Ask about this productRelated genes to: MAPK1 antibody
- Gene:
- MAPK1 NIH gene
- Name:
- mitogen-activated protein kinase 1
- Previous symbol:
- PRKM2, PRKM1
- Synonyms:
- ERK, ERK2, p41mapk, MAPK2
- Chromosome:
- 22q11.22
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-05
- Date modifiied:
- 2019-04-23
Related products to: MAPK1 antibody
Related articles to: MAPK1 antibody
- WIN55,212-2, a non-selective cannabinoid receptor agonist, was investigated for its protective effects and underlying mechanisms in a sepsis-induced pulmonary fibrosis (SIPF) mouse model. In vivo experiments demonstrated that WIN55,212-2 effectively attenuates pulmonary inflammation and fibrosis. Integration with network pharmacology analyses further revealed a multi-target, multi-pathway mechanism of action, providing a theoretical framework for its potential clinical application and targeted therapeutic strategies. In this study, a cecal ligation and puncture (CLP)-induced SIPF model was established in mice. WIN55,212-2 markedly alleviated CLP-induced lung injury, as evidenced by improved alveolar architecture, reduced inflammatory cell infiltration, and decreased collagen deposition. Histological analyses confirmed restoration of lung morphology, while immunofluorescence demonstrated reduced collagen I expression. At the molecular level, WIN55,212-2 suppressed pro-inflammatory cytokines (IL-1β, IL-6, and TNF-α) and enhanced anti-inflammatory and reparative mediators (IL-10 and TGF-β). Furthermore, it downregulated fibrosis markers (α-SMA, vimentin, and collagen I) and inhibited activation of the RAGE signaling axis and its downstream effectors, including phosphorylated JAK2, STAT1, PI3K, and JNK. CB1 or CB2 antagonists effectively reverse the effects of WIN55,212-2. Network pharmacology analysis indicated that WIN55,212-2 modulates multiple inflammation- and fibrosis-associated pathways, with key targets such as TP53, TLR4, MAPK1, and PIK3R1, supporting a synergistic, multi-target mode of action. Collectively, these findings suggest that WIN55,212-2 mitigates SIPF progression through coordinated regulation of multiple molecular targets and pathways, highlighting its potential as a therapeutic candidate and providing a basis for future translational and targeted intervention strategies. - Source: PubMed
Publication date: 2026/05/25
He QuanYang Dei-XingDuo LinShi Tong-LingYang Yuan-WeiLi Jie-ChengLi Shu-TingZhu Shang-Shang - Alkaloids are the primary active ingredients of various traditional Chinese medicines. Preclinical studies show they possess anti-inflammatory, antioxidant, and anti-fibrotic effects in pulmonary fibrosis (PF) models. - Source: PubMed
Publication date: 2026/05/27
Wang HualingLiu XinyuZeng YiJiang JunCao XiyuMa JianliHu QiongyingZhang Chuantao - Kaposi's sarcoma (KS) is an angioproliferative malignancy caused by Kaposi's sarcoma-associated herpesvirus (KSHV), characterized by aberrant angiogenesis, chronic inflammation, and endothelial cell transformation. Given the multi-factorial nature of KS pathogenesis, strategies that simultaneously modulate multiple mo-lecular targets are considered more promising than single-target approaches. However, effective multi-target therapeutic agents for KS remain limited, prompting this study to employ an integrative in silico pipeline. An integrative in silico pipeline combining compound screening, target predic-tion, network pharmacology, Gene Ontology (GO) and Kyoto Encyclopedia of Genes and Ge-nomes (KEGG) enrichment, protein-protein interaction (PPI) analysis, molecular docking, and molecular dynamics (MD) simulations was employed. Streptomyces-derived metabolites were prioritized based on chemical diversity, annotation, and clinical prece-dent. Predicted targets were intersected with KS-associated genes, with hubs ranked by network topology. Docking and MD simulations evaluated binding affinity and stability. Endostemonine I emerged as the top candidate, engaging nine of ten hub proteins, including EGFR, mTOR, PTGS2, SRC, PARP1, PPARγ, MAPK1, MAPK14, and ICAM1. Key nodes such as mTOR, PTGS2, PPARγ, and MAPK14 are central to KS-related an-gi-ogenesis, inflammation, and viral oncogenesis. GO and KEGG analyses revealed en-richment in kinase activity, cell adhesion, and PI3K-Akt/mTOR and MAPK signaling pathways. Docking indicated strong binding to mTOR, PTGS2, PARP1, PPARγ, and MAPK14, while MD simulations confirmed stable interactions for mTOR, PTGS2, PPARγ, and MAPK14. Collectively, these proteins represent high-confidence, druggable KS targets, with Endostemonine I as a promising multi-target scaffold. These findings highlight the therapeutic potential of Endostemonine I and warrant further validation through future in vitro and in vivo studies. - Source: PubMed
Publication date: 2026/05/04
Sama-Ae ImranDaloh MollayaTedasen AmanChangrob SirirukLertcanawanichakul MonthonKwankaew PattamapornIssaro PhenphitchaMaidam NatthanichaRattanapong NichakanAuma NurulKaseng MirfartTayeh Malatee - To investigate the mechanism of cephaeline for suppressing malignant biological behaviors of colorectal cancer (CRC). - Source: PubMed
Han LiangLi BaichaoWang BingzheZhang ZhiweiZhang Jiuna - Dual-specificity protein phosphatases (DUSPs) are key modulators of mitogen-activated protein kinase (MAPK) signaling pathways that regulate cellular proliferation, differentiation, and stress adaptation. Although extensively characterized in higher eukaryotes, the functional roles of DUSPs in Leishmania remain poorly understood. In this study, we investigated the function of an atypical dual-specificity phosphatase/kinatase (LINF_340027100) in Leishmania infantum using CRISPR/Cas9-mediated genome editing. Repeated attempts to generate DUSP-null mutants were unsuccessful, and episomal complementation prior to chromosomal disruption did not permit deletion of the endogenous locus, suggesting that DUSP is essential for promastigote viability. To investigate DUSP function, we generated parasite lines with altered gene expression, including a heterozygous knockout (Li DUSP+/-) and an episomal overexpressor (Li WT + pIR1_SAT-DUSP). Modulation of DUSP expression resulted in pronounced alterations in parasite morphology, cell-cycle progression, differentiation, and intracellular proliferation in macrophages. The Li DUSP+/- line exhibited a twofold reduction in transcript abundance and maintained normal growth kinetics, but displayed elongated morphology, increased flagellar length, and a reduced G0/G1 population with concomitant S-phase accumulation. In addition, Li DUSP+/- parasites showed decreased tolerance to hydrogen peroxide, being 1.5- and 5.7-fold more sensitive in promastigote and intracellular amastigote forms, respectively. Conversely, the DUSP-overexpressing line exhibited a 2.3-fold increase in DUSP transcript levels, accompanied by modest impairment of promastigote proliferation, rounded morphology, altered cell-cycle distribution, and increased resistance to trivalent antimony, with 2.6- and 3.1-fold higher resistance observed in promastigote and intracellular amastigote forms, respectively. Both mutant lines showed reduced intracellular proliferation at 72 h post-infection. Transcript level analysis revealed altered expression of MAPK1, MAPK3, and MAPK10 in both promastigote and axenic amastigote-like forms, supporting a functional link between DUSP activity and MAPK signaling homeostasis. Together, these findings identify DUSP as a key regulator of parasite biology that integrates MAPK signaling with oxidative stress response, differentiation, and antimony susceptibility in L. infantum. This study provides the first functional characterization of this atypical DUSP/kinatase in Leishmania and highlights its potential as a target for therapeutic intervention. - Source: PubMed
Publication date: 2026/05/26
Ribeiro Juliana MartinsFonseca Giovanna Ferreira daAnbo Milena Airi KimuraCosta Karla FerreiraOliveira Amanda Cristina Silva deLopes Karine FerreiraCruz Mariza Gabriela Faleiro de Moura LodiCosta-Silva Héllida MarinaSanti Ana Maria MurtaMurta Silvane Maria Fonseca