HSC70 | heat shock cognate protein 70
- Known as:
- HSC70 | heat shock cognate protein 70
- Catalog number:
- AS07 233
- Product Quantity:
- 100 ul
- Category:
- -
- Supplier:
- Agris
- Gene target:
- HSC70 | heat shock cognate protein 70
Related genes to: HSC70 | heat shock cognate protein 70
- 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: HSC70 | heat shock cognate protein 70
Related articles to: HSC70 | heat shock cognate protein 70
- Diabetic nephropathy (DN) is one of the most prevalent microvascular complications of diabetes mellitus. In the present study, the effects of PLCG1 DN, as well as its underlying molecular mechanisms associated with ferroptosis, were investigated. Single-cell RNA sequencing data and bioinformatic analyses were employed to support these experimental findings. For experiments, a DN model was established in C57BL/6 mice via streptozotocin injection. For investigations, NRK-52E cells were exposed to 20 mmol/L d-glucose to induce a DN-like cellular phenotype. PLCG1 mRNA expression levels were upregulated in DN patients, compared with the normal group. Elevated serum PLCG1 mRNA expression in DN patients correlated with increased urinary creatinine (Cre), blood urea nitrogen (Bun), and 24 h urinary microalbuminuria (mAlb) levels. The mRNA and protein expression levels of PLCG1 m in tissues were significantly upregulated in the mouse DN model and high glucose-induced NRK-52E. Single-cell analysis was performed to detect PLCG1 expression in renal cells of the DN model. Additionally, high glucose exposure induced PLCG1 histone acetylation in the DN model. Sh-PLCG1 alleviated DN progression and reduced oxidative stress in the mouse model. Mechanistically, PLCG1 increased mitochondria-dependent ferroptosis in the DN model. PLCG1 is interlinked with LAMP2A and facilitates the ubiquitination of LAMP2A. Specifically, PLCG1 upregulation enhanced K48-linked ubiquitination of LAMP2A protein in high glucose-induced NRK-52E cells. Ultimately, PLCG1 inhibited the LAMP2A/HSPA8 signaling pathway in the DN model. Our study identifies PLCG1 as a novel regulatory target that inhibits the LAMP2A/HSPA8 signaling pathway. This inhibition promotes mitochondrial oxidative stress, which in turn increases cellular ferroptosis and accelerates the progression of DN. Importantly, PLCG1 holds promise as a critical clinical biomarker for diagnosing DN. It may serve as a potential therapeutic target to mitigate glucose-induced ferroptosis, with implications for the management of not only DN but also other diabetes-related complications. - Source: PubMed
Publication date: 2026/01/14
Ge JunWang ZhenzhenXu TingJiang RuifengZhang Xuefeng - Nucleated erythroid cells (NECs) have emerged as active participants in immune responses in addition to their canonical oxygen transport function. The subpopulations and immune heterogeneity of chick erythroid cells (ch-ECs) upon infection have not been fully characterized. Single-cell RNA sequencing (scRNA-seq) was used to profile ch-ECs in chicks infected with avian pathogenic (APEC). Unsupervised clustering uncovered ten distinct ch-EC subpopulations (C1-C10), with significant compositional shifts between infected and control groups. Pseudotime analysis revealed a developmental continuum: C1, C3, C5, and C9 as early progenitors; C2, C4, C6, C7, and C10 as mature erythroid cells; and C8 as a naive population. We revealed 62 immune-related genes, including protein kinases and heat shock proteins, and subpopulation-specific differentially expressed genes (DEGs) linked to immune functions. SCENIC analysis revealed Fos, Srf, and Stat3 as key transcription factors with elevated regulon activity and specificity following infection. Subpopulations C2, C4, C6, and C7, which exhibited marked abundance changes, were scrutinized for immune relevance through integrated multi-omics analysis. Immune-related genes including , , , , , , , and were identified. Enrichment analysis indicated activation of the MHC class I antigen presentation pathway, while pathways such as Mitogen-Activated Protein Kinase (MAPK) signaling, NOD-like receptor (NLR) signaling, and the heat shock response were found to be suppressed. In conclusion, this study delineates the immune gene repertoire and signaling networks of ch-ECs during APEC infection, offering new perspectives on NEC immunoregulatory functions. - Source: PubMed
Publication date: 2026/01/07
Cai FujuanWang XianjueWang ChunzhiWang YuzhenZhang Wenguang - Notwithstanding the declaration by the World Health Organization in May 2023 regarding the conclusion of the COVID-19 pandemic, new cases of this potentially lethal infection continue to be documented globally, exerting a sustained influence on the worldwide economy and social structures. Contemporary SARS-CoV-2 variants, while associated with a reduced propensity for severe acute pathology, retain the capacity to induce long-term post-COVID syndrome, including in ambulatory patient populations. This clinical phenomenon may be attributable to potential autoimmune reactions hypothetically triggered by antiviral antibodies, thereby underscoring the need for developing novel, universal vaccines against COVID-19. The nucleocapsid protein (N), being one of its most conserved and highly immunogenic components of SARS-CoV-2, presents a promising target for such investigative efforts. However, the protective role of anti-N antibodies, generated during natural infection or through immunization with N-based vaccines, alongside the potential adverse effects associated with their production, remains to be fully elucidated. In the present study, we aim to identify potential sites of homology in structures or sequences between the SARS-CoV-2 N protein and human antigens detected using hyperimmune sera against N protein obtained from mice, rabbits, and hamsters. - Source: PubMed
Publication date: 2025/12/22
Rak AlexandraZabrodskaya YanaWong Pei-FongIsakova-Sivak Irina - Detyrosination is one of the most well-studied post-translational modifications of microtubules (MTs), significantly impacting cell growth, differentiation, division, and intracellular traffic. The VASH1/2-SVBP complex is the first identified carboxypeptidase that specifically catalyzes the detyrosination modification of microtubules. While the structure and mechanisms of the VASH1/2-SVBP complex in mediating this modification are well studied, the regulatory mechanisms governing the catalytic activity of this enzyme remain elusive. Here, we identify a highly conserved five-residue motif located at the C-terminus of VASH1, demonstrating that this motif is crucial for the in vivo detyrosination activity of VASH1. Through peptide pull-down assays combined with mass spectrometry analysis, we identified the chaperone protein HSPA8 as a binding partner of VASH1. The structural model of the HSPA8-VASH1-SVBP ternary complex, predicted by AlphaFold, indicates that HSPA8 interacts with VASH1 through two distinct interaction surfaces. The subsequent biochemical analysis with mutagenesis assays was performed to validate the binding model of HSPA8 to VASH1. Furthermore, in vivo detyrosination assays in HeLa cells reveal that HSPA8 promotes the detyrosination modification of microtubules through direct binding to VASH1. Thus, our study identifies the HSPA8-regulated pathway of microtubule detyrosination, providing a potential target for the diagnosis and therapy of human diseases associated with abnormal microtubule detyrosination. - Source: PubMed
Guo HaoHe LibangWu ZhuoxiYuan RuifangSu HuilingLiu XianchuLi Faxiang - - Source: PubMed
Publication date: 2026/01/16
Wang FeiHuang HuimingZhang RuoxinWei XuejiaoWang ZhuguoQiu XinyuGao YufengWang XiaoxueXie WanyingZhang HongbingTu PengfeiHu Zhongdong