Polyclonal APG7 (CT), (Autophagy Protein 7)
- Known as:
- Polyclonal APG7 (CT), (Autophagy Protein 7)
- Catalog number:
- pc-514
- Product Quantity:
- USD
- Category:
- -
- Supplier:
- Kamiya biomedical company
- Gene target:
- Polyclonal APG7 () (Autophagy Protein 7)
Related genes to: Polyclonal APG7 (CT), (Autophagy Protein 7)
- Gene:
- ATG7 NIH gene
- Name:
- autophagy related 7
- Previous symbol:
- APG7L
- Synonyms:
- GSA7, DKFZp434N0735
- Chromosome:
- 3p25.3
- Locus Type:
- gene with protein product
- Date approved:
- 2003-11-20
- Date modifiied:
- 2016-10-05
Related products to: Polyclonal APG7 (CT), (Autophagy Protein 7)
Related articles to: Polyclonal APG7 (CT), (Autophagy Protein 7)
- LncRNAs emerge as critical regulators of gene expression and epigenetic modulation in human cancer. However, the biological and clinical significance of the lncRNA in differentiated thyroid cancers (DTCs) remains poorly understood. - Source: PubMed
Publication date: 2026/06/08
Murugan Avaniyapuram KannanAl-Hindi HindiAlzahrani Ali S - The present study aimed to investigate the therapeutic effects and underlying mechanism of oridonin (ORI) in ulcerative colitis (UC) using the lipopolysaccharide (LPS)‑induced macrophage inflammatory model and the dextran sulfate sodium (DSS)‑induced mouse UC model. Cell Counting Kit‑8 assay was used to determine the appropriate drug concentrations for the experiments. Western blotting and reverse transcription‑quantitative polymerase chain reaction were performed to evaluate the expression levels of proteins and mRNAs related to signaling pathways, autophagy and inflammatory cytokines. The autophagy inhibitor 3‑methyladenine was applied to verify the role of the PI3K/AKT/mTOR pathway. , the disease activity index (DAI) was recorded and colon tissue damage was assessed by hematoxylin and eosin staining. Serum inflammatory cytokines were measured using an enzyme‑linked immunosorbent assay. Network pharmacology based on GeneCards and Traditional Chinese Medicine Systems Pharmacology databases, along with Gene Ontology and Kyoto Encyclopedia of Genes and Genomes enrichment analysis, predicted involvement of the PI3K/AKT/mTOR pathway in the pathogenesis of UC, which was further validated by the immunohistochemistry, immunofluorescence and western blotting of colon tissues. The results indicated that ORI significantly reduced the expression of pro‑inflammatory cytokines and increased the anti‑inflammatory cytokine interleukin‑10 in LPS‑stimulated macrophages. In DSS‑induced colitis mice, ORI treatment alleviated body weight loss, decreased DAI scores, improved colon shortening and upregulated the expression of intestinal tight junction proteins. Mechanistically, ORI inhibited the PI3K/AKT/mTOR pathway and altered autophagy‑related molecular markers, as evidenced by increased levels of autophagy‑related (ATG)13, beclin‑1, ATG12, ATG7 and ATG5 as well as decreased expression of p62. In conclusion, ORI alleviates inflammatory responses and mitigates UC‑related pathological changes , which may be associated with suppression of the PI3K/AKT/mTOR pathway and modulation of autophagy‑associated protein markers. - Source: PubMed
Publication date: 2026/06/19
Miao ZhongxingLiu BaohongZhou XingzhiLu MengruJia NiZhang HuaminQi YingTan XiaoyuZhang Qinggao - Atg8ylation is a key step during autophagy where Atg8-family proteins are conjugated to the expanding phagophore. In addition to double-layered autophagic compartments, Atg8ylation occurs on various other cellular membranes and is emerging as a general eukaryotic membrane-tagging system comparable to that of ubiquitin tagging of proteins. While canonical autophagy has been characterized across eukaryotes, Atg8ylation beyond canonical autophagy has mostly been explored in mammals. ATG7 is an E1-like enzyme which participates in the three-step ubiquitin-like cascade that mediates Atg8-family protein conjugation. Apart from its role in Atg8ylation, several independent functions have been reported in mammals. Exploring functions of ATG7 from an evolutionary perspective highlights that Atg8ylation on single-layer membranes is conserved across eukaryotes. Although Atg8ylation-independent functions of ATG7 remain largely unexplored outside mammals, evidence from other eukaryotic clades suggests that some of these functional roles may be conserved. In this review, ATG7 functions are organized by eukaryotic clades to gain better understanding of their evolutionary history.: AD: active domain; CASM: conjugation of Atg8 to single layer membranes; EMT: endothelial-to-mesenchymal transition; ESCRT: endosomal sorting complexes required for transport; HFD: high-fat diet; LAP: LC3-associated phagocytosis; LECA: last eukaryotic common ancestor; NTD: N-terminal domain; PE: phosphatidylethanolamine; PS: phosphatidylserine; UBL: ubiquitin-like. - Source: PubMed
Publication date: 2026/06/23
Hjaltalin Valgerdur JOgmundsdottir Margret Helga - Japanese encephalitis virus (JEV) is a neurotropic flavivirus that causes a substantial threat to human health and livestock; however, the epitranscriptomic mechanisms that support its replication remain poorly defined. Here, we identify a proviral host factor CH zinc-finger protein ZNF33B that promotes JEV infection through coupling N-methyladenosine (mA) RNA modification to autophagy regulation. Mechanistically, ZNF33B recruits METTL14 to stabilize the METTL3-METTL14 methyltransferase complex, thereby increasing global mA deposition. Multi-omics analyses reveal that ZNF33B selectively binds mA-modified sites within the antiviral transcript Trim25 (c.1567 and c.1669 bp) to accelerate its decay. We further demonstrate that TRIM25 functions as an E3 ubiquitin ligase that catalyzes K48-linked ubiquitination of ATG7 at lysines 389 and 423, leading to its proteasomal degradation and ultimately suppressing autophagic flux. In contrast, ZNF33B-mediated Trim25 degradation counteracts its inhibitory effect on autophagy, creating a favorable environment for viral replication. In vivo, adeno-associated virus (AAV)-mediated ZNF33B delivery increases mouse brain mA levels, decreases TRIM25 expression, elevates ATG7 abundance, exacerbates JEV-induced neuropathology, and accelerates mouse mortality. Together, these findings reveal a previously uncharacterized ZNF33B-mA-TRIM25-autophagy axis that JEV hijacks to evade host antiviral responses, providing new insights into flaviviral pathogenesis and potential therapeutic targets. - Source: PubMed
Publication date: 2026/06/18
Du JianLi ChunweiLuo JiyuanZhang HuizhiZhang JinyanWang SuyaChen HuanchunXu HongliLi XiangminQian Ping - The formation of the enteric nervous system (ENS) primarily involves the migration of enteric neural crest-derived cells (ENCCs) and the subsequent maturation of enteric neurons. The developmental dysfunction of ENCCs and enteric neurons can result in ENS disorders, such as hypoganglionosis (HG). Although neurite outgrowth is fundamental to neuronal maturation, the mechanisms by which neurite outgrowth influences neuronal maturation remain poorly defined. Here, we identified EMB as a critical regulator of enteric neuronal maturation. In mutant patients, the expression of EMB is reduced in the enteric neurons of the HG-affected colon. In mice, knockdown of exhibited HG-like features and defects. In vitro experiments, along with analyses using Smart-seq2 and immunoprecipitation-mass spectrometry, demonstrated that EMB is essential for autophagic flux and physically interacts with ATG7, recruiting it to the autophagosomal membrane to facilitate autophagosome formation, and then EMB/ATG7-mediated autophagy promotes neurite outgrowth. Our findings elucidate EMB-mediated autophagy as a pivotal pathway in regulating neurite outgrowth and promoting the maturation of enteric neurons, which provides a mechanistic basis for understanding ENS disorders. - Source: PubMed
Publication date: 2026/06/15
Wu LuyaoWang JingXiao JunMeng XinyaoWang JingMao HandanYou JingyiLi ZejianChen KeWang QiongZhou BingyanChen YingjianXiang LeiYu XiaosiYang ShiminZhang JiaxinZhuansun DidiJiao ChunleiWang DiYang JixinChen XuyongFeng Jiexiong