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The autoantibodies to GluD2 are common in patients with OMAS, bind to surface determinants, and are potentially pathogenic.
In HEK293 cell lines GDH2 and GDH1 were over-expressed and found to be co-localized in subcellular fractions.
GLUD2 overexpression inhibited Glioblastoma (GBM) cell growth suggesting a novel potential drug target for control of GBM progression. The possibility to enhance GLUD2 activity in GBM could result in a blocked/reduced proliferation of GBM cells without affecting the survival of the surrounding neurons.
hGDH2 evolution bestowed large human neurons with enhanced glutamate metabolizing capacity, thus strengthening cortical excitatory transmission.
This study demonstrated that hGDH2 expression increases capacity for uptake and oxidative metabolism of glutamate, particularly during increased workload and hypoglycemia.
This proliferation requires glutamate dehydrogenase 2, which synthesizes glutamate from ammonia and alpha-ketoglutarate and is expressed in MCF7 and T47D cells. Our findings provide insight into how cancer cells survive under glutamine deprivation conditions and thus contribute to elucidating the mechanisms of tumor growth.
The expression of GLUD2 was identified in the cellular and subcellular compartments of numerous tissues.
Notably, the introduction of GLUD2 did not affect glutamate levels in mice, consistent with observations in the primates. Instead, the metabolic effects of GLUD2 center on the tricarboxylic acid cycle, suggesting that GLUD2 affects carbon flux during early brain development, possibly supporting lipid biosynthesis.
Study of the expression of the GDH1/2 in human steroidogenic organs revealed that, while GDH2 was expressed specifically in steroid-synthesizing cells, GDH1 was expressed both in the cells that produce steroids and in those that lack endocrine function.
IDH1(R132H) exhibits a growth-inhibitory effect that is abrogated in the presence of glutamate dehydrogenase 2 (GLUD2), a hominoid-specific enzyme purportedly optimized to facilitate glutamate turnover in human forebrain.
hGDH2 can operate efficiently in the relatively acidic environment that prevails in astrocytes following glutamate uptake [review]
first N-terminal alpha helical structure is crucial for the mitochondrial import of hGDH2 and these findings may have implications in understanding the evolutionary mechanisms that led to the large mitochondrial targeting signals of human GDHs
[review] Whereas GDH2 in most mammals is encoded by a single functional GLUD1 gene expressed widely, humans have acquired through retroposition an X-linked GLUD2 gene that encodes a highly homologous isoenzyme GDH2 expressed in testis and brain.
Human GDH1 appears to act like bovine GDH1, but human GDH2 does not show the same enhancement of branched chain alpha-keto acid dehydrogenase complex enzyme activities.
A protein encoded by this locus was found to be differentially expressed in postmortem brains from patients with atypical frontotemporal lobar degeneration.
GLUD2 glutamate dehydrogenase is expressed in neural and testicular supporting cells
A gain-of-function rare polymorphism in hGDH2 hastens the onset of Parkinson's disease in hemizygous subjects.
identify the structural basis for allosteric differences of GlUD1 and GLUD2
These results suggest that the Ser443 residue plays an important role in the different thermal stability of human glutamate dehydrogenase isozymes (hGDH1 and hGDH2).
these data illustrate the essential role of EIN3-regulated GDH activity in metabolic adjustment during anoxia-reoxygenation.
In leaves and stems of arabidopsis and tobacco, both the alpha- and beta-subunits of Glutamate dehydrogenase are targeted to the mitochondria of the companion cells.
role in amino acid breakdown under C-deficient conditions
Protein phosphorylation by serine/threonine protein kinases is the essential step required for signal transduction into nucleus resulting in the induction of glutamate dehydrogenase 2 expression.
The protein encoded by this gene is localized to the mitochondrion and acts as a homohexamer to recycle glutamate during neurotransmission. The encoded enzyme catalyzes the reversible oxidative deamination of glutamate to alpha-ketoglutarate. This gene is intronless.
, glutamate dehydrogenase 2, mitochondrial
, glutamate dehydrogenase pseudogene 1
, glutamate dehydrogenase 2