HSP70_1
- Known as:
- HSP70_1
- Catalog number:
- 000063A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- HSP70_1
Related products to: HSP70_1
Related articles to: HSP70_1
- The human HSP70 family is a type of heat shock protein (HSP), consisting of 13 members encoded by the HSPA genes. HSPs play important roles in regulating cellular responses and functions during carcinogenesis, but their relationship with colon cancer is unclear. In our study, we found that the expressions of HSPA1B, HSPA4, HSPA5, HSPA6, HSPA8, HSPA9, HSPA13, and HSPA14 were significantly increased, while those of HSPA1A, HSPA2, HSPA7, and HSPA12B were significantly decreased in colon cancer tissues. The expression of HSPA gene family members was associated with some clinicopathological characteristics, including age, gender, TNM stage, pathological stage, and CEA level. Furthermore, the Kaplan-Meier method and Cox regression analysis showed that high HSPA1A, HSPA1B, and HSPA7 expressions were related to unfavorable survival, and high HSPA9 was associated with favorable survival. The relationships between HSPA1A and HSPA9 expression and survival were validated in the GEO dataset, and the HSPA1A and HSPA9 protein expression differences between colon cancer tissues and normal tissues were validated in the UALCAN database. Methylation of HSPA1A and HSPA9 was also analyzed, and it was found that the methylation of the HSPA1A promoter was significantly increased, and the methylation of the HSPA9 promoter was significantly decreased in colon cancer tissues. Increasing the methylation level of the HSPA1A gene and decreasing the methylation level of HSPA9 were related to favorable prognosis. The expression difference of HSPA1A/HSPA1B/HSPA7/HSPA9 was verified in colon cancer cell lines and colonic epithelial cells. Gene ontology analysis was used to screen signal pathways related to HSPA1A-, HSPA1B-, HSPA7-, and HSPA9- high phenotype. In summary, the increased expressions of HSPA1A1, HSPA1B, and HSPA7 were associated with poor prognosis, while that of HSPA9 was related to favorable prognosis for colon cancer patients. - Source: PubMed
Publication date: 2021/10/26
Guan YufengZhu XianjunLiang JunjieWei MinHuang ShanPan Xiaofen - The HSP70 family of heat shock protein plays a critical role in protein synthesis and transport to maintain protein homeostasis. Several studies have indicated that HSP70s are related to the development and occurrence of various cancers. - Source: PubMed
Publication date: 2021/05/31
Wang BenLan TianXiao HanChen Zhong-HuoWei ChaoChen Lei-FengGuan Jia-FuYuan Rong-FaYu XinHu Zhi-GangWu Hua-JunDai ZhiWang Kai - Transcriptional enhancer factor domain family member 4 (TEAD4) is a downstream effector of the conserved Hippo signaling pathway, regulating the expression of genes involved in cell proliferation and differentiation. It is up-regulated in several cancer types and is associated with metastasis and poor prognosis. However, its role in hepatocellular carcinoma (HCC) remains largely unexplored. Using data from The Cancer Genome Atlas, we found that TEAD4 was overexpressed in HCC and was associated with aggressive HCC features and worse outcome. Overexpression of TEAD4 significantly increased proliferation and migration rates in HCC cells as well as tumor growth . Additionally, RNA sequencing analysis of -overexpressing HCC cells demonstrated that overexpression was associated with the up-regulation of genes involved in epithelial-to-mesenchymal transition, proliferation, and protein-folding pathways. Among the most up-regulated genes following overexpression were the 70-kDa heat shock protein (HSP70) family members and A. Chromatin immunoprecipitation-quantitative real-time polymerase chain reaction experiments demonstrated that TEAD4 regulates and expression by directly binding to their promoter and enhancer regions. The pharmacologic inhibition of HSP70 expression in -overexpressing cells reduced the effect of TEAD4 on cell proliferation. Finally, by overexpressing in yes-associated protein ()/transcriptional coactivator with PDZ binding motif ()-knockdown HCC cells, we showed that the effect of TEAD4 on cell proliferation and its regulation of HSP70 expression does not require YAP and TAZ, the main effectors of the Hippo signaling pathway. A novel Hippo-independent mechanism for TEAD4 promotes cell proliferation and tumor growth in HCC by directly regulating HSP70 family members. - Source: PubMed
Publication date: 2021/01/20
Coto-Llerena MaireneTosti NadiaTaha-Mehlitz StephanieKancherla VenkateshParadiso ViolaGallon JohnBianco GaiaGarofoli AndreaGhosh SouvikTang FengyuanErcan CanerChristofori Gerhard MMatter Matthias SDroeser Raoul AZavolan MihaelaSoysal Savas Dvon Flüe MarkusKollmar OttoTerracciano Luigi MNg Charlotte K YPiscuoglio Salvatore - Out of the total forty four members of Plasmodium falciparum Hsp40 protein family, nineteen of them possess a PEXEL motif, and are predicted to be exported into the cytosol of an infected RBC. It is speculated that the human Hsp70 (hHsp70), which resides into the cytosol of the host erythrocyte, along with the exported PfHsp40s assists in the folding of parasitic proteins, thus playing a crucial role in the establishment of virulence. However, till date no experimental evidence supports this hypothesis. Our work establishes that the PEXEL motifs containing Type II PfDNAJ proteins specifically interact with hHsp70 (HSPA1A). It suggests that there exists a specific factor in PfDNAJ that determines the choice of cognate Hsp70. This opens up an interesting avenue of malaria research. - Source: PubMed
Publication date: 2017/03/18
Jha PayalLaskar ShyamasreeDubey SwatiBhattacharyya Mrinal KBhattacharyya Sunanda - Heat shock proteins 70 (HSP70s) are molecular chaperones that aid in protection against environmental stress. In this study, we cloned and characterized five members of the HSP70 family (designated as HSPa1a, HSC70-1, HSC70-2, HSPa4 and HSPa14) from Lateolabrax maculatus using rapid amplification cDNA ends (RACE). Multiple sequence alignment and structural analysis revealed that all members of the HSP70 family had a conserved domain architecture, with some distinguishing features unique to each HSP70. Quantitative real-time (qPCR) analysis revealed that all members of the HSP70 family were ubiquitously and differentially expressed in all major types of tissues, including testicular tissue. This indicated that HSP70s have vital and conserved biological functions, and may also function in the development of germinal cells. The expression of mRNA of the five HSP70 family members mRNA expression was significantly increased in the head kidney, intestine and gill after Vibrio harveyi challenge, suggesting that HSP70s play an important role in the immune response. - Source: PubMed
Publication date: 2016/11/28
Han Ying-LiHou Cong-CongDu ChenZhu Jun-Quan