Abstract 2216 Does Cytosolic Malate Dehydrogenase (hMDH1) Have a Sinister Role in Tumor Cell Survival? Could Phosphorylation Transform hMDH1 from a Mild-Mannered Metabolic Enzyme to a Supporter of Cancer Cell Progression

Malate dehydrogenase (EC 1.1.1.37) is an enzyme involved in cellular metabolism that catalyzes the reversible oxidation of malate to oxaloacetate using the reduction of nicotinamide adenine dinucleotide (NAD+/NADH). Human cytosolic, malate dehydrogenase splice variant 3 (hMDH1V3) is encoded by MDH-1 gene. In acidic conditions where tumor cells undergo a high rate of glycolysis, hMDH1V3 can at low rates produce the oncometabolite 2-hydroxyglutarate (2HG) from α-Ketoglutarate (αKG). Several mass-spectroscopy databases have identified more than 25 phosphorylation sites of hMDH1.

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Journal
Journal of Biological Chemistry
Published
2025-05-01
DOI
https://doi.org/10.1016/j.jbc.2025.108710
Primary Topic
Cancer, Hypoxia, and Metabolism
Type
article
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Abstract 2216 Does Cytosolic Malate Dehydrogenase (hMDH1) Have a Sinister Role in Tumor Cell Survival? Could Phosphorylation Transform hMDH1 from a Mild-Mannered Metabolic Enzyme to a Supporter of Cancer Cell Progression

Joseph Provost, Anastasia Alkhouri
Journal of Biological Chemistry
Cancer, Hypoxia, and Metabolism
article

Abstract 2216 Does Cytosolic Malate Dehydrogenase (hMDH1) Have a Sinister Role in Tumor Cell Survival? Could Phosphorylation Transform hMDH1 from a Mild-Mannered Metabolic Enzyme to a Supporter of Cancer Cell Progression

Joseph Provost, Anastasia Alkhouri
article en

Abstract

Malate dehydrogenase (EC 1.1.1.37) is an enzyme involved in cellular metabolism that catalyzes the reversible oxidation of malate to oxaloacetate using the reduction of nicotinamide adenine dinucleotide (NAD+/NADH). Human cytosolic, malate dehydrogenase splice variant 3 (hMDH1V3) is encoded by MDH-1 gene. In acidic conditions where tumor cells undergo a high rate of glycolysis, hMDH1V3 can at low rates produce the oncometabolite 2-hydroxyglutarate (2HG) from α-Ketoglutarate (αKG). Several mass-spectroscopy databases have identified more than 25 phosphorylation sites of hMDH1.

Journal of Biological ChemistryVol. 301(5)
University of San Diego (US)
Good health and well-being
Openalex Percentile: Top 82%
Cancer, Hypoxia, and Metabolism
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