Glutamate dehydrogenase (GDH, EC
1.4.1.2) converts glutamate to alpha-ketoglutarate yielding ammonia in the
presence of its coenzyme NAD(P)+. It is an oxidoreductase using both
NAD+ or NADP+ as acceptor. GDH was known as a
mitochondrial indicator and because of the crucial function of linking
catabolic-anabolic pathways, it is ubiquitously found in whole tissues, mostly
in liver. While most mammals have only GDH1,
humans have been shown to acquire the second isoform, hGDH2 (h for human)
displaying tissue specificity. Intracellular localizations of GDH were
identified as mitochondrial matrix, membrane and nuclear fractions (1).
GDH plays an important role in
the amino acid, carbohydrate, oxidative phosphorylation metabolisms and has
been associated with several cellular processes such as balancing ammonia and acid-base
concentrations, redox homeostasis, lipid and lactate biosynthesis (1). Previous reports proved that enhanced activity of
GDH aids tumor cells for proliferation through supporting nitrogen sources (1-3). Besides, GDH serum level may show the liver tissue
damage, particularly mitochondrial dysfunction considering the cellular
sublocalization of the enzyme (4). Thus, measuring serum GDH activity may provide great
advantages for clinical and diagnostic purposes.
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