrial protein may function as a signaling molecule in the innate immune system. This protein is essential for the folding and assembly of newly imported proteins in the mitochondria. This gene is adjacent to a related family member and the region between the 2 genes functions as a bidirectional promoter. Two pseudogenes, both located on chromosome 8, have been associated with this gene. Two transcript variants encoding the same protein have been identified for this gene. Mutations associated with this gene cause autosomal recessive spastic paraplegia 13. [provided by RefSeq].
Gene References into function
- H9724, a monoclonal antibody to Borrelia burgdorferi's flagellin, binds within live neuroblastoma cells, a potential role in peptide hormone signaling in an autoimmune pathogenesis of the neuropathy of Lyme disease.
- promoter polymorphism of the IL-6 gene is associated with levels of antibodies to 60-kDa heat-shock proteins
- Hereditary spastic paraplegia SPG13 is associated with a mutation in the gene encoding the mitochondrial chaperonin Hsp60 (HSPD1)
- Gene expression of HSP1 was down-regulated during early apoptosis in human hepatoma cells exposed to Paeoniae Radix in vitro.
- A regulatory role for human HSP60 autoreactivity is demonstrated by DNA vaccine therapy of rat adjuvant arthritis that results in increased T cell proliferation and variable changes in cytokine production.
- HSP60 reactivity showed no apparent difference between normal and neoplastic odontogenic epithelium
- HLA-E can present a peptide derived from the signal sequence of human hsp60.
- The genome structure of this gene has been established.
- Deficiency of chaperonin 60 in Down's syndrome. A quantitative analysis by Western blots showed a marked reduction of Cpn60 per equal amount of total protein in DS cells to an average of 35% of normal.
- Maturation of murine bone marrow-derived dendritic cells is strongly induced by human HSP60 and paralleled by release of Th1-promoting cytokines.
- The recombinant protein does not induce the release of tumor necrosis factor alpha from murine macrophages
- the host factor, Hsp60, is essential for in vivo hepatitis B virus replication, and the mechanism of Hsp60 is probably through an activation of HBV pol by Hsp60
- Evidence of elevated anti-HSP60 reactivity in the serum of patients with tic disorder supports HSP60 as an autoantigen and implicates the involvement of autoimmunity in tic disorders.
- A regulatory HSP60 peptide specifically recognized by the T cells of DNA-vaccinated rats is successfully used as an effective vaccine to inhibit the development of adjuvant arthritis in rats.
- Chlamydial heat shock protein 60-1 antibodies are associated with an increased cervical cancer risk suggests that persistent Chlamydia trachomatis infection may contribute to cervical neoplasia.
- A novel association between anti-heat shock protein 65 autoantibodies and occurrence of postoperative atrial fibrillation.
- The perioperative kinetics of HSP60 in serum may result from suppressed protein synthesis caused by a reduced energy charge of hepatocytes during early reperfusion in liver transplantation.
- T cell immunity to Hsp70 and Hsp90, like Hsp60-specific immunity, can modulate arthritogenic response in adjuvant arthritis. Regulatory mechanisms induced by Hsp60, Hsp70, and Hsp90 are reinforced by an immune network that connects their reactivities.
- Hsp10 exerts anti-inflammatory activity by inhibiting Toll-like receptor signaling possibly by interacting with extracellular Hsp60
- The HSP60 is a mitochondrial chaperonin, highly preserved during evolution, responsible of protein folding. Its function is strictly dependent on HSP10 in both prokaryotic and eukaryotic elements.
- A defined region of HSP60 (amino acids 354-365) is involved in lipopolysaccharide (LPS) binding, thereby implicating a physiological role of human HSP60 as an LPS-binding protein.
- a decrease of Hsp60 in the cytoplasmic fraction of dilated cardiomyopathy-affected left ventricles was observed; at the same time an increase in P450 2E1 expression in dilated hearts' cytoplasmic fractions was observed
- Overall, we found clear evidence for the occurrence of HSP60 on the surface of stressed HUVECs in a very similar patchy distribution pattern in living and fixed cells
- Atherosclerotic plaques harbor in vivo-activated CD4+ T cells that recognize the human 60-kDa HSP and become target for both autoreactive T cells and cross-reactive T cells to Chlamydia pneumoniae 60-kDa HSP via a mechanism of molecular mimicry.
- Mortalin and HSP60 interact both in vivo and in vitro, and that the N-terminal region of mortalin is involved in these interactions.
- Autoantibodies recognizing amino acid residues 288 to 366 of HSP60 induce atherosclerosis via the mechanisms of autoimmune reactions to HSP60 expressed on arterial endothelial cells, which can be prevented by F(ab)2 segments derived from these antibodies
- human HSP60 induced naive mouse B cells to proliferate and to secrete IL-10 and IL-6 and up-regulate their expression of MHC class II and accessory molecules
- The 14-3-3 protein forms molecular complex with Hsp60 and PrPC in human CNS under physiological conditions, and this complex might become disintegrated in pathologic process of prion diseases.
- HSP60 and HSP10 are expressed in large bowel carcinomas with lymph node metastases
- Our study provides the first prospective data confirming an association between high levels of sHSP60 and early carotid atherosclerosis.
- Hsp60 is an important target for anti-endothelial antibodies; such an interaction contributes to pathogenic effects, especially in vasculitis-associated systemic autoimmune disease
- With HSP60, results from cell-lines correlated with clinical results, indicating that this model can be used for dissection of mechanisms involved in transformation to androgen resistance and assignment of protein markers in prostate cancer.
- Results suggest that heat shock protein 60, a self-molecule, can downregulate adaptive immune responses by upregulating regulatory t cells innately through Toll-like receptor 2 signaling.
- HSP60 is a potent inducer of venous smooth muscle cell (VSMC) proliferation; HSP60 uses TLR2 as well as TLR4 to cause its mitogenic effect on VSMCs
- Mitochondrial heat shock protein 60 is able to neutralize the inhibition of electron transport complex IV by amyloid beta-protein.
- Investigation of single-nucleotide variations in the Hsp60 gene and their disease-causing potential.
- Yersinia Hsp60-specific T cells of one patient cross-reacted directly with human Hsp60
- dysregulated expression of DHX32 might lead to as of yet unknown changes in mitochondrial homeostasis manifested by cytoplasmic redistribution of the molecular chaperon Hsp60
- A negative association between Hsp60 in plasma, and seropositivity for three microbial agents which are risk factors for cardiovascular disease, suggest a protective effect of circulating stress protein Hsp60.
- Plasminogen bound to hsps 27, 60, and 70 and Angiostatin predominantly bound to hsp 27 and to hsp 70 in a concentration- and kringle-dependent manner.
- found that the function of the p.Gln461Glu heat shock protein 60 was mildly compromised. The c.1381C > G mutation likely represents a novel low-penetrance HSP allele.
- HSP60 and HSP70 released upon tissue damage might play a role in the regulation of bacteria-induced inflammation
- Extracellular Hsp60 levels are significantly elevated in children with septic shock compared with both healthy controls and critically ill children without sepsis. Extracellular Hsp60 may play a role in the pathogenesis of sepsis in children.
- HSP60 was present in the uterus and oviduct epithelial cells and was shown to bind to human spermatozoa. Hsp60 partially prevented the increase in p81 phosphotyrosine content induced by the phosphodiesterase inhibitor 3-isobutyl-1-methylxanthine.
- Abnormal trafficking of HSP60 to the cell surface may be an early trigger for myocyte loss and the progression of heart failure.
- Results indicate that miR-1 and miR-133 are involved in regulating cell fate, and that post-transcriptional repression of HSP60 and HSP70 by miR-1 and of caspase-9 by miR-133 contributes significantly to their opposing actions.
- Cytosolic accumulation of HSP60 during apoptosis with or without apparent mitochondrial release: evidence that its pro-apoptotic or pro-survival functions involve differential interactions with caspase 3.
- Hsp60 and Hsp72 activation and inflammatory markers were correlated with the extent of cardiac and microvascular dysfunction in patients with angiographycally normal coronary arteries.
- Three single nucleotide polymorphisms (SNPs) were studied in 100 RA trio families. Genetic analyses were performed by comparing allelic frequencies, applying the transmission disequilibrium test, and assessing the genotype relative risk.
- The extended range of plasma Hsp60 concentrations in the general population is genuine and is likely to be related to genetic, biological, and psychosocial risk factors for coronary artery disease.
- human (self) Hsp60 is a disease-relevant autoantigen in juvenile dermatomyositis
- Intracellular chaperone heat-shock protein 60 (HSP60) induces extensive axonal loss and neuronal death in microglial cultures from wild-type (but not TLR4 loss-of-function mutant) mice.
- a strong association between in vitro resistance to platinum compounds and increased HSP60 mRNA expression
- Hsp60 is a key player in the resistance mechanism against oxidative stress and aging
- Co-expression of Hsp60-(p.V98I) and wild-type Hsp60 exerted a dominant negative effect only when the chaperonin genes were expressed at relatively low levels.
- HSP60 is a rare cause of hereditary spastic paraparesis, but may act as a genetic modifier.
- Mitochondrial HSP60 chaperonopathy causes an autosomal-recessive neurodegenerative disorder linked to brain hypomyelination and leukodystrophy.
- HSP60 exerted a protective role in digoxin-induced apoptosis through inhibition of caspase-3 activity in HUVEC.
- mitochondrial ribosomal protein S12 3'-UTR interacts specifically with TRAP1 (tumor necrosis factor receptor-associated protein1), hnRNPM4 (heterogeneous nuclear ribonucleoprotein M4), Hsp70 and Hsp60 (heat shock proteins 70 and 60), and alpha-tubulin
- The GroEL-GroES chamber behaves as a passive "Anfinsen cage" whose primary role is to prevent multimolecular association during folding.
- HSP60 is a potent activator of vascular endothelial cells and smooth muscle cells. It is possible that long-term stimulation of these cell populations by blood-borne HSP60 acts to drive blood vessel changes resulting in decreased arterial elasticity.
- These results indicate that c-MYC may promote transformation through the induction of HSP60 expression.
- A strong positive relationship is identified between circulating levels of heat shock protein 60 and the risk of coronary heart disease.
- Although oxidative stress may induce early apoptosis in NCI-H292 cells, Hsp60 exerts an anti-apoptotic effect in these cells.
- This protein has been found differentially expressed in the dorsolateral prefrontal cortex from patients with schizophrenia.
- HSP27 and HSP60 are predictors of biochemical recurrence of prostate cancer after radical prostatectomy.