Heat Shock 105kDa/110kDa Protein 1 Proteins (HSPH1)

Xenopus laevis Heat Shock 105kDa/110kDa Protein 1 (HSPH1) interaction partners

1. These studies demonstrate that Xenopus hsp110 gene expression is constitutive and stress inducible in cultured cells and developmentally- and tissue specifically-regulated during early embryogenesis[hsp110]

Human Heat Shock 105kDa/110kDa Protein 1 (HSPH1) interaction partners

1. High HSP110 is associated with B-cell diffuse large B-cell lymphoma through regulating NF-kappaB signaling and MyD88 stabilization.

2. HSP110 through its interaction with the Ku70/80 heterodimer may participate in DNA repair.

3. expression not an independent prognostic factor in gastric cancer patients with peritoneal metastasis, but might be a new marker of chemosensitivity

4. Established heat shock protein 110 (HSP110) as a prognostic biomarker of colorectal carcinomas (CRCs) with microsatellite instability-high (MSI-H) by considering the intratumoral heterogeneity of HSP110 expression. The HSP110wt-low MSI-H CRCs were significantly correlated with larger deletions in the HSP110 T17 mononucleotide repeat (>/=4 bp; p < 0.001).

5. HSP110 HT17 alone correctly classified samples judged to be uncertain with the pentaplex panel.

6. deletion of the HSP110 T17 repeat was frequently observed in microsatellite-unstable advanced gastric cancers.

7. Hsp105alpha localizes to the nucleus, interacts with HIF-1alpha and induces HIF-1a accumulation in CoCl2-treated cells.

8. the expression of HSP110 in colon cancer contributes to STAT3-dependent tumor growth

9. About 25% of patients with stages II-III colorectal tumors with microsatellite instability have an excellent response to chemotherapy, due to large, biallelic deletions in the T(17) intron repeat of HSP110 in tumor DNA.

10. HSP105 depletion disrupts the integration of protein phosphatase 2A into the beta-catenin degradation complex, favoring the hyperphosphorylation and degradation of beta-catenin.

11. A receiver operating characteristic curve constructed with HSP105 and TIM gave a sensitivity of 54.3% and 95% (38/40) specificity in discriminating esophageal squamous cell carcinoma from matched controls.

12. we measured the binding of human Hsp72 (HSPA1A) to BAG1, BAG2, BAG3, and the unrelated NEF Hsp105. These studies revealed a clear hierarchy of affinities: BAG3 > BAG1 > Hsp105 >> BAG2.

13. HSPH1 and HSPH2 are bona fide chaperones on their own that collaborate with DNAJA1 and DNAJB1 to hydrolyze ATP and unfold polypeptides and HSPA1A and HSPH1 formed a powerful molecular machinery.

14. High HSP105 expression is associated with Barrett's esophagus.

15. It restricts aggregation of denaturated proteins,plays a role in protein folding in cytoplasms,and enhance expression of hsp70 in cell nucleus.(review)

16. The Hsp105-mediated multilevel regulation of DeltaF508 CFTR folding and quality control provides new opportunities to understand how chaperone machinery regulates the homeostasis and functional expression of misfolded proteins in the cell.

17. A direct correlation between HSP105 expression and lymphoma aggressiveness was also apparent.

18. Hsp105alpha and Hsp105beta suppressed the expanded polyQ tract-induced protein aggregation and apoptosis through the induction of Hsp70.

19. Heat shock protein 105 is overexpressed in a variety of human tumors

20. HSP105 appears to chaperone the responses to endoplasmic reticulum (ER) stress through its interactions with GRP78 and GSK3, and without HSP105 cell death following ER stress proceeds by a non-caspase-3-dependent process.

Mouse (Murine) Heat Shock 105kDa/110kDa Protein 1 (HSPH1) interaction partners

1. These observations suggest that GGA administration is a therapeutic candidate for depressive diseases by increasing hippocampal BDNF levels via HSP105 expression.

2. Hsp105 may play an important role in the refolding of denatured proteins and protection against stress-induced cell death in mammalian cells.

3. Hsp110 over-expression increases the immunogenicity of the murine CT26 colon tumor.

4. Data suggest that Hsp105 has opposite effects on stress-induced apoptosis depending on the cell type; a pro-apoptotic effect in embryonal cells and an anti-apoptotic effect in neuronal cells.

5. enhances activation of p38, release of cytochrome c and caspase activation; may play important roles in organogenesis, during which marked apoptosis occurs, by enhancing apoptosis during mouse embryogenesis

6. Hsp105alpha is suggested to regulate the substrate binding cycle of Hsp70/Hsc70 by inhibiting the ATPase activity of Hsp70/Hsc70, thereby functioning as a negative regulator of the Hsp70/Hsc70 chaperone system.

7. The constitutive overexpression of HSP105 in cancer cells is involved in malignant transformation by protecting tumor cells from apoptosis.

8. it is suggested that Hsp105 suppresses the stress-induced apoptosis at its initial step, the translocation of Bax to mitochondria

9. HSP105 appears to chaperone the responses to endoplasmic reticulum (ER) stress through its interactions with GRP78 and GSK3, and without HSP105 cell death following ER stress proceeds by a non-caspase-3-dependent process.

10. hsp110/105 KO mice are resistant to ischemic injury and that the protective effects of hsp110/105 deficiency in cerebral ischemia may partly be mediated by an increase in the chaperone activity of Hsp70.