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…
292 Citations
N‐Acetylaspartylglutamate is an agonist at mGluR3 in vivo and in vitro
- Biology, ChemistryJournal of neurochemistry
- 2011
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 Identification of N-Acetylaspartylglutamate Synthase and β-Citrylglutamate Synthase*
- Biology, ChemistryThe Journal of Biological Chemistry
- 2010
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…
Molecular Characterization of N-Acetylaspartylglutamate Synthetase
- Biology, ChemistryThe Journal of Biological Chemistry
- 2010
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.
N-Acetylaspartate synthase is bimodally expressed in microsomes and mitochondria of brain.
- Biology, ChemistryBrain research. Molecular brain research
- 2004
N-acetylaspartylglutamate (NAAG) and Glutamate Carboxypeptidase II: An abundant peptide neurotransmitter-enzyme system with multiple clinical applications
- BiologyProgress in Neurobiology
- 2019
Immunohistological and electrophysiological evidence that N‐acetylaspartylglutamate is a co‐transmitter at the vertebrate neuromuscular junction
- BiologyThe European journal of neuroscience
- 2013
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
- Biology, ChemistryNeurology
- 2008
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 in brain - studies on efflux and function
- Biology
- 2006
The results suggest that the NMDA receptor is involved in the regulation of NAA efflux from neurons and NAA does not seem to function as an important Ca2+ chelator or as an osmoregulator under physiological decreases in osmolarity.
N-Acetylaspartylglutamate Synthetase II Synthesizes N-Acetylaspartylglutamylglutamate
- Biology, ChemistryThe Journal of Biological Chemistry
- 2011
It is shown here that a structurally related protein, encoded by the ribosomal modification protein rimK-like family member A (Rimkla) gene, is another NAAG synthetase (NAAGS-II), which in addition, synthesizes the N-acetylated tripeptide N- acetylaspartyl glutamylglutamate (nAAG2).
References
SHOWING 1-10 OF 152 REFERENCES
Immunohistochemistry and Biosynthesis of N‐Acetylaspartylglutamate in Spinal Sensory Ganglia
- Biology, ChemistryJournal of neurochemistry
- 1987
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
- BiologyJournal of neurochemistry
- 1993
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
- BiologyJournal of neurochemistry
- 1988
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
- BiologyJournal of neurochemistry
- 1994
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
- Biology, ChemistryGlia
- 1998
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
- BiologyNeuropeptides
- 1993
Immunocytochemical distribution of n-acetylaspartylglutamate in the rat forebrain and glutamatergic pathways
- BiologyJournal of Chemical Neuroanatomy
- 1993
N‐Acetylaspartylglutamate Selectively Inhibits Neuronal Responses to N‐Methyl‐d‐Aspartic Acid In Vitro
- BiologyJournal of neurochemistry
- 1994
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
- BiologyJournal of neurochemistry
- 1997
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
- Biology, ChemistryJournal of neurochemistry
- 1994
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.