Ask about this productRelated genes to: BACE2 antibody
- Gene:
- BACE2 NIH gene
- Name:
- beta-secretase 2
- Previous symbol:
- AEPLC
- Synonyms:
- CEAP1, DRAP, ALP56
- Chromosome:
- 21q22.2-q22.3
- Locus Type:
- gene with protein product
- Date approved:
- 2000-05-23
- Date modifiied:
- 2018-05-09
Related products to: BACE2 antibody
Related articles to: BACE2 antibody
- Alzheimer's disease (AD) is characterized by the accumulation of amyloid-β (Aβ) peptides, which are a key factor in its pathogenesis. In this study, we present the design and evaluation of cis-γ-amino-L-proline peptides as metabolically stable, cell-penetrating molecules that can modulate amyloidogenic processing. We screened a library of γ-peptides in primary neuronal cultures to determine their effects on endogenous Aβ1-42 production, cytotoxicity, and β-secretase (BACE1)-associated activity. Comparative analysis of structurally related analogues enabled the identification of molecular features associated with Aβ-lowering activity, establishing a qualitative structure-activity relationship. Peptide 33 (P33) emerged as a lead candidate, selectively reducing BACE1-associated activity without significantly inhibiting the associated activity of the homologous enzyme, BACE2. In vitro blood-brain barrier (BBB) assays revealed that P33 exhibits favorable transendothelial permeability. Intraperitoneal administration of P33 in APP/PS1 mice decreased Aβ levels, reduced amyloid plaque burden, and improved performance in a behavioral recognition task without inducing cytotoxicity, and with no overt histopathological or selected neuroinflammatory changes. These results define cis-γ-amino-L-proline peptides as a bioorganically distinct and modular scaffold for the development of intracellular modulators of Aβ production. - Source: PubMed
Publication date: 2026/08/15
Jácome DayanethPérez-Palau MarinaMartínez-Soria InésLidón LaiaVergara CristinaCarbajo DanielPulido XimenaSánchez-Navarro MacarenaGiralt ErnestAlbericio FernandoRoyo MiriamGavín RosalinaDel Río José Antonio - Chemoresistance to platinum-based regimens, primarily gemcitabine plus cisplatin, remains a major obstacle in the treatment of advanced bladder cancer. Identifying the underlying molecular mechanisms is critical for developing effective therapeutic strategies to improve clinical outcomes. - Source: PubMed
Publication date: 2026/08/18
Li ZekunLi SanxiangLiu ZhenyuSun YulinZhang Yun - : Pathological aggregation of islet amyloid polypeptide (IAPP) contributes to β-cell dysfunction in type 2 diabetes. Our previous studies demonstrated that caveolin-1 (Cav-1) deficiency protects β-cells from palmitate-induced apoptosis. Microarray profiling further indicated that Cav-1 silencing alters IAPP expression. This study aimed to investigate the effects of Cav-1 depletion on IAPP secretion and expression and to explore the potential involvement of thioredoxin-interacting protein (TXNIP). : We performed lentiviral-mediated Cav-1 knockdown in NIT-1 cells and isolated murine islets, and simultaneously generated an inducible β-cell-specific Cav-1 knockout (iβ-Cav1 KO) mouse model. IAPP secretion and expression were assessed by ELISA, Western blot, qPCR and immunofluorescence. The expression of IAPP-processing enzymes (PAM, PC1, and PC2) and degradation factors (IDE and BACE2) was examined. Co-immunoprecipitation (Co-IP) and immunofluorescence were performed to investigate the interaction between Cav-1 and TXNIP. : Cav-1 depletion significantly reduced both IAPP secretion and expression in vitro and in vivo. High-fat-diet-fed iβ-Cav1 KO mice exhibited the lowest serum IAPP levels. Mechanistically, Cav-1 depletion was associated with downregulation of PAM, PC1, and PC2 and upregulation of IDE and BACE2. Additionally, Cav-1 depletion decreased TXNIP expression. Immunofluorescence revealed co-localization of Cav-1 and TXNIP, and co-immunoprecipitation further demonstrated their direct physical interaction. : Cav-1 is essential for IAPP secretion and expression in β-cells. The direct physical interaction between Cav-1 and TXNIP suggests that TXNIP may mediate the regulatory effects of Cav-1 on IAPP processing or secretion. These findings identify the Cav-1-TXNIP axis as a potential target for mitigating IAPP-related β-cell dysfunction. - Source: PubMed
Publication date: 2026/06/15
Liu KunyingYang XubinLin ShuoLin ChuwenCai NanZeng LongyiZeng Wen - To investigate the potential molecular mechanisms underlying aspartame (APM)-induced malignant phenotypic changes in colorectal cancer (CRC). Candidate targets of APM were identified by integrating the ChEMBL, SwissTargetPrediction, and SEA databases. Differential expression analysis was performed using transcriptomic data from The Cancer Genome Atlas (TCGA) CRC cohort, followed by weighted gene co-expression network analysis (WGCNA) to identify key modules associated with CRC. The intersection of differentially expressed genes (DEGs), key module genes, and candidate APM targets was used to identify shared APM-CRC candidate genes. Gene Ontology and Kyoto Encyclopedia of Genes and Genomes enrichment analyses, machine learning, SHAP-based interpretability analysis, molecular docking, and molecular dynamics simulations were then conducted to identify key feature genes and evaluate their potential interactions with APM. Finally, EdU, CCK-8, ROS fluorescence staining, and Western blot assays were performed in HCT116 and SW480 cells to validate the effects of APM on CRC cell proliferation, oxidative stress, and epithelial-mesenchymal transition (EMT)-related molecular alterations. A total of 4790 DEGs were identified between CRC and normal tissues, and WGCNA further identified key modules significantly associated with the tumor phenotype. Intersection analysis yielded 1003 CRC-related candidate genes and 26 shared APM-CRC candidate genes. Enrichment analysis indicated that these genes were mainly involved in extracellular matrix remodeling, regulation of cell adhesion, glutathione metabolism, and xenobiotic metabolism. Machine learning combined with SHAP analysis ultimately identified SLC7A5, MMP3, ITGA2, CAPN2, and BACE2 as key feature genes. Molecular docking and molecular dynamics simulations suggested that APM could potentially interact with all five key proteins, with MMP3 and ITGA2 showing relatively stronger binding affinity. In vitro experiments showed that APM increased the proliferation of HCT116 and SW480 cells, elevated intracellular ROS levels, and was associated with decreased E-cadherin expression and increased N-cadherin and Vimentin expression. These findings suggest that APM exposure may be associated with increased CRC cell proliferation and EMT-related molecular alterations, accompanied by changes in oxidative stress-related processes, extracellular matrix remodeling, and abnormal cell adhesion. SLC7A5, MMP3, ITGA2, CAPN2, and BACE2 may represent APM-responsive candidate molecules involved in these cellular responses. - Source: PubMed
Publication date: 2026/06/19
Liu QuanxiaYu DongQiao LijiaoWang NanFan WeiningWei TingtingTian ZhiqiangMa XiaoqiangXie Xiaoliang - Lynch Syndrome (LS) is an autosomal dominant disease characterized by germline heterozygous mutations in DNA mismatch repair (MMR) genes. High-risk LS patients may proceed to colorectal cancer (CRC). However, the drivers or biomarkers of LS benign colon tissue approaching malignant CRC are not completely understood. This study aimed to understand the molecular and cellular changes during malignant transition in LS. - Source: PubMed
Publication date: 2026/05/25
Xu JunfengZhang JianlinLi YuhangWang ZhiqinLi QianruLiu AijunSheng JianqiuDong GeYang LangCai Zhigang