RPS6KB1 (phospho-Ser411) Antibody
- Known as:
- RPS6KB1 (phosphorilated-Ser411) Antibody
- Catalog number:
- abx000298
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- RPS6KB1 (phospho-Ser411) Antibody
Related genes to: RPS6KB1 (phospho-Ser411) Antibody
- Gene:
- RPS6KB1 NIH gene
- Name:
- ribosomal protein S6 kinase B1
- Previous symbol:
- STK14A
- Synonyms:
- S6K1, p70(S6K)-alpha, PS6K, S6K
- Chromosome:
- 17q23.1
- Locus Type:
- gene with protein product
- Date approved:
- 1994-07-11
- Date modifiied:
- 2018-04-18
Related products to: RPS6KB1 (phospho-Ser411) Antibody
Related articles to: RPS6KB1 (phospho-Ser411) Antibody
- Pulmonary fibrosis is a severe, chronic, and often lethal interstitial lung disease characterized by a destructive cycle of alveolar injury and inflammation, culminating in irreversible lung scarring. Its complex and multifactorial pathogenesis contributes to a poor prognosis and susceptibility to recurrent lung damage. This study employed an integrated network pharmacology and molecular docking approach to investigate the therapeutic repurposing of cilostazol for pulmonary fibrosis. Cilostazol was selected as a highly promising candidate owing to its broad pharmacological profile, encompassing anti-inflammatory, antioxidant, antiapoptotic, and antifibrotic properties. Network pharmacology analysis identified 10 potential targets of cilostazol, of which eight emerged as key network regulators: phosphodiesterase 3 (PDE3), PIK3CA, PTK2, RPS6KB1, VEGFR, F2-thrombin, ULK3 kinase, and PI3K delta. Molecular docking demonstrated that cilostazol binds to these profibrotic and fibrotic target proteins with binding affinities comparable to those of established experimental inhibitors. Experimental validation was performed using a bleomycin (BLM)-induced rat model of pulmonary fibrosis, incorporating histopathological and biochemical analyses of lung tissue and bronchoalveolar lavage fluid. Cilostazol exhibited significant antioxidant activity by reducing lipid peroxidation and restoring antioxidant enzyme levels. It exerted anti-inflammatory effects by downregulating proinflammatory cytokines (TNF-α, NO, and IL-6) and inflammatory markers (CRP, LDH, and MPO). Furthermore, cilostazol attenuated key indicators of fibrosis progression, including KL-6 and endothelin-1, alongside fibrotic markers such as TGF-β, α-SMA, and collagen I and III. At the molecular level, it significantly reduced the mRNA expression of fibrosis-associated genes, including TGF-β, fibronectin, α-SMA, collagen I, and MMP-7. Collectively, these findings demonstrate that cilostazol confers significant protection against bleomycin-induced pulmonary fibrosis through the targeted inhibition of the TGF-β/Smad, PI3K/AKT, and Wnt/β-catenin signaling cascades, highlighting its potential as a viable repurposed therapeutic strategy for inflammation-driven pulmonary fibrosis. - Source: PubMed
Publication date: 2026/05/28
Misar Pranaya LOtari Kishor VPande Vishal VIge Pradyumna P - Metabolic dysfunction-associated steatohepatitis (MASH) is emerging as a leading cause of chronic liver disease. MTOR (mechanistic target of rapamycin kinase) complex 1 (MTORC1) is a potential therapeutic target, whereas suppression of total MTORC1 activity can lead to unwanted effects. Here, we found that byakangelicin (Bya), a natural compound, selectively inhibited MTORC1-mediated phosphorylation of TFEB (transcription factor EB), without affecting canonical MTORC1 substrates. Knockout of hepatic blocked the alleviation effects of Bya on hepatic steatosis, inflammation, insulin resistance, and fibrosis in mice, while reintroduction of TFEB restored these effects. We identified Bya directly bound to MET370 and PHE552 of FLCN (folliculin), suppressing the function of the FLCN-FNIP1 (folliculin interacting protein 1)/FNIP2 complex, which in turn inhibited MTORC1-mediated cytoplasmic sequestration of TFEB. Mutation of FLCN (M370A and F552A) in the liver abolished Bya-induced protection against MASH. Thus, Bya is a promising therapeutic natural compound for MASH, and selective inhibition of MTORC1 is a potential approach to treat this disease. aa, amino acids; AAV, adeno-associated virus; Bio, biotin; Bio-Bya, biotin-conjugated Bya; BSA, bovine serum albumin; BW, body weight; Bya, byakangelicin; CETSA, cellular thermal shift assay; CHIP-atlas, chromatin immunoprecipitation atlas; C, maximum concentration; CQ, chloroquine; DARTS; drug affinity responsive target stability assay; EIF4EBP1/4E-BP1, eukaryotic translation initiation factor 4E binding protein 1; FBS, fetal bovine serum; FDA, food and drug administration; FIMO-JASPAR, find individual motif occurrences-JASPAR; FLCN, folliculin; FNIP1, folliculin interacting protein 1; GAP, GTPase-activating protein; GOT1/AST, glutamic-oxaloacetic transaminase 1; GPT/ALT, glutamic-pyruvic transaminase; GTRD, gene transcription regulatory database; GTT, glucose tolerance test; H&E, hematoxylin and eosin; Hbonds, hydrogen bonds; HFD, high-fat diet; HFHC, high-fat and high-cholesterol; HOMA-IR, homeostatic model assessment of insulin resistance; HSCs, hepatic stellate cells; IP, immunoprecipitation; ITT, insulin tolerance test; K, dissociation constant; KEGG, kyoto encyclopedia of genes and genomes; KPBS, potassium phosphate-buffered saline; LC-MS/MS, liquid chromatography-tandem mass spectrometry; LW/BW, liver-to-body weight ratio; MAP1LC3/LC3, microtubule associated protein 1 light chain 3; MASH, metabolic dysfunction-associated steatohepatitis; MASLD, metabolic dysfunction-associated steatotic liver disease; MCD, methionine and choline deficient; MST, microscale thermophoresis assay; MTOR, mechanistic target of rapamycin kinase; MTORC1, MTOR complex 1; ND, normal diet; NFKB/NF-κB, nuclear factor kappa B; NFKBIA/IKBA, NFKB inhibitor alpha; OP, oleate acid and palmitate acid; PBS, phosphate-buffered saline; PCA, principal component analysis; qRT-PCR, real-time quantitative PCR; RELA/p65, RELA proto-oncogene, NF-kB subunit; Res, resmetirom; Rg, radius of gyration; RMSD, root-mean-square deviation; RMSF, root-mean-square fluctuation; RPS3, ribosomal protein S3; RPS6KB1/S6K1, ribosomal protein S6 kinase B1; RRAGC, ras related GTP binding C; SASA, solvent-accessible surface area; SNRPD2, small nuclear ribonucleoprotein D2 polypeptide; SQSTM1/p62, sequestosome 1; T, half-life; TFE3, transcription factor binding to IGHM enhancer 3; TFEB, transcription factor EB; TMEM192, transmembrane protein 192; VIM, vimentin; WT, wild-type. - Source: PubMed
Publication date: 2026/05/25
Du XiliangFang ZhiyuanLiu GuowenWang LiJu LingxueGao WenwenSong YuxiangLei LinLi Xinwei - Cardiac fibrosis is a defining pathological feature of diabetic cardiomyopathy (DCM), and excessive activation of cardiac fibroblasts plays a critical role in regulating cardiomyocyte function through paracrine signaling. CCN1 (cellular communication network factor 1), an extracellular matrix protein involved in intercellular communication, has been suggested to influence cardiac remodeling, although its specific impact on cardiomyocytes in DCM has remained unclear. In this study, we found that CCN1 expression was markedly elevated in cardiac tissues from DCM mouse models and in insulin-resistant cell models, with fibroblasts serving as the primary source. Proteomic analysis and co-culture experiments demonstrated that CCN1 suppressed cardiomyocyte macroautophagy/autophagy. To determine its role in vivo, we generated fibroblast-specific knockout mice and established a DCM model, demonstrating that deletion ameliorated cardiac dysfunction and restored autophagic activity. We further identified ITGAV-ITGB1/integrin αvβ1 as the receptor mediating CCN1 signaling in cardiomyocytes. Molecular dynamics simulations and co-immunoprecipitation experiments confirmed that CCN1 engaged ITGAV-ITGB1/integrin αvβ1 through its cysteine-knot-containing (CT) domain. Mechanistically, this interaction activated the downstream PTK2/FAK-MTOR signaling pathway, leading to inhibition of cardiomyocyte autophagy. Together, these findings reveal a previously unrecognized fibroblast-cardiomyocyte signaling axis in which fibroblast-derived CCN1 drives DCM progression by suppressing autophagy through ITGAV-ITGB1/integrin αvβ1-dependent signaling. This work provides mechanistic insight into the pathogenesis of DCM and identifies CCN1 as a potential therapeutic target for mitigating disease onset and progression.: AAV9: adeno-associated virus serotype 9; ADGRE1/EMR1/F4/80: adhesion G protein-coupled receptor E1; BafA1: bafilomycin A; BSA: bovine serum albumin; C8: compound 8; CCN1: cellular communication network factor 1; CF: cardiac fibroblast; CSA: cross-sectional area; DCM: diabetic cardiomyopathy; EIF4EBP1: eukaryotic translation initiation factor 4E binding protein 1; ELISA: enzyme-linked immunosorbent assay; HE: hematoxylin and eosin; HFD: high-fat diet; HG: high glucose; IR: insulin resistance; MAP1LC3/LC3: microtubule associated protein 1 light chain 3; MD: molecular dynamics; MTOR: mechanistic target of rapamycin kinase; NRCM: neonatal rat cardiomyocyte; PDGFRA: platelet derived growth factor receptor alpha; PECAM1/CD31: platelet and endothelial cell adhesion molecule 1; PTK2/FAK: protein tyrosine kinase 2; PTPRC/CD45: protein tyrosine phosphatase receptor type C; RPS6KB1: ribosomal protein S6 kinase B1; S100A4/FSP1: S100 calcium binding protein A4; SQSTM1/p62: sequestosome 1; STZ: streptozotocin; TUNEL: terminal deoxynucleotidyl transferase-mediated dUTP-biotin nick end labeling; WGA: wheat germ agglutinin. - Source: PubMed
Publication date: 2026/05/07
Hu Bo-AngZhang LeiSong MingKong Yan-RuJiao Ya-QiongJia XuZhu PingLi Yu-LinTi YunZhang WeiWang Zhi-HaoZhong Ming - Breast cancer (BC) is a complex illness that affects millions of women globally. As its incidence rises, new treatment strategies are needed. Veratrum viride, a traditional medicinal herb, is known for its therapeutic potential, yet its molecular mechanism of action against BC remains unclear. The purpose of this preliminary investigation is to assess V. viride's anti-breast cancer potential by identifying its active compounds and using bioinformatics techniques to clarify their multi-target mechanisms. - Source: PubMed
Publication date: 2026/04/01
Eswaran Anu PriyaJayaraman SelvarajNatarajan Sathan RajVeeraraghavan Vishnu Priya - Angiosarcomas are very rare, malignant tumors of the endothelial lining of blood vessels and most present cutaneously, while only 10% present as deep soft tissue angiosarcomas. Literature is sparse regarding secondary deep soft tissue angiosarcoma, especially in cases that have formed surrounding a foreign body such as orthopedic implants. - Source: PubMed
Publication date: 2026/03/17
Morales Pocholo Iñigo BHobusch GerhardFunovics PhilippClodi NikolausScharrer AnkeWindhager Reinhard