Ask about this productRelated genes to: HSPA6 antibody
- Gene:
- HSPA6 NIH gene
- Name:
- heat shock protein family A (Hsp70) member 6
- Previous symbol:
- -
- Synonyms:
- HSP70B'
- Chromosome:
- 1q23.3
- Locus Type:
- gene with protein product
- Date approved:
- 1991-07-26
- Date modifiied:
- 2015-11-19
Related products to: HSPA6 antibody
Related articles to: HSPA6 antibody
- The small-molecule pyridazinone derivative IMB5036 (IMB) exhibits significant cytotoxicity against multiple cancer cell lines, and KH-type splicing regulatory protein (KSRP) is confirmed as its direct binding partner. However, KSRP's functional role in neuroblastoma (NB) and the mechanism mediating IMB's antitumor effects remain unclear. This study analyzed public tumor databases and found KSRP expression negatively correlates with NB patients' median survival. Experiments showed IMB induces NB cell pyroptosis, immunogenic cell death (ICD, with calreticulin exposure), and cGAS-STING activation (to boost antitumor immunity), while CRISPR-Cas9-mediated KSRP knockout notably attenuates these effects. Transcriptome sequencing further confirmed KSRP mediates IMB's regulation of HSPA6/RSAD2. This study clarifies KSRP-dependent ICD drives NB antitumor immunity, providing a basis for KSRP-targeted NB immunotherapies. - Source: PubMed
Publication date: 2026/05/26
Dong YanqunXu YanfengZhang JunyiHong HanyuGao LingliWei HanruiZheng YijiaLv XingZheng Yan-BoYang JigangGong Jian-Hua - The mechanisms underlying gastric cancer (GC) progression, including recurrence and metastasis, remain unclear. Studies have reported that microRNAs and Men1 are closely associated with multiple tumors, including GC. Therefore, assessing the impact of Men1 on GC and investigating the underlying mechanisms are essential. - Source: PubMed
Publication date: 2026/05/06
Jiang Jin-XunZhang Shi-JieZhao KunZheng Kai-TianWang Shan-HuChen Tian-deWang Zhen - Given the lack of effective targeted therapeutic options for triple-negative breast cancer (TNBC), there is an imperative demand for innovative treatment approaches, with ferroptosis standing out as a promising direction. This study identifies HSPA6 as a key ferroptosis sensitizer in TNBC. Mechanistically, HSPA6 binds to NF-κB p65, inhibits its nuclear translocation and Ser468 phosphorylation, thereby suppressing transcription of the lipogenic enzyme FASN and downregulating phospholipid-remodeling enzymes LPCAT1/cPLA2. This dual inhibition enriches membrane phospholipids with polyunsaturated fatty acids, heightening peroxidation susceptibility and triggering ferroptosis. Concurrently, HSPA6-mediated suppression of lipogenesis depletes palmitate, thereby attenuating ANKIB1 palmitoylation and inhibiting its E3 ligase activity. This impairs K48-linked ubiquitination and degradation of HSPA6, forming a stabilizing positive feedback loop. Our study uncovers a HSPA6-p65-FASN-ANKIB1 axis linking lipid metabolism to ferroptosis, offering a novel TNBC therapeutic target. - Source: PubMed
Publication date: 2026/04/08
Hai Lin-YueYu Zhi-HaoLiu Wen-BoZhang Yuan-YuanXu YueCheng ShanYue Hao-RanGuo Zhang-YinYan Shi-JieSun RuiLiu Xiao-FengLiu Bo-WenWang XinCao Xu-ChenYu Yue - The heat shock protein 70 (Hsp70) family is essential for maintaining protein homeostasis and mediating responses to environmental stresses; however, comprehensive characterizations of this family in the mandarin fish (Siniperca chuatsi) are presently absent. Through comparative genomic analysis, a total of 178 Hsp70 genes were identified across nine vertebrate species (human, mouse, and seven teleost fishes), including 17 unique members within the mandarin fish genome. Phylogenetic and gene structure analyses demonstrated that the mandarin fish Hsp70 family has remained highly conserved throughout teleost evolution, marked by lineage-specific expansions (notably in hspa1, hspa4, hspa8, and hspa12) and selective gene loss (e.g., the absence of hspa2 and hspa6). Specifically, tandem duplication was observed for hspa8.1 and hspa8.2, at the same time, two pairs of syntenic genes (hspa4a/hspa4b and hyou1/hspa8b) were found. Ka/Ks analysis further indicated that this gene family has mainly evolved under purifying selection. Transcriptomic profiling showed that hspa8.1 was constantly expressed across all examined tissues. In addition, under thermal stress and Aeromonas hydrophila infection, Hsp70 genes in mandarin fish exhibited divergent expression patterns: certain members contribute to basal homeostasis (e.g., hspa8.1), whereas others demonstrate specialized responses to heat/cold adaptation (e.g., hspa5) or pathogen infection (e.g., hspa1l). Respectively, these findings together provide a thorough understanding of the composition, evolutionary trajectory, and stress-responsive dynamics of the Hsp70 family, establishing a foundational molecular basis for understanding the environmental adaptation of mandarin fish. - Source: PubMed
Publication date: 2026/04/21
Liu YufeiYao XiaoliGao JinhuaIsmaeel HossamChen XiaowuZhao Jinliang - Glioblastoma multiforme is an aggressive and therapy-resistant tumor, necessitating the identification of novel therapeutic targets. Here, we investigated the role of transient receptor potential vanilloid 1 (TRPV1) in mediating capsaicin-induced changes in cell viability in U87 glioblastoma cells. Wild-type cells tolerated capsaicin concentrations up to 175 μM, whereas TRPV1 knockout (TRPV1KO) cells exhibited reduced viability at 164 μM, indicating a cytoprotective function of TRPV1. Transcriptomic analyses revealed that wild-type cells activated the MAPK-MSTRG.66879-MYC-HSF1-axis, resulting in robust induction of heat shock proteins (HSPA1B, HSPA6, HSP90AA1) and dual-specificity phosphatases (DUSP1, DUSP8, DUSP10), which collectively maintained protein homeostasis and mitigated cellular damage. In contrast, TRPV1KO cells displayed impaired calcium-mediated MAPK activation, leading to altered mitochondrial oxidative phosphorylation, significant changes in electron transport chain (ETC I, II, III, IV), and enhanced intrinsic apoptosis through HRK. Notably, two long non-coding RNAs, MSTRG.56099 and MSTRG.66879, were identified as potential cis-regulators of DUSP1 and MYC, respectively. MSTRG.66879, upregulated in wild-type cells, appeared to form a TRPV1-associated regulatory axis with MYC and miR-182, promoting cell survival under capsaicin exposure. Disruption of this network in TRPV1KO cells sensitized them to capsaicin-induced apoptosis. Collectively, TRPV1 orchestrates calcium influx, MAPK signaling, heat shock protein induction, and noncoding RNA-mediated regulation to facilitate glioblastoma cell adaptation, suggesting that targeting TRPV1 and the MSTRG.66879-MYC axis may offer new therapeutic avenues and biomarkers for glioblastoma management. - Source: PubMed
Publication date: 2026/04/10
Chinreddy Subramanyam ReddyMashozhera Nicole TendayiLee GwonjinZaman IqraaPatel VaibhaviHarris Robert THankins Gerald RReddy Umesh K