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Last update 08 May 2025

MDH1

Last update 08 May 2025

Basic Info

Synonyms

Cytosolic malate dehydrogenase, Diiodophenylpyruvate reductase, malate dehydrogenase 1

+ [3]

Introduction

Catalyzes the reduction of aromatic alpha-keto acids in the presence of NADH (PubMed:2449162, PubMed:3052244). Plays essential roles in the malate-aspartate shuttle and the tricarboxylic acid cycle, important in mitochondrial NADH supply for oxidative phosphorylation (PubMed:31538237). Catalyzes the reduction of 2-oxoglutarate to 2-hydroxyglutarate, leading to elevated reactive oxygen species (ROS) (PubMed:34012073).

Drugs associated with MDH1

FM-701

Target

MDH1 x MDH2

Mechanism

MDH1 inhibitors [+1]

Active Org.

Future Medicine Co., Ltd.

Originator Org.

Future Medicine Co., Ltd.

Active Indication

Non-Small Cell Lung Cancer

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with MDH1

100 Translational Medicine associated with MDH1

0 Patents (Medical) associated with MDH1

560

Literatures (Medical) associated with MDH1

01 May 2025·Pathology - Research and Practice

M2 macrophages-derived exosomal MDH1 drives lung adenocarcinoma progression via the Hippo/YAP signaling

Article

Author: Liu, Jinpeng ; Liu, Zhuixing ; Zhang, Jie ; Liu, Xueqin ; Guo, Lihong

BACKGROUNDExosomes are released by most cell types, including tumor-associated macrophages (TAMs), transfer diverse macromolecules and participate in intercellular communication in cancer. However, whether M2-polarized TAMs (M2-TAMs)-derived exosomes (M2-exos) transmit the oncogenic protein malate dehydrogenase 1 (MDH1) to reprogram lung adenocarcinoma (LUAD) cancer cells is unknown.METHODSTHP-1-differentiated macrophages were co-cultured with A549 cells to generate TAMs (M0-TAMs and M2-TAMs). Exosomes (M0-exos and M2-exos) were isolated from the co-culture supernatant and characterized. Xenograft studies were used to explore the effect of M2-exos-derived MDH1 on tumor growth. Expression analysis was performed by quantitative PCR, immunoblot and immunohistochemistry (IHC). Cell phenotype changes were detected by CCK-8, EdU, colony formation, wound-healing and transwell assays.RESULTSBioinformatics analyses confirmed that MDH1 was overexpressed in human LUAD and high MDH1 expression was associated with poor prognosis. MDH1 depletion resulted in the in vitro suppression of LUAD cell growth, migration and invasiveness. M2-exos contained and transferred MDH1 into LUAD cells to upregulate MDH1 level in these cells. M2-exos-derived MDH1 enhanced the growth of A549 xenograft tumors in vivo and activated the Hippo/YAP pathway in vitro. Furthermore, Yes-associated protein (YAP) depletion could abrogate M2-exos-induced enhancements in these malignant phenotypes of A549 and HCC827 LUAD cells.CONCLUSIONThese findings demonstrate that exosomal MDH1 derived from M2-TAMs enhance LUAD cell growth and metastasis by activating the Hippo/YAP signaling, uncovering a novel exosomal mechanism of crosstalk between tumor microenvironment and LUAD cells.

01 May 2025·International Journal of Biological Macromolecules

Regulation and mechanism of Bletilla striata polysaccharide on delaying aging in Drosophila melanogaster

Article

Author: Zhou, Jihai ; Du, Dongsheng ; Zhu, Kai ; Ni, Hang ; Hu, Fan ; Hafeez, Eqra ; Chen, Dongsheng

Bletilla striata polysaccharide (BSP) is a natural bioactive compound known for its promising health benefits, including antioxidant, immunomodulatory, and anti-inflammatory effects. However, its potential in combating aging remains largely unexplored. This study aims to investigate the anti-aging effects of BSP in the Drosophila melanogaster model. The results show that BSP supplementation significantly extends the lifespan of flies in a concentration-dependent manner, with the most pronounced effects observed at a concentration of 3 mg/mL. Lifespan extension is associated with enhanced antioxidative capacities, as evidenced by increased SOD and CAT activities, and decreased MDA content. Additionally, BSP ameliorates age-related symptoms, including improved climbing ability and enhanced intestinal barrier function. Furthermore, BSP supplementation enhances resistance to H₂O₂-induced oxidative and starvation stresses, attenuates the lead (Pb)-induced toxicity, and delays the onset of Alzheimer's phenotypes in flies. RNA-Seq analysis reveals that BSP supplementation leads to the differential expression of 992 genes. KEGG pathway analysis highlights significant changes in metabolic pathways, including galactose metabolism, starch and sucrose metabolism, and carbon metabolism. Key genes such as Mal-A1, Amy-d, Men-b, Pgm-1, Mdh1, and Hex-C are downregulated, while CG32026, CG11291, and Ald2 are upregulated. These findings suggest BSP exhibits significant anti-aging and protective properties, making it a potential therapeutic agent.

01 Apr 2025·Theriogenology

Nicotinamide dual treatment enhances morula-to-blastocyst transition through binding to Zonula Occludens-1 protein

Article

Author: El-Sayed, Ahmed F ; El-Sheikh, Marwa ; Mesalam, Ayman ; Metwally, Heba M ; Lee, Seo-Hyun ; Kong, Il-Keun ; Mesalam, Ahmed Atef

Nicotinamide (NAM) is a widely utilized compound in cell culture systems, yet its role during the morula-to-blastocyst transition remains underexplored. This study investigates the effects of NAM supplementation during both in vitro maturation (IVM) of oocytes and late-stage embryo culture (IVC3; the morula stage) on blastocyst development, metabolic flux, mitochondrial bioenergetics, and pluripotency of cells. Bovine oocytes were subjected to dual NAM treatment during IVM and IVC3 and its impact was assessed through cleavage and blastocyst development rates, mitochondrial membrane potential (ΔΨm), and the expression of key metabolic and pluripotency markers using RT-qPCR and immunofluorescence. Additionally, molecular docking was performed to evaluate NAM's interaction with Zonula Occludens-1 (ZO-1) protein. Dual NAM administration significantly increased both blastocyst formation and hatching rates. Computational modeling revealed a strong binding affinity (-6.44 kcal/mol) between NAM and the ZO-1 protein, associated with the morula-to-blastocyst transition. Quantitative RT-PCR analysis showed upregulation of genes related to NAD + biosynthesis (NAMPT, MDH1), glycolysis (PFK1), glycogenesis (GSK-3A), and mitochondrial bioenergetics (SDHA, ND2, ATPase8, TFAM) in NAM-treated group. Additionally, mitochondrial profiling demonstrated enhanced polarization, and OCT4 expression was elevated in NAM-treated embryos. These findings underscore NAM's potential role in enhancing morula-to-blastocyst transition, improving embryonic development through metabolic and mitochondrial regulation, as well as pluripotency factor enhancement.

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MDH1

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