RhoA Antibody
- Known as:
- RhoA Antibody
- Catalog number:
- abx000657
- Product Quantity:
- EUR
- Category:
- -
- Supplier:
- Abbexa
- Gene target:
- RhoA Antibody
Related genes to: RhoA Antibody
- Gene:
- RHOA NIH gene
- Name:
- ras homolog family member A
- Previous symbol:
- ARH12, ARHA
- Synonyms:
- RhoA, Rho12, RHOH12
- Chromosome:
- 3p21.31
- Locus Type:
- gene with protein product
- Date approved:
- 1990-03-19
- Date modifiied:
- 2019-04-23
Related products to: RhoA Antibody
Related articles to: RhoA Antibody
- Oxidative stress, a pervasive cancer vulnerability, remains a challenging therapeutic target attributed to tumor heterogeneity and adaptive resistance. Herein, we identify RhoA as a "redox rheostat" during oncolytic virotherapy through regulating mitochondrial dynamics, thereby addressing this bottleneck to enable pan-cancer therapy via oxidative-oncolytic synergy. Engineering oncolytic virus to express RhoA (rNDV-RHOA) elicits robust oxidative mitophagic cell death with inherent tumor selectivity and demonstrates superior oncolysis in a comprehensive panel of preclinical cancer models spanning in vitro, ex vivo, and in vivo settings, including models evaluated under intravenous administration. The construct exhibits favorable safety profiles without inducing seroconversion, facilitating repeated systemic dosing. Mechanistically, RhoA drives mitochondrial fission to impair mitochondrial Complex III, initiating oxidative stress while tempering it via mitophagy induction downstream of Akt/mTOR inhibition. Concurrently, viral infection serves as the decisive precipitating event that shifts the cellular response from adaptive mitophagy to mitochondrial catastrophe by enhancing Complex I and V activities to promote ATP biosynthesis, thereby culminating in acute cell death characterized by a precipitous decline in mitochondrial mass and ATP bioavailability. This establishes rNDV-RHOA as an oncolytic virotherapy platform that transcends conventional oncolysis to surmount tumor heterogeneity by exploiting inherent tumor redox dependency. - Source: PubMed
Publication date: 2026/08/19
Feng ShufengCui LuZhu YongxinCheng YaoDiao DongmeiLi XuefengDuan HuiminZhang HaixiaLiu XiaoxiaoPan QingJi FanpuZhang YuOu ChangboLi Hai - The anterior pituitary integrates endocrine regulation, cellular growth, and adaptive responses. Adipokines, secreted mainly by adipose tissue, act as hormonal signals linking metabolism, inflammation, appetite, and reproduction. They regulate hypothalamic-pituitary-ovarian axis by modulating hormone secretion and intracellular signaling. The presence of adipokine receptors in anterior pituitary suggests local metabolic-endocrine interactions. Omentin-1, predominantly expressed in visceral adipose tissue, participates in glucose metabolism and ovarian steroid regulation. Recent findings indicate that omentin-1 modulates tropic hormones, their receptors, and adipokine balance in anterior pituitary cells. We hypothesized that omentin-1 affects protein expression and signaling pathways involved in pituitary cell proliferation and apoptosis. This study examined its effects in anterior pituitary cells from Large White and Meishan pigs. Proteomic analysis identified 230 candidate differentially abundant proteins after omentin-1 treatment: 30 downregulated and 3 upregulated in Large White pigs, and 107 downregulated and 90 upregulated in Meishan pigs, associated with enriched 116 Gene Ontology terms. Key proteins were associated with cell cycle, DNA replication, gene expression, and posttranscriptional/posttranslational regulation. Responses differed between breeds. CDK5RAP2 and SIX1 were linked to proliferative control in Large White pigs, whereas AKT1S1 and RHOA were among the proteins associated with the broader proteomic response observed in Meishan pigs. Meishan pigs showed dynamic apoptotic protein regulation, including HTRA2, PARP2, and DFFA. Complementary in vitro experiments demonstrated that omentin-1 downregulated cyclins and caspase-3, upregulated BCL2, increased BCL2/BAX ratio, and modulated ERK1/2, AKT, AMPKα, and STAT3 phosphorylation. Together, these findings suggest that omentin-1 modulates proteomic networks and intracellular signaling associated with anterior pituitary cell function during the mid-luteal phase of the estrous cycle. - Source: PubMed
Publication date: 2026/08/19
Respekta-Długosz NataliaKubicka KarolinaGreggio AleksandraŚwiderska BiankaMalinowska AgataRytelewska EdytaOpydo MałgorzataDupont JoëlleKamiński TadeuszSmolińska NinaRak Agnieszka - Endoplasmic reticulum (ER)-phagy receptors have elusive physiological functions beyond ER remodeling. To gain insight into these, we screen for cytoplasmic interactors of well-known receptors in mouse pancreatic ductal adenocarcinoma cells. Our data subsequently reveal a non-canonical action of PRKAR1A, a subunit of protein kinase A (PKA), in binding and activating FAM134B/C. At a molecular level, an amphipathic helix in the otherwise-disordered C terminus of FAM134B directly binds PRKAR1A dimers. Multimodal imaging reveals that this interaction occurs at interorganellar contact sites between the ER and liquid-like condensates of PRKAR1A. Mechanistically, ER-condensate contacts promote clustering of FAM134B/C with LC3B and recruit lysosomes, forming degradation hubs. Unexpectedly, these structures are found to control cytoplasmic signaling through FAM134B/C-mediated lysosomal sequestration of RhoA. Underscoring the physiologic relevance of this, these cytoplasmic-facing actions of FAM134B/C result in RhoA-dependent cell morphologic and migratory control in response to cyclic AMP (cAMP) stimuli. Thus, interorganellar contacts expand the roles of FAM134B/C ER-phagy receptors beyond ER degradation. - Source: PubMed
Publication date: 2026/08/17
Jimenez-Moreno NataliaKarageorgiou AriannaWinnington-Ingram KatieWills JimiPednekar ChinmayiOverhoff MelinaPaine KatherinePearson MatthewGerasimavicius LukasWheeler AnnKononenko Natalia LMarsh Joseph AVerkade Paulvon Kriegsheim AlexLane Jon DWilkinson Simon - Fuchs endothelial corneal dystrophy (FECD) involves pathological extracellular matrix (ECM) accumulation within Descemet's membrane, leading to guttae formation, endothelial dysfunction, and vision impairment. As current treatment is primarily surgical, we investigated whether Rho-associated protein kinase (ROCK) inhibition can reduce fibrotic ECM remodeling in FECD and related corneal endothelial diseases. - Source: PubMed
Schlötzer-Schrehardt UrsulaZenkel MatthiasPulasani SaiStrunz MariaGießl AndreasEkici ArifOkumura NaokiKoizumi NorikoKinoshita ShigeruTourtas TheofilosKruse Friedrich E - Peste des petits ruminants (PPR) is an acute, severe, and highly contagious disease caused by peste des petits ruminants virus (PPRV), which primarily induces tissue damage through the formation of syncytia. Therefore, elucidating the molecular mechanism underlying PPRV-induced syncytium formation is of critical importance. In this study, we generated Vero CCL-81 cell lines stably expressing the PPRV receptors SLAM (lymphocytic) or Nectin-4 (epithelial) and further found that PPRV infection significantly induced syncytium formation in these cell lines as well as in goat mammary epithelial cells (GMECs) and ovine rumen epithelial cells (ORECs). Furthermore, the viral H and F proteins served as the pivotal determinants of syncytium formation. More importantly, we discovered that PPRV-induced syncytium formation is dependent on the RhoA-Rock1 signaling pathway and that inhibition of syncytium formation markedly suppressed PPRV replication. Collectively, our findings provide novel insights into the molecular mechanism of PPRV-induced syncytium formation, offer theoretical references for the development of new antiviral strategies, and advance the scientific eradication of PPR. - Source: PubMed
Publication date: 2026/08/04
Li WeiWang HongnuanSong ChenyuPang RongYin HanweiLiu MengyuanYang XiaozhuSun ZilongZhang DingWang JingyuWen BoYang Bo