2_Amino_3_methyl_3_sulfino_4_(1H_1,2,3_t Tazobactam related co
- Known as:
- 2_Amino_3_methyl_3_sulfino_4_(1H_1,2,3_t Tazobactam related co
- Catalog number:
- 118175-11-4
- Product Quantity:
- 1g
- Category:
- -
- Supplier:
- chemotra
- Gene target:
- 2_Amino_3_methyl_3_sulfino_4_(1H_1 2 3_t Tazobactam related
Related genes to: 2_Amino_3_methyl_3_sulfino_4_(1H_1,2,3_t Tazobactam related co
- Gene:
- MAPK4 NIH gene
- Name:
- mitogen-activated protein kinase 4
- Previous symbol:
- PRKM4
- Synonyms:
- Erk3-related, Erk4
- Chromosome:
- 18q21.1-q21.2
- Locus Type:
- gene with protein product
- Date approved:
- 1993-11-08
- Date modifiied:
- 2018-02-13
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CAS: 263900-32-9 Formula: C14H30O4Si(+)_2_[4_[(isobut_2_enyl)amino]phenyl]pro (+)_2_[4_[(isobut_2_enyl)(+)_4,5_Bis[hydroxy(diphenyl)methyl]_2_m (+)_4,5_Bis[hydroxy(dip Related articles to: 2_Amino_3_methyl_3_sulfino_4_(1H_1,2,3_t Tazobactam related co
- The parasite Leishmania resides as amastigotes within the macrophage parasitophorous vacuoles inflicting the disease Leishmaniasis. Leishmania selectively modulates mitogen-activated protein kinase (MAPK) phosphorylation subverting CD40-triggered anti-leishmanial functions of macrophages. The mechanism of any pathogen-derived molecule induced host MAPK modulation remains poorly understood. Herein, we show that of the fifteen MAPKs, LmjMAPK4 expression is higher in virulent L. major. LmjMAPK4- detected in parasitophorous vacuoles and cytoplasm- binds MEK-1/2, but not MKK-3/6. Lentivirally-overexpressed LmjMAPK4 augments CD40-activated MEK-1/2-ERK-1/2-MKP-1, but inhibits MKK3/6-p38MAPK-MKP-3, phosphorylation. A rationally-identified LmjMAPK4 inhibitor reinstates CD40-activated host-protective anti-leishmanial functions in L. major-infected susceptible BALB/c mice. These results identify LmjMAPK4 as a MAPK modulator at the host-pathogen interface and establish a pathogen-intercepted host receptor signaling as a scientific rationale for identifying drug targets. - Source: PubMed
Publication date: 2024/05/09
Kumari SangeetaBodhale NeelamSarode AdityaJha Mukesh KumarBhadange SagarPandey Surya PrakashSelvaraj SathishkumarChande Ajit GMukhopadhyaya RobinGhosh Soumya KantiSingh ShailzaMukherjee DebasriDuffin RebekahAndrews PhilipSaha Bhaskar - The exosome-mediated extracellular secretion of miRNAs occurs in many cancers, and RAB27A is a potent regulator of exosome secretion. For metastatic renal cell carcinoma (RCC), this study examines the mechanisms of cancer metastasis via the RAB27A-regulated secretion of specific miRNAs. - Source: PubMed
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Song Dae HyunLee Jong SilLee Jeong-HeeKim Dong ChulYang Jung WookKim Min HyeNa Ji MinCho Hyun-KyungYoo JiyunAn Hyo Jung - 17-Estradiol (E2), an important endocrine hormone in the mammalian body, participates in the regulation of the physiological functions of the reproductive system, mammary glands, bone, and cardiovascular system, among others. Paradoxically, despite the physiological actions of endogenous E2 (0.2-1.0 nmol/L), numerous clinical and experimental studies have demonstrated that high-dose E2 treatment can cause tumor regression and exert pro-apoptotic actions in multiple cell types; however, the underlying mechanism remains undescribed. In particular, little information of the cellular processes responding to the lethality of E2 is available. In the present study, we attempted to characterize the cellular processes responding to high-dose (μmol/L) E2 treatment using quantitative phosphoproteomics to obtain a better understanding of the regulatory mechanism of E2-induced cell death. First, the cell phenotype induced by high-dose E2 was determined by performing Cell Counting Kit-8 assay (CCK8), cell cytotoxicity analysis by trypan blue staining, and microscopic imaging on HeLa cells treated with 1-10 μmol/L E2 or dimethyl sulfoxide (DMSO) for 1-3 d. E2 inhibited cell proliferation and induced cell death in a dose- and time-dependent manner. Compared with the DMSO-treated HeLa cells, the cells treated with 5 μmol/L E2 for 2 d demonstrated >74% growth inhibition and approximately 50% cell death. Thus, these cells were used for quantitative phosphoproteomic analysis. Next, a solid-phase extraction (SPE)-based immobilized titanium ion affinity chromatography (Ti-IMAC) phosphopeptide-enrichment method coupled with data-independent acquisition (DIA)-based quantitative proteomics was employed for the in-depth screening of high-dose E2-regulated phosphorylation sites to investigate the intracellular processes responding to high-dose E2 treatment. Liquid chromatography-tandem mass spectrometry (LC-MS/MS) identified over 10000 phosphorylation sites regulated by E2 and DMSO in HeLa cells. In comparison with the DMSO-treated cells, the cells treated with 5 μmol/L E2 showed 537 upregulated phosphorylation sites and 387 downregulated phosphorylation sites, with a threshold of <0.01 and |log(fold change)|≥1. A total of 924 phosphorylation sites on 599 proteins were significantly regulated by high-dose E2, and these sites were subjected to enrichment analysis. In addition, 453 differently regulated phosphorylation sites on 325 proteins were identified only in the E2- or DMSO-treated cell samples. These phosphorylation sites may be phosphorylated or dephosphorylated in response to high-dose E2 stimulation and were subjected to parallel enrichment analyses. Taken together, 1218 phosphorylation sites on 741 proteins were significantly regulated by high-dose E2 treatment. The functional phosphoproteins in these two groups were then analyzed using Gene Ontology (GO) and Gene Set Enrichment Analysis (GSEA) to determine the biological processes in which they participate and the Kyoto Encyclopedia of Genes and Genomes (KEGG) pathway database. Consistent with the cell-phenotype data, cell cycle-related proteins were highly enriched in the two groups of E2-regulated phosphoproteins (<0.05), indicating that high-dose E2 treatment can regulate cell proliferation. In addition, E2-regulated phosphoproteins were highly enriched in the cellular processes of ribosome biogenesis, nucleocytoplasmic transport, and messenger ribonucleic acid (mRNA) processing/splicing (<0.05), indicating that the activation of these processes may contribute to high-dose E2-induced cell death. These results further confirm that high-dose E2 treatment inhibits protein translation and induces cell death. Furthermore, the significant upregulation of multiple phosphorylation sites associated with epidermal growth factor receptor (EGFR) and mitogen-activated protein kinases (MAPKs) MAPK1, MAPK4, and MAPK14 by high-dose E2 indicates that the EGFR and MAPK signaling pathways are likely involved in the regulation of E2-induced cell death. These phosphorylation sites likely play vital roles in E2-induced cell death in HeLa cells. Overall, our phosphoproteomic data could be a valuable resource for uncovering the regulatory mechanisms of E2 in the micromolar range. - Source: PubMed
Li YananLiu XiaoyanWang YanLiu ZhenYe MingliangWang Hailin - Caffeine has been extensively studied in the context of CNS pathologies as many researchers have shown that consuming it reduces pro-inflammatory biomarkers, potentially delaying the progression of neurodegenerative pathologies. Several lines of evidence suggest that adenosine receptors, especially A and AA receptors, are the main targets of its neuroprotective action. We found that caffeine pretreatment 15 min before LPS administration reduced the expression of Il1b in the hippocampus and striatum. The harmful modulation of caffeine-induced inflammatory response involved the downregulation of the expression of AA receptors, especially in the hippocampus. Caffeine treatment alone promoted the downregulation of the adenosinergic receptor Adora2A; however, this promotion effect was reversed by LPS. Although administering caffeine increased the expression of the enzymes DNA methyltransferases 1 and 3A and decreased the expression of the demethylase enzyme Tet1, this effect was reversed by LPS in the hippocampus of mice that were administered Caffeine + LPS, relative to the basal condition; no significant differences were observed in the methylation status of the promoter regions of adenosine receptors. Finally, the bioinformatics analysis of the expanded network demonstrated the following results: the Adora2B gene connects the extended networks of the adenosine receptors Adora1 and Adora2A; the Mapk3 and Esr1 genes connect the extended Adora1 network; the Mapk4 and Arrb2 genes connect the extended Adora2A network with the extended network of the proinflammatory cytokine Il1β. These results indicated that the anti-inflammatory effects of acute caffeine administration in the hippocampus may be mediated by a complex network of interdependencies between the Adora2B and Adora2A genes. - Source: PubMed
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Lemes Dos Santos Sanna PaulaBernardes Carvalho LiebertCristina Dos Santos Afonso Camilade Carvalho KassiaAires RogérioSouza JennyfferRodrigues Ferreira MarcelBirbrair AlexanderMartha Bernardi MariaLatini AlexandraFoganholi da Silva Rodrigo A - Breast cancer (BC) is a common gynaecological malignancy worldwide. Long noncoding RNAs (lncRNAs) were identified to take part in the regulation of the occurrence and development of tumors. LncRNA The role of LINC00467 in lung adenocarcinoma has been reported, but its mechanism remains unclear in BC. To explore the role of LINC00467 deeply, we designed and performed a series of experiments. According to the result, it was discovered that LINC00467 was overexpressed in BC tissues and cells, and then the knockdown of LINC00467 resulted in a decline in cell growth and metastasis. Mechanistically, miR-18a/b-5p was screened out and validated to bind with LINC00467. Additionally, LINC00467 was negatively correlated with miR-18a/b-5p. Hereafter, there is evidence that miR-18a/b-5p targets MAPK4. Rescue assays suggested that MAPK4 amplification recovered the inhibitive effect of LINC00467 knockdown on cell growth and metastasis. In a word, LINC00467 enhanced BC cell growth and metastasis by targeting miR-18a/b-5p/MAPK4, which implies a potential revelation for exploring the therapeutic tactic of BC. - Source: PubMed
Publication date: 2023/12/20
Zhang ZhitaoLan HuanZhao Shuai