Ask about this productRelated genes to: CCT7 antibody
- Gene:
- CCT7 NIH gene
- Name:
- chaperonin containing TCP1 subunit 7
- Previous symbol:
- -
- Synonyms:
- Ccth, Nip7-1
- Chromosome:
- 2p13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1999-02-26
- Date modifiied:
- 2016-01-06
Related products to: CCT7 antibody
Related articles to: CCT7 antibody
- Posttraumatic joint contracture (PTJC) is a prevalent complication of joint injury, characterised by marked reductions in both active and passive joint motion. Previous studies have indicated that the chaperonin-containing T-complex polypeptide (CCT) is involved in fibrotic processes. Thus, this study aims to explore the role of CCT7 in PTJC and clarify its underlying regulatory mechanisms. We found that CCT7 expression was significantly upregulated in PTJC joint tissues and in fibroblasts stimulated with TGF-β1. Knockdown of CCT7 markedly reduced the expression of α-SMA and COL-I and suppressed fibroblast migration, while simultaneously promoting autophagy, as indicated by increased LC3-II and Beclin-1 levels and decreased p62 expression, thereby alleviating joint fibrosis. Interestingly, CCT7 interacted with TRAF6 to facilitate its ubiquitination and degradation. Knockdown of TRAF6 reversed the promoting effect of CCT7 knockdown on autophagy in fibroblasts and exacerbated fibrosis. Consistently, in vivo experiments demonstrated that CCT7 knockdown improved joint range of motion, reduced the expression of fibrosis-related proteins, enhanced autophagy and ultimately alleviated fibrosis. - Source: PubMed
Li YutaiZhang WenhuiXu WenbinHuang YuliangCai HonghuaZhang NanweiLiang TangzhaoLiu Guihua - TFEB (transcription factor EB) regulates the expression of autophagy and lysosomal genes, is activated by various cellular stresses, and plays a key role in maintaining cellular homeostasis. Recent work demonstrates that TFEB is activated during lysosomal damage through two distinct mechanisms: ATG conjugation-dependent and -independent. TFEB activation proceeds sequentially through two modes. In the early ATG conjugation-independent mode (Mode I), APEX1 interacts with TFEB in the nucleus, maintaining its transcriptional activity and protein stability. In the later ATG conjugation-dependent mode (Mode II), CCT7 and TRIP6 translocate to lysosomes and interact with TFEB, modulating its phosphorylation and nuclear localization. Moreover, TFEB regulation induced by other cellular stresses-such as oxidative stress, proteasome inhibition, mitochondrial damage, and DNA damage-also involves either Mode I or Mode II. Our findings provide new insights into a unified understanding of TFEB regulation under diverse cellular stress conditions. - Source: PubMed
Publication date: 2026/03/30
Shima TakayukiNakamura Shuhei - N6-methyladenosine (m6A) modification is a key epigenetic modification involved in many diseases. However, the roles of m6A regulators in the progression of colorectal adenoma (CRA) or colorectal cancer (CRC) are still unclear fully. - Source: PubMed
Publication date: 2026/03/05
Wang WeiZhang XiaohuiWang MinWang LiQian ShiqingCheng WenliXu FangDing ShaopengZhu YutingJin GuoqingYang WanshuiHu AnlaZhao Qihong - CCT7, a member of the t-complex polypeptide 1 chaperone family, facilitates ATP-dependent protein folding; however, its role in development and progression of malignant tumors remains unclear. This study aimed to characterize the expression pattern of CCT7 in colonic adenocarcinoma (COAD) and evaluate its role in the initiation and development of COAD. Public bioinformatic databases were analyzed to assess CCT7 expression in COAD, and these findings were validated using human clinical specimens through immunohistochemistry (IHC) assay. The prognostic significance of CCT7 was examined using Kaplan–Meier method and Cox regression analysis. Gene Ontology-Biological Process (GO-BP) and Kyoto Encyclopedia of Genes and Genomes (KEGG) enrichment analyses were performed to explore the potential biological functions and downstream pathways associated with CCT7. CCK-8, colony formation and Transwell assays were conducted to determine the impact of CCT7 on cell proliferation, migration and invasion in COAD cell lines. Associations between CCT7 expression and immune cell infiltration or drug sensitivity were evaluated using single-sample gene set enrichment analysis and correlation analysis. Finally, immune checkpoint inhibitor therapy scores and their relationship with CCT7 expression were assessed using data from The Cancer Immunome Atlas. CCT7 expression was significantly up-regulated statistically in COAD tissues compared with normal colonic tissues (< 0.05) and elevated CCT7 levels were associated with poorer prognosis of COAD patients (< 0.05). GO-BP enrichment analysis indicated that CCT7 was primarily involved in the processes related to cell proliferation and microtubule organization (< 0.05). Consistently, functional assays confirmed that CCT7 knockdown inhibited COAD cell proliferation, migration, and invasion (< 0.05). CCT7 expression showed a negative correlation with infiltration of most immune cell types (< 0.05) and demonstrated no significant association with predicted responses to PD-1 and CTLA-4 inhibitor therapies (> 0.05). Moreover, drug sensitivity analyses showed that CCT7 affected the sensitivity of COAD samples to several anti-cancer drugs (< 0.001). KEGG enrichment analysis revealed that CCT7 was associated with multiple pathways (< 0.05). CCT7 may function as an oncogenic driver that promotes the malignant phenotype of COAD and represents a promising prognostic biomarker. It may also provide a valuable reference for guiding clinical therapeutic strategies in COAD. - Source: PubMed
Publication date: 2026/01/28
Li WenxuShi QizhongMu YonghuiLi ChengleiZhao WenchaoHan Na - Profiling the interactome of catechol derivatives plays a key role in revealing their pharmacology. Existing approaches for target identification generally rely on either the modification of ligands or significant perturbation of protein properties, which may restrict the coverage of interacting proteins. Here, we present a modification-free strategy, termed oxidative addition-boronate affinity enrichment (OABA), that employed catechol oxidation to -quinones to covalently capture nucleophilic residues of proteins, followed by selective enrichment via boronate affinity recognition of the catechol moiety. This redox-enabled approach eliminated the requirement for drug molecule modification while enabling direct mapping of catechol-protein interactomes in living cells. Proof-of-concept studies with isoproterenol (ISO) achieved a 2-fold enrichment of SOD1-adduct peptides from the HeLa peptide mixture. Application to quercetin in live HeLa cells identified 74 high-confidence interacting targets, enriched in biological process linked to the modulation of protein stabilization, energy metabolism, and cell growth. Through molecular docking and CETSA profiling, we validated the interaction of FDPS, CCT7, and CS with quercetin. Collectively, the OABA provided a reliable, modification-free platform for mapping the native interactome of catechol-containing compounds and advancing the understanding of polyphenolic pharmacology. - Source: PubMed
Publication date: 2026/01/12
Qiao ZichunZhang XiaozheWang HeShan YichuLi XiaoCao ChuhanLiang ZhenZhang YukuiJiang BoZhang Lihua