ArticleThe journal of histochemistry and cytochemistry : official journal of the Histochemistry Society2014
Determination of glutamate dehydrogenase activity and its kinetics in mouse tissues using metabolic mapping (quantitative enzyme histochemistry).
Article in The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 57 citations in OpenAlex.
- Recent insights into the roles and therapeutic potentials of GLS1 in inflammatory diseases.Journal of pharmaceutical analysis · 2025Review
- Review
- Age-related changes of skeletal muscle metabolic response to contraction are also sex-dependent.The Journal of physiology · 2025Article
- The role of glutamate dehydrogenase in the ageing brain.Frontiers in pharmacology · 2025Review
- Antiplasmodial evidence, host mitochondrial biology and possible mechanisms of action of a composite extract ofJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2024Article
- Metabolic and stress resistance effects in Macrobrachium rosenbergii juveniles supplemented with Curcuma longa extract.Veterinary research communications · 2024Article
- Dietary protein load affects the energy and nitrogen balance requiring liver glutamate dehydrogenase to maintain physical activity.The Journal of biological chemistry · 2024Article
- Effects of Metabolites, Sex, Sire, and Muscle Type on Chilled Lamb Meat Colour.Foods (Basel, Switzerland) · 2023Article
- Epigenetic activation of secretory phenotypes in senescence by the FOXQ1-SIRT4-GDH signaling.Cell death & disease · 2023Article
- Fundamental Role of Pentose Phosphate Pathway within the Endoplasmic Reticulum in Glutamine Addiction of Triple-Negative Breast Cancer Cells.Antioxidants (Basel, Switzerland) · 2022Article
- The Role of Glutamine and Glutaminase in Pulmonary Hypertension.Frontiers in cardiovascular medicine · 2022Review
- Review
- LncRNA GIRGL drives CAPRIN1-mediated phase separation to suppress glutaminase-1 translation under glutamine deprivation.Science advances · 2021Article
- The Impact of Acetyl-CoA and Aspartate Shortages on the N-Acetylaspartate Level in Different Models of Cholinergic Neurons.Antioxidants (Basel, Switzerland) · 2020Article
- UGCG influences glutamine metabolism of breast cancer cells.Scientific reports · 2019Article
- Glutamine Supplementation Ameliorates Chronic Stress-induced Reductions in Glutamate and Glutamine Transporters in the Mouse Prefrontal Cortex.Experimental neurobiology · 2019Article
- Immunometabolism: A new target for improving cancer immunotherapy.Advances in cancer research · 2019Review
- Glutamate Dehydrogenase, a Complex Enzyme at a Crucial Metabolic Branch Point.Neurochemical research · 2019Review
- Blood and Tissue Enzymatic Activities of GDH and LDH, Index of Glutathione, and Oxidative Stress among Breast Cancer Patients Attending Referral Hospitals of Addis Ababa, Ethiopia: Hospital-Based Comparative Cross-Sectional Study.Oxidative medicine and cellular longevity · 2018Article
- The Glutamate Dehydrogenase Pathway and Its Roles in Cell and Tissue Biology in Health and Disease.Biology · 2017Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glutamate dehydrogenase (GDH) catalyses the reversible conversion of glutamate into α-ketoglutarate with the concomitant reduction of NAD(P)(+) to NAD(P)H or vice versa. GDH activity is subject to complex allosteric regulation including substrate inhibition. To determine GDH kinetics in situ, we assessed the effects of various glutamate concentrations in combination with either the coenzyme NAD(+) or NADP(+) on GDH activity in mouse liver cryostat sections using metabolic mapping. NAD(+)-dependent GDH V(max) was 2.5-fold higher than NADP(+)-dependent V(max), whereas the K(m) was similar, 1.92 mM versus 1.66 mM, when NAD(+) or NADP(+) was used, respectively. With either coenzyme, V(max) was determined at 10 mM glutamate and substrate inhibition was observed at higher glutamate concentrations with a K(i) of 12.2 and 3.95 for NAD(+) and NADP(+) used as coenzyme, respectively. NAD(+)- and NADP(+)-dependent GDH activities were examined in various mouse tissues. GDH activity was highest in liver and much lower in other tissues. In all tissues, the highest activity was found when NAD(+) was used as a coenzyme. In conclusion, GDH activity in mice is highest in the liver with NAD(+) as a coenzyme and highest GDH activity was determined at a glutamate concentration of 10 mM.
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