HSPB8 Antibody

1. results strongly suggest that HSP22 represses HCC progression, especially HCC cell migration, by the down-regulation of the PI3K/AKT signaling pathway. PMID: 28456666
2. Data indicated that the HSPB8 expression level was strongly positively correlated with MAPK signaling pathway and CREB pathway and worse prognosis. The methylation level of its DNA was negatively associated with its expression and positively associated with overall survival. These results suggest that HSPB8 could promote the proliferation and inhibit the apoptosis of GC cells by activating ERKCREB signaling. PMID: 29693129
3. HSPB2 competes with HSPB8 for binding to BAG3. In contrast, HSPB3 negatively regulates HSPB2 association with BAG3. PMID: 28181153
4. Silencing of HSPB8 markedly decreased the mitotic levels of BAG3 in HeLa cells, supporting its crucial role in BAG3 mitotic functions. The results support a role for the HSPB8-BAG3 chaperone complex in quality control of actin-based structure dynamics that are put under high tension, notably during cell cytokinesis. PMID: 28275944
5. HSPB8 is involved in regulating the cell cycle and cell migration in MCF-7 cells. PMID: 28060751
6. suggest that HSPB8 may act as an intracellular factor against hepatitis C virus replication and that DNAJC5B has the same function, with more relevant results for genotype 3 PMID: 29182667
7. It has been demonstrated that HSPB8-BAG3-HSP70 ensures the functionality of stress granules and restores proteostasis by targeting defective ribosomal products for degradation. PMID: 27570075
8. HSPB8 counteracts accumulation of aberrantly localized misfolded forms of TDP-43 and its 25 KDa fragment involved in most sporadic cases of Amyotrophic Lateral Sclerosis and of Fronto Lateral Temporal Dementia. PMID: 26961006
9. expands the understanding of disease mechanisms, tissue involvement, and phenotypic outcome of HSPB8 mutations PMID: 26718575
10. our findings suggest the existence of a so-far unrecognized quality control mechanism involving BAG3, HSPB8 and p62/SQSTM1 for accurate remodelling of actin-based mitotic structures that guide spindle orientation. PMID: 26496431
11. This study demonstreated that expression of HSPB8 was restricted to GFAP+ astrocytes in patient with multiple sclerosis. PMID: 26694816
12. Pangenomic profiling of velcade-sensitive and resistant cells showed that the small heat shock protein HSPB8 was overexpressed in multiple myeloma resistant cells. PMID: 25051369
13. HSP22 acts as a positive regulator in TGF-alpha-induced migration of ovarian cancer cells, subsequently directing ovarian cancer toward progression. PMID: 25731856
14. HSP22 plays an important role on gastric tumor aggressiveness and prognosis and may act as a promising target for prognostic prediction. PMID: 24804817
15. Mutant HSPB8 causes protein aggregates and a reduced mitochondrial membrane potential in dermal fibroblasts from distal hereditary motor neuropathy patients. PMID: 22595202
16. The expression of HspB8 inhibits the growth of genetically diverse melanoma cells that include caspase-1 activation outside of the realm of the inflammasome, mTORC1-dependent Beclin-1 upregulation and its cleavage by the activated caspase-1. PMID: 22898869
17. findings show that during heat shock recovery NF-kappaB activates selective removal of misfolded or aggregated proteins by controlling expression of BAG3 and HSPB8 and by modulating the level of the BAG3-HspB8 complex PMID: 22302993
18. we observed upregulation of HSPB8 and BAG3 selectively in astrocytes located within the degenerated areas of patients with protein aggregation diseases PMID: 21696420
19. We studied the HSPB1 and HSPB8 mutation occurrence in patients with distal hereditary motor neuropathy and those with the axonal form of Charcot-Marie-Tooth disease type 2 PMID: 22176143
20. present study demonstrates that HSPB8 is silenced by DNA methylation in hematopoietic malignant and normal cells PMID: 21914495
21. The results of this syudy suggested that defects in HspB8-mediated autophagy are likely to contribute to dHMNII pathology and their detection in peripheral blood mononuclear cells could be a useful, accessible biomarker for the disease. PMID: 21985219
22. HSPB8 may play an important role in the protection of cells under lethal heat shock treatment, and the K141N mutation can impair the protective effect. PMID: 21983727
23. phosphorylation of HspB8 by ERK1 might be important for regulation of interaction of HspB8 with different target proteins PMID: 21526341
24. Overexpression of HSPB1, as well as HSPB6, HSPB7 and HSPB8 independently protect against tachycardia remodeling by attenuation of the RhoA GTPase pathway at different levels. PMID: 21731611
25. The complexes formed by Bag3 and HspB8 might have variable stoichiometry and can participate in different processes including clearing of the cell from improperly folded proteins. PMID: 21767525
26. Drosophila HSP67Bc is the functional ortholog of human HSPB8 and Dm-HSP67Bc induces autophagy via the eIF2alpha pathway. PMID: 20858900
27. HspB8 increases misfolded SOD1 clearance via autophagy. PMID: 20570967
28. Data show that the interaction between HspB6 and Bag3 requires the same regions that are involved in the HspB8-Bag3 association. PMID: 19845507
29. The results confirm predictions that Hsp22 belongs to the family of intrinsically disordered proteins with certain parts of its molecule retaining folded structure and undergoing reversible thermal unfolding. PMID: 19783089
30. Forced H11 expression triggers apoptosis. PMID: 12832417
31. In two pedigrees with distal hereditary motor neuropathy type II linked to chromosome 12q24.3, we identified the same mutation (K141N) in small heat-shock 22-kDa protein 8 (encoded by HSPB8; also called HSP22). PMID: 15122253
32. Hsp22 is highly homologous to small heat shock proteins and effectively prevents aggregation of denatured protein both in vitro and in vivo. It is supposed that chaperone-like activity is of great importance for Hsp22 functioning PMID: 15541337
33. Reduced chaperone activity of mutated HspB8 is associated with neuromuscular disorders PMID: 15879436
34. The rate of HSP22 gene mutation in Chinese patients with Charcot-Marie-Tooth disease is as low as 0.87%(1/115). PMID: 16086267
35. Our results suggest that a variety of oligomers composed of different proportions of different sHSPs may form in cell types expressing multiple sHSPs. PMID: 16225851
36. HspB8 might play important role in regulating Abeta aggregation and, therefore, development of classic senile plaques in Alzheimer's disease and cerebral amyloid angiopathy in hereditary cerebral hemorrhage with amyloidosis of Dutch type. PMID: 16485107
37. Small heat shock protein B8 (HSP22) is a novel TLR4 agonist abundantly expressed in synovial tissue from patients with rheumatoid arthritis. PMID: 16709864
38. found aberrantly increased interactions of neuropathy-associated mutant HSP22 forms with themselves, with wild-type HSP22, and with the other sHSPs, alphaB-crystallin, and HSP27. PMID: 16935933
39. Aberrant DNA methylation silences the novel heat shock protein H11 in melanoma PMID: 17033167
40. HspB8 overload causes melanoma growth arrest and apoptosis through TAK1 activation PMID: 17173073
41. Displays chaperone activity, autokinase activity, and trigger or block apoptosis activity. Decrease may contribute to development of some neurologic diseases and others. (Review) PMID: 17304582
42. HSP22 seems to play an important role in the nervous system. PMID: 17722063
43. Effect of mutations in the beta5-beta7 loop on the structure and properties of human small heat shock protein HSP22 PMID: 17922839
44. These results suggested that the HspB8-Bag3 complex might stimulate the degradation of Htt43Q by macroautophagy. PMID: 18006506
45. HSPB8 is a candidate CDK-independent cyclin D1 target that can mediate its effects PMID: 18006821
46. HspB8 and Bag3: a new chaperone complex targeting misfolded proteins to macroautophagy. PMID: 18094623
47. Hsp22 induction represents a new aspect of the estrogenic response with potential significance for the biology of estrogen receptor-positive breast cancer cells. PMID: 18229450
48. Mutations in serine residues of HSP22 which are phosphorylated by cAMP-dependent protein kinase were accompanied by decrease of chaperone-like activity. PMID: 18298377
49. Activation of the bone morphogenetic protein receptors Alk3 and Bmpr2 by H11kinase/Hsp22 promotes cardiac cell growth and survival. PMID: 19246680
50. H11 kinase is a novel mediator of myocardial hypertrophy in vivo PMID: 12456486

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HGNC: 30171

OMIM: 158590

KEGG: hsa:26353

STRING: 9606.ENSP00000281938

UniGene: Hs.400095