CLIA kit Cytosolic malate dehydrogenase,Malate dehydrogenase, cytoplasmic,Mdh,Mdh1,Rat,Rattus norvegicus
- Known as:
- CLIA reagent Cytosolic malate dehydrogenase,Malate dehydrogenase, cytoplasmic,Mdh,Mdh1,Rat,Rattus norvegicus
- Catalog number:
- U2124r
- Product Quantity:
- 96T
- Category:
- -
- Supplier:
- EIAab
- Gene target:
- CLIA kit Cytosolic malate dehydrogenase Malate cytoplasmic Mdh Mdh1 Rat Rattus norvegicus
Ask about this productRelated genes to: CLIA kit Cytosolic malate dehydrogenase,Malate dehydrogenase, cytoplasmic,Mdh,Mdh1,Rat,Rattus norvegicus
- Gene:
- MDH1 NIH gene
- Name:
- malate dehydrogenase 1
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 2p15
- Locus Type:
- gene with protein product
- Date approved:
- 2001-06-22
- Date modifiied:
- 2016-10-05
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- The liver is the main organ associated with metabolism. In our previous studies, we identified that the metabolic enzymes malate dehydrogenase 1 (MDH1) and isocitrate dehydrogenase 1 (IDH1) were differentially expressed in ALF. The aim of this study was to explore the changes in the acetylation of MDH1 and IDH1 and the therapeutic effect of histone deacetylase (HDAC) inhibitor in acute liver failure (ALF). Decreased levels of many metabolites were observed in ALF patients. MDH1 and IDH1 were decreased in the livers of ALF patients. The HDAC inhibitor ACY1215 improved the expression of MDH1 and IDH1 after treatment with MDH1-siRNA and IDH1-siRNA. Transfection with mutant plasmids and adeno-associated viruses, identified MDH1 K118 acetylation and IDH1 K93 acetylation as two important sites that regulate metabolism and . - Source: PubMed
Publication date: 2024/04/06
Shi ChunxiaZhang YanqiongChen QianWang YukunZhang DanmeiGuo JinZhang QingqiZhang WenbinGong Zuojiong - Adaptation to chronic hypoxia occurs through changes in protein expression, which are controlled by hypoxia-inducible factor 1α (HIF1α) and are necessary for cancer cell survival. However, the mechanisms that enable cancer cells to adapt in early hypoxia, before the HIF1α-mediated transcription programme is fully established, remain poorly understood. Here we show in human breast cancer cells, that within 3 h of hypoxia exposure, glycolytic flux increases in a HIF1α-independent manner but is limited by NAD availability. Glycolytic ATP maintenance and cell survival in early hypoxia rely on reserve lactate dehydrogenase A capacity as well as the activity of glutamate-oxoglutarate transaminase 1 (GOT1), an enzyme that fuels malate dehydrogenase 1 (MDH1)-derived NAD. In addition, GOT1 maintains low α-ketoglutarate levels, thereby limiting prolyl hydroxylase activity to promote HIF1α stabilisation in early hypoxia and enable robust HIF1α target gene expression in later hypoxia. Our findings reveal that, in normoxia, multiple enzyme systems maintain cells in a primed state ready to support increased glycolysis and HIF1α stabilisation upon oxygen limitation, until other adaptive processes that require more time are fully established. - Source: PubMed
Publication date: 2024/03/14
Grimm FionaAsuaje AgustínJain AakritiSilva Dos Santos MarianaKleinjung JensNunes Patrícia MGehrig StefanieFets LouiseDarici SalihanurMacRae James IAnastasiou Dimitrios - Glutathione (GSH) depletion, mitochondrial damage, and oxidative stress have been implicated in the pathogenesis of acetaminophen (APAP) hepatotoxicity. Here, we demonstrated that the expression of histone deacetylase 6 (HDAC6) is highly elevated, whereas malate dehydrogenase 1 (MDH1) is downregulated in liver tissues and AML-12 cells induced by APAP. The therapeutic benefits of LT-630, a novel HDAC6 inhibitor on APAP-induced liver injury, were also substantiated. On this basis, we demonstrated that LT-630 improved the protein expression and acetylation level of MDH1. Furthermore, after overexpression of MDH1, an upregulated NADPH/NADP ratio and GSH level and decreased cell apoptosis were observed in APAP-stimulated AML-12 cells. Importantly, MDH1 siRNA clearly reversed the protection of LT-630 on APAP-stimulated AML-12 cells. In conclusion, LT-630 could ameliorate liver injury by modulating MDH1-mediated oxidative stress induced by APAP. - Source: PubMed
Publication date: 2024/03/13
Zhang Guo-DongWang Li-LiZheng LingWang Shi-QiYang Rong-QuanHe Yu-TingWang Jun-WeiZhao Ming-YuDing YiLiu MeiYang Tian-YuWu Bao-MingCui HaoZhang Lei - Intramuscular fat (IMF) content and its fatty acid (FA) composition are typically controlled by several genes, each with a small effect. In the current study, to pinpoint candidate genes and putative regulators involved in FA composition, we performed a multivariate integrative analysis between intramuscular FA and transcriptome profiles of porcine longissimus dorsi (LD) muscle. We also carried out a combination of network, regulatory impact factor (RIF), in silico prediction of putative target genes, and functional analyses to better support the biological relevance of our findings. - Source: PubMed
Publication date: 2024/02/12
Valdés-Hernández JesúsFolch Josep MCrespo-Piazuelo DanielPassols MagíSebastià CristinaCriado-Mesas LourdesCastelló AnnaSánchez ArmandRamayo-Caldas Yuliaxis - Natural honey contains glycoconjugates as minor components. We characterized acacia honey glycoconjugates with molecular masses in the range of 2-5 kDa. The glycoconjugates were separated by RP-HPLC into three peaks (termed RP-2-5 k-I, RP-2-5 k-II, and RP-2-5 k-III) which demonstrated paralyzing effects on the model nematode C. elegans (ED of 50 ng glycoconjugates/μL). To examine molecular mechanisms underlying the nematicidal effects of honey glycoconjugates, expressional analyses of genes that are essential for the growth, development, reproduction, and movement of C. elegans were carried out. Quantitative PCR-based assays showed that these molecules moderately regulate the expression of genes involved in the citric acid cycle (mdh-1 and idhg-1) and cytoskeleton (act-1 and act-2). MALDI-ToF-MS/MS analysis of RP-HPLC peaks revealed the presence of paucimannose-like N-glycans which are known to play important roles in invertebrates e.g., worms and flies. These findings provided novel information regarding the structure and nematicidal function of honey glycoconjugates. - Source: PubMed
Publication date: 2024/02/07
Bilal BushraAzim M Kamran