AKT2 Antibody
- Known as:
- AKT2 Antibody
- Catalog number:
- abx000688
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- AKT2 Antibody
Related genes to: AKT2 Antibody
- Gene:
- AKT2 NIH gene
- Name:
- AKT serine/threonine kinase 2
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 19q13.2
- Locus Type:
- gene with protein product
- Date approved:
- 1992-11-05
- Date modifiied:
- 2016-10-05
Related products to: AKT2 Antibody
Related articles to: AKT2 Antibody
- Polycystic ovary syndrome (PCOS) is a complex endocrine-metabolic disorder characterised by hypothalamic-pituitary-gonadal (HPG) axis dysfunction and pathological gonadotropin-releasing hormone (GnRH) hypersecretion. While metformin demonstrates therapeutic efficacy in PCOS, its potential neuroendocrine mechanisms remain incompletely understood. This study aimed to investigate the involvement of hypothalamic signalling in metformin-responsive neuroendocrine regulation in PCOS. - Source: PubMed
Publication date: 2026/07/24
Guo NaLi HongyunHe JinhongZhou HuanhuanWang XingYang LinlinMa Huijuan - Insulin attenuates the effects of advanced glycation end products (AGEs) by inducing a disintegrin and metalloprotease 10 (ADAM10)-mediated cleavage of the receptor for AGEs (RAGE); however, the molecular mechanism underlying this process remains incompletely understood. We investigated the mechanism by which insulin promotes ADAM10-mediated RAGE shedding in cultured human aortic endothelial cells (HAECs). AGE-modified bovine serum albumin (AGE-BSA) increased intercellular adhesion molecule-1 (ICAM-1) expression, whereas insulin pretreatment (0.1-100 nM) attenuated this effect. Mechanistically, insulin activated AKT1, AKT2, and AKT3, promoted ADAM10 translocation to the cell surface, and enhanced RAGE ectodomain shedding. In contrast, treatment with GI254023X (an ADAM10 inhibitor) or ADAM10 knockdown using siRNA abolished insulin-induced RAGE ectodomain shedding. Likewise, knockdown of AKT1, AKT2, or AKT3 using siRNA, as well as treatment with the pan-AKT inhibitor MK-2206, inhibited insulin-induced ADAM10 cell surface translocation and RAGE ectodomain shedding. Co-immunoprecipitation analysis further demonstrated an interaction between Rab14 and ADAM10. Insulin enhanced this interaction and promoted the translocation of both Rab14 and ADAM10 to the cell surface. Conversely, Rab14 knockdown blocked insulin-induced ADAM10 cell surface translocation and RAGE ectodomain shedding, thereby abolishing the protective effect of insulin against AGE-BSA-induced ICAM-1 expression. Collectively, these findings demonstrate that insulin promotes Rab14-mediated trafficking of ADAM10 to the cell surface through AKT activation in HAECs, resulting in enhanced RAGE ectodomain shedding. - Source: PubMed
Publication date: 2026/09/18
Baek Chung HeeKim HyosangMoon Soo YoungLee Eun KyoungYang Won Seok - Metabolic dysfunction-associated steatohepatitis (MASH) is characterized by hepatic steatosis, inflammation, fibrosis, and metabolic dysfunction, with limited therapeutic options currently available. This study investigated whether pharmacological inhibition of Galectin-3 (Gal-3), a β-galactoside-binding lectin implicated in inflammation and fibrosis, using modified citrus pectin (MCP), attenuates established MASH in ApoE-deficient mice. Mice were assigned to four groups: standard chow (CTL), standard chow plus MCP (CTL + MCP), Western diet with fructose-enriched drinking water (WD), and WD plus MCP (WD + MCP). MCP (1% in drinking water) was administered during the final four weeks of the 11-week experimental protocol, after the establishment of metabolic dysfunction and hepatic steatosis. Compared with untreated WD mice, WD + MCP mice exhibited improved glucose tolerance, as evidenced by a 22.9% reduction in glucose area under the curve ( = 0.01), and enhanced hepatic insulin signaling, reflected by a 254.1% increase in insulin-stimulated AKT2 phosphorylation ( = 0.0002). MCP treatment also reduced hepatic lipid accumulation (39.8%, = 0.0055) and hepatic triglyceride content (26.1%, = 0.0003), accompanied by reductions in circulating triglyceride and cholesterol concentrations. Furthermore, WD + MCP mice exhibited reduced hepatic Gal-3 expression (25.8%, = 0.0199), decreased F4/80 immunoreactivity (49.2%, = 0.0061), attenuated JNK phosphorylation (46.6%, = 0.0118), reduced collagen deposition (47.0%, = 0.0002), and lower plasma ALT (52.9%, = 0.0009) and AST (48.8%, = 0.04) activities. Collectively, these findings demonstrate that MCP attenuates multiple metabolic, inflammatory, fibrotic, and hepatic injury features of established Western diet-induced MASH, supporting Gal-3 as a promising therapeutic target and MCP as a potential pharmacological strategy for MASH. - Source: PubMed
Publication date: 2026/08/27
Santos Anne R MCruz Alessandra GCamargo Felipe NSantos Jessica D MModel Jorge F ASilva José F TMatos Sandro LAraujo Layanne C CCamporez João Paulo - (), a primary exacerbating factor in eczema, remains a prevalent pathogenic public-health threat. The mechanism of mast cell/basophil degranulation in the context of -exacerbated eczema remains unclear. We sought to investigate the direct effect of mast cell/basophil activation by isolated from patients with severe eczema undergoing topical steroid withdrawal (TSW) and understand the mechanism of berberine (BBR) in inhibiting this activation. Clinical strains (N = 8) were isolated from skin swabs of severe eczema patients and confirmed by sequencing. Human basophils (KU812), rat basophils (RBL-2H3) and murine mast cells (MC/9) were pre-treated with BBR for 48 h. and stimulated with heat-killed standard - and clinical strains for 45 min, and degranulation was measured. BBR's molecular-targets on basophils were identified by computational modeling and validated by qRT-PCR. BBR prevented degranulation following standard stimulation in KU812, RBL-2H3 and MC/9 cells. BBR dose-dependently inhibited degranulation in KU812. BBR inhibited TNF-α and IL-4 release, and markedly suppressed the expression of FcεR1 (α, β, γ), TNFα, MAPK1, MAPK3, AKT2, CASP9, and CCND1 following standard stimulation. BBR dose-dependently inhibited KU812 cell degranulation, markedly reduced TNF-α, IL-4, and MAPK1 and enhanced NFκB1A expression following clinical strain stimulation. BBR inhibition of -induced KU812 activation was at least associated with inhibition of MAPK-associated gene expression. This study provides novel insights into BBR's effect in preventing and human basophil interaction. - Source: PubMed
Publication date: 2026/09/03
Maskey Anish RKopulos DanielSpears MadisonWang Zhen-ZhenMo XianMusa IbrahimYang NanNowak-Wegrzyn AnnaChung DannaMaitland Anne LWang JulieTiwari Raj KSampson Hugh AGeliebter JanLi Xiu-Min - Obesity and type 2 diabetes mellitus (T2DM) are associated with chronic low-grade inflammation that sustains insulin resistance and metabolic dysfunction. Adipose tissue, through the secretion of adipokines and cytokines, plays a central role in shaping macrophage polarization and maintenance of an inflammatory microenvironment. While kinase-mediated signaling such as PI3K-AKT has been extensively studied, the contribution of phosphatases, particularly protein phosphatase 2A (PP2A), to macrophage polarization remains poorly defined. In this study, RAW264.7 macrophages exposed to inflammatory adipocyte-conditioned medium exhibited altered AKT isoform expression, including upregulation of AKT2 and downregulation of AKT1, along with activation of the PI3K, mTORC1/S6K pathway and suppression of protein phosphatase 2A (PP2A) activity, collectively promoting M1 pro-inflammatory polarization. To further elucidate the molecular mechanism, we performed molecular docking and 100 ns molecular dynamics simulations of both unphosphorylated AKT and ATP-bound (phosphorylated) AKT interacting with PP2A. The simulations revealed that phosphorylated AKT has higher binding affinity and greater structural stability with PP2A, facilitated by persistent hydrogen bonds with the regulatory and scaffolding subunits, suggesting a natural self-limiting mechanism that maintains the phosphorylation-dephosphorylation balance. We hypothesise that the experimentally observed reduction in PP2A levels in macrophages exposed to inflammatory adipocyte signals may impair this regulatory loop, favouring sustained pro-inflammatory signaling. These integrated experimental and computational findings highlight PP2A as a critical negative regulator of AKT-driven macrophage activation and suggest that therapeutic strategies aimed at restoring PP2A activity could prevent chronic inflammation in obesity and T2DM and could serve as a potential molecular target for mitigating metabolic inflammation. - Source: PubMed
Publication date: 2026/09/09
K Vinoth KannanT KothaiB S Lakshmi