Ask about this productRelated genes to: HSPA8 antibody
- Gene:
- HSPA8 NIH gene
- Name:
- heat shock protein family A (Hsp70) member 8
- Previous symbol:
- HSPA10
- Synonyms:
- HSC71, HSC70, HSP73
- Chromosome:
- 11q24.1
- Locus Type:
- gene with protein product
- Date approved:
- 1995-05-08
- Date modifiied:
- 2015-11-19
Related products to: HSPA8 antibody
Related articles to: HSPA8 antibody
- 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 - Type 1 diabetes mellitus (T1DM) compromises the mechanical adaptive capacity of bones, posing challenges in orthodontic treatment and increases periodontal complication risks. Mechanical loading is the main inducer of craniofacial bone adaptation; however, the early proteomic responses of the maxillary bone to stress under diabetic conditions remain unexplored. Therefore, we aimed to characterize the early proteomic signatures of the maxillary bone in T1DM rats subjected to controlled mechanical stress and identify potentially relevant molecular pathways for orthodontic treatment in patients with diabetes. - Source: PubMed
Publication date: 2026/04/06
Tobias-López Luis FernandoTrejo-Iriarte Cynthia GeorginaGarcía-Muñoz AlejandroGómez-Clavel José Francisco - Skeletal muscle is a fundamental tissue as it is found throughout the body, sustains posture, and produces movement. Yet, skeletal muscle disorders, such as myopathies, affect a large percentage of the population, degrading an individual's quality of life. A recent study links myopathy progression to the decline in chaperone-mediated autophagy that occurs during aging. Underscoring the importance of a balanced CMA pathway in maintaining skeletal muscle function and integrity, the study also provides mechanistic insights into the pathways that are dysregulated due to defective CMA and presents an approach to reverse the age-dependent decline in this process.: ATP2A1, ATPase sarcoplasmic/endoplasmic reticulum Ca2+ transporting 1; CMA, chaperone-mediated autophagy; HSPA8, heat shock protein family A (Hsp70) member 8; LAMP2A, lysosomal associated membrane protein 2A. - Source: PubMed
Publication date: 2026/04/19
Dialynaki DimitraKlionsky Daniel J - This study aimed to develop a non-invasive method combining urinary metabolomics and proteomics to identify biomarkers for gastric cancer and to elucidate the molecular mechanisms associated with its progression. - Source: PubMed
Publication date: 2026/04/01
Wang YadanWu JingSu JiayiLi WenkunDing PengpengWang Miaomiao - Wuweiganlu (WGL) is a traditional formulation widely applied in the treatment of rheumatoid arthritis (RA), yet the identity of its bioactive constituents remains inadequately defined. In this study, ultra-performance liquid chromatography coupled with quadrupole time-of-flight mass spectrometry (UPLC-Q-TOF-MS) and untargeted serum metabolomics were employed to characterize the active components of WGL. Fraxin was identified as a principal compound from WGL. To investigate its therapeutic mechanism in RA, a series of in silico and experimental approaches were conducted. Network pharmacology analysis and RNA sequencing identified heat shock protein family member 8 (HSPA8) as a potential molecular target of Fraxin, which was further validated by molecular docking studies. Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses indicated that Fraxin exerts its effects primarily by modulating cell apoptosis through the PI3K signaling pathway. In vitro experiments demonstrated that Fraxin significantly reduced inflammatory responses and downregulated HSPA8 expression in lipopolysaccharide (LPS)-stimulated fibroblast-like synoviocytes (FLs) and macrophages. In vivo, Fraxin administration markedly reduced paw swelling, alleviated bone deformities, and improved bone volume fraction (BV/TV) in male IL1RA-deficient mice exhibiting spontaneous arthritis. Histological analysis confirmed that Fraxin attenuated joint inflammation by modulating the inflammatory microenvironment. Additionally, Fraxin inhibited synovial hyperplasia by regulating mitochondrial membrane potential collapse in FLs. Functional assays revealed that this regulation occurred via the inhibition of HSPA8/PI3K/AKT signaling axis, thereby suppressing aberrant FLS proliferation and contributing to the attenuation of RA progression. - Source: PubMed
Publication date: 2026/03/24
Xu AnjingHou BaoZhang ShijieMa XiaoyueWen YuanyuanZhu XuexueCai WeiweiChen JingMi MaNhamdrie TsedienQiu LiyingSun HaijianHua Minhui