N‐Acetylaspartylglutamate

@article{Neale2000NAcetylaspartylglutamate,
  title={N‐Acetylaspartylglutamate},
  author={Joseph H Neale and Tomasz Bzdȩga and B. Wr{\'o}blewska},
  journal={Journal of Neurochemistry},
  year={2000},
  volume={75}
}
In the progress of science, as in life, timing is important. The acidic dipeptide, N‐acetylaspartylglutamate (NAAG), was discovered in the mammalian nervous system in 1965, but initially was not considered to be a neurotransmitter candidate. In the mid‐1980s, a few laboratories revisited the question of NAAG's role in the nervous system and pursued hypotheses regarding its function that ranged from a precursor for the transmitter pool of glutamate to a direct role as a peptide transmitter… 
N‐Acetylaspartylglutamate is an agonist at mGluR3 in vivo and in vitro
  • J. Neale
  • Biology, Medicine
    Journal of neurochemistry
  • 2011
TLDR
The application of inhibitors of the extracellular enzymes that inactivate NAAG revealed that elevating the synaptic level of this peptide has considerable therapeutic potential in clinical conditions ranging from stroke and traumatic brain injury to inflammatory pain and schizophrenia.
Molecular Characterization of N-Acetylaspartylglutamate Synthetase
TLDR
Results strongly suggest that the identified gene encodes a NAAG synthetase, which will enable further studies to examine the role of this abundant neuropeptide in the vertebrate nervous system.
Molecular Identification of N-Acetylaspartylglutamate Synthase and β-Citrylglutamate Synthase*
The purpose of the present work was to determine the identity of the enzymes that synthesize N-acetylaspartylglutamate (NAAG), the most abundant dipeptide present in vertebrate central nervous system
N-Acetylaspartate synthase is bimodally expressed in microsomes and mitochondria of brain.
TLDR
The tentative conclusion is that ANAT is bimodally targeted to MIT and a component of MIC-likely endoplasmic reticulum.
N-acetylaspartylglutamate (NAAG) and Glutamate Carboxypeptidase II: An abundant peptide neurotransmitter-enzyme system with multiple clinical applications
TLDR
Data militate in favor of the development and application of GCPII inhibitors in more advanced preclinical research as a prelude to clinical trials.
Immunohistological and electrophysiological evidence that N‐acetylaspartylglutamate is a co‐transmitter at the vertebrate neuromuscular junction
TLDR
Electrophysiological studies showed that exogenous NAAG inhibited evoked neurotransmitter release by activating a group II metabotropic glutamate receptor (mGluR2 or mGLUR3) and localisation in the presynaptic terminal consistent with N AAG's demonstrated role as a regulator of synaptic release at central synapses support the conclusion that NAAGs is a co‐transmitter at the vertebrate NMJ.
N-Acetylaspartate and N-acetylaspartylglutamate
TLDR
In conclusion, elucidation of the neurobiology of NAA and NAAG provides insight into the role of these molecules in the pathophysiology of several neurologic disorders and their potential as a therapeutic target for these conditions.
N-acetylaspartate as a reservoir for glutamate.
TLDR
It is hypothesize that NAA conversion to glutamate is a logical and favorable use of this highly concentrated metabolite, and future studies to demonstrate the chemical, metabolic and pathological links between NAA and glutamate will support this hypothesis.
N-acetylaspartate in brain - studies on efflux and function
N-acetylaspartate (NAA) is an amino acid derivative present in high concentration in the brain. The function of NAA is still unsettled in spite of 50 years of research. The mainly neuronal synthesis
N-Acetyl-Aspartate (NAA) Metabolism
N-Acetyl-Aspartate (NAA) remains a unique molecule in medicine, where although its been associated with a number of brain pathologies, primarily due to its non-invasive visibility by magnetic
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References

SHOWING 1-10 OF 152 REFERENCES
Immunohistochemistry and Biosynthesis of N‐Acetylaspartylglutamate in Spinal Sensory Ganglia
TLDR
NAAG is present in a subpopulation of primary afferent spinal neurons and that its biosynthesis is mediated by a dipeptide synthetase, suggesting a precursor role for the large N‐acetylaspartate pool.
Localization and Transport of N‐Acetylaspartylglutamate in Cells of Whole Murine Brain in Primary Culture
TLDR
Results indicate that synaptically released NAAG, as well as that which may be released from glia, is removed from the extracellular space by direct uptake aswell as the robust enzymatic degradation of the peptide.
Release of N‐Acetylaspartylglutamate on Depolarization of Rat Brain Slices
TLDR
The present demonstration of NAAG release is consistent with electrophysiological and immunohistochemical evidence for its neurotransmitter function at terminals of the lateral olfactory tract and support the hypothesis that NAAGs is a neurotransmitter.
The Regional Distribution of N‐Acetylaspartylglutamate (NAAG) and Peptidase Activity Against NAAG in the Rat Nervous System
TLDR
The hypothesis that hydrolysis of NAAG to glutamate and N‐acetylaspartate is a consistent aspect of the physiology and metabolism of this peptide after synaptic release is supported.
N‐acetylaspartylglutamate activates cyclic AMP‐coupled metabotropic glutamate receptors in cerebellar astrocytes
TLDR
It is concluded that cerebellar astrocytes respond to NAAG via the mGluR3 receptor and that the peptide may selectively activate this receptor subtype in astroCytes following release from neurons or glia.
N-Acetylaspartylglutamate catabolism is achieved by an enzyme on the cell surface of neurons and glia
TLDR
The steady rise in extracellular glutamate as a consequence of NAAG hydrolysis by these brain cells, including glia, supports the conclusion that glutamate uptake is not tightly coupled to peptidase activity and thus that N AAG serves as a significant source of glutamate in the synaptic space following depolarization-induced peptide release.
Immunocytochemical distribution of n-acetylaspartylglutamate in the rat forebrain and glutamatergic pathways
TLDR
Findings indicate that NAAG is a neuropeptide localized to subpopulations of neurons throughout forebrain as well as in brainstem and spinal cord.
N‐Acetylaspartylglutamate Selectively Inhibits Neuronal Responses to N‐Methyl‐d‐Aspartic Acid In Vitro
TLDR
Testing the actions of NAAG and NAA on NMDA‐evoked responses in cultured cerebellar granule cells raises the possibility that disruption of NMDA receptor processes by NAAg may be of pathophysiological relevance.
Molecular Cloning of a Peptidase Against N‐Acetylaspartylglutamate from a Rat Hippocampal cDNA Library
TLDR
In situ hybridization data demonstrated the widespread distribution of the peptidase mRNA in the brain, consistent with the distribution of peptid enzyme activity.
Interactions Between N‐Acetylaspartylglutamate and AMPA, Kainate, and NMDA Binding Sites
TLDR
The hypothesis that, relative to glutamate, NAAG functions as a specific, low potency agonist at N‐methyl‐d‐aspartate subclass of ionotropic acidic amino acid receptors, but the peptide is not likely to activate directly the kainate or quisqualate subclasses of excitatory ionotropic receptors under physiologic conditions is supported.
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