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Amino acids are among the most abundant of all neurotransmitters present within the
central nervous system (CNS). Studies which have characterized the high-affinity
uptake of amino acids, in either brain slices or subcellular fractions, support current
dogma that the majority of neurons in the mammalian brain utilize either glutamate
or -aminobutyric acid (GABA) as their primary neurotransmitters. In effect, GABA
and glutamate serve to regulate the excitability of virtually all neurons in brain and,
not surprisingly, therefore have been implicated as important mediators of many
critical physiological as well as pathophysiological events that underlie brain function
and/or dysfunction. Pharmacological studies utilizing drugs which selectively block or
augment the actions of GABA or glutamate support the notion that these two
neurotransmitters, by virtue of their often opposing excitatory and inhibitory actions,
control, to a large degree, the overall excitability of the CNS. Thus, drugs which
enhance inhibitory synaptic events mediated by GABA often decrease opposing
excitatory events mediated by glutamate and vice versa (see Excitatory Amino Acid
Neurotransmission, Schizophrenia and Glutamate: An Update, Amyotrophic Lateral Sclerosis,
Glutamate, and Oxidative Stress, Potential Mechanisms of Neurologic Disease in HIV Infection,
and Abuse and Therapeutic Use of Benzodiazepines and Benzodiazepine-Like Drugs). The
behavioral consequences of such pharmacologically induced changes in the "balance"
between inhibition and excitation are often profound (e.g., following administration of
convulsant or anesthetic drugs which are known to alter GABAergic or glutamatergic
neurotransmission).
GABA and glycine are arguably the most important inhibitory neurotransmitters in
the brain and brainstem/spinal cord, respectively. These inhibitory amino acids are of
particular interest to the neuropsychopharmacologist, because many commonly
studied (and therapeutically useful) drugs work by selectively affecting these two
neurotransmitter systems. What follows is a review of these two inhibitory amino acid
neurotransmitters, with an emphasis on the important role they play in mediating the
actions of a variety of neuropsychopharmacologic agents.
GABA is formed in vivo via a metabolic pathway called the GABA shunt. The initial
step in this pathway utilizes -ketoglutarate formed from glucose metabolism via the
Krebs cycle. -Ketoglutarate is then transaminated by -oxoglutarate transaminase
(GABA-T) to form glutamate, the immediate precursor of GABA. Finally, glutamate
is decarboxylated to form GABA by the enzyme(s) glutamic acid decarboxylase
(GAD) (18, 39). GAD is expressed only in GABAergic neurons and in certain
peripheral tissues which are also known to synthesize GABA (see below). Like most
neurotransmitters, GABA is stored in synaptic vesicles and is released in a Ca 2+-
dependent manner upon depolarization of the presynaptic membrane. Following
release into synaptic cleft, GABA's actions are terminated principally by reuptake into
presynaptic terminals and/or surrounding glia. GABA is also metabolized by GABA-
T to form succinic semialdehyde. This transamination will regenerate glutamate when
it occurs in the presence of -ketoglutarate. Succinic semialdehyde is oxidized by
succinic semialdehyde dehydrogenase (SSADH) to succinic acid which then reenters
the Krebs cycle.
The reuptake of GABA occurs via highly specific transmembrane transporters which
have recently been shown to be members of a large family of Na +-dependent
neurotransmitter transporters. GABA uptake is temperature- and ion-dependent (both
Na+ and Cl- ions are required for optimal uptake). Affinity purification of the GABA
transporter protein has recently led to its molecular cloning (20). The principal
neuronal GABA transporter appears to be a 70- to 80-kDa glycoprotein which, based
on its deduced amino acid sequence, is predicted to contain 12 hydrophobic
membrane-spanning domains. To date, at least two other GABA transporter cDNAs
have been cloned (9). However, the physiological and pharmacological significance of
this heterogeneity is unknown. Nonetheless, specific inhibitors of GABA uptake
which directly bind to the transporter itself have been synthesized, and several have
been shown to have anticonvulsant and/or antinociceptive properties in laboratory
animals.
Unlike the other enzymes involved in GABA synthesis, GAD is expressed only in
neurons and certain peripheral tissues which make or utilize GABA for signaling
and/or endocrine functions (18). Early work strongly suggested the existence of at
least two GAD enzymes which differed in their interaction(s) with PLP as well as in
their subcellular distributions (18). Native GAD appears to exist as a dimer—probably
a homodimer of two subunits of approximately 60 kDa each. GAD activity is quite
high in brain, and it is now clear that approximately 50% of the enzyme(s) exists as
apo-GAD (not bound to PLP) whereas the rest is bound to PLP (holo-GAD).
Interestingly, there is also evidence that increased neuronal activity (e.g., that induced
by depolarizing conditions) results in an increase in local GABA synthesis by
promoting the association of PLP with apo-GAD to form active enzyme (18).
Although the presence of two GAD isoforms was strongly supported by both
biochemical and immunochemical data, their similarities and differences were not
fully appreciated until both forms were cloned in an elegant series of studies by Tobin
and colleagues (17, 18).
GAD is also expressed outside the CNS. For example, both GAD isozymes are
present in cells of the pancreatic islets where GABA is suspected to play a role in
pancreatic endocrine function. (Immunohistochemical and lesion studies with -cell
toxins such as streptozotocin have shown that GAD and insulin coexist in the cell.)
In this regard, Baekkeskov et al. (3) have shown that antibodies to the 64-kDa form of
GAD (which appears to be related to GAD65) occur in most, if not all, patients with
insulin-dependent diabetes, and their presence appears to precede the clinical onset of
disease. Autoantibodies to GAD may therefore underlie the development of insulin-
dependent (type I) diabetes as well as that of the relatively rare neurological disorder
known as stiff-man syndrome.
GABAA receptors, like most receptors, can be defined by the drugs (and other ligands)
which selectively bind to, and either stimulate or block, receptor activity ( ).
A variety of GABA receptor agonists have been discovered and have been shown to
selectively activate GABAA receptors. Muscimol, a rigid GABA analogue isolated
from the hallucinogenic mushroom Amanita muscaria, is one of the most selective
and potent GABA agonists known. Muscimol is also not a substrate for the GABA
transporter, which makes it useful for electrophysiological and biochemical studies.
Both competitive and noncompetitive GABAA receptor antagonists have also been
described (16). Bicuculline is the prototypical competitive antagonist and directly
competes with GABA for binding to the receptor complex. Bicuculline reduces both
the frequency and mean open time of the GABA-gated Cl - ion channel. Picrotoxin and
other extremely potent cage convulsants such as t-butylbicyclophosphorothionate
(TBPS) are noncompetitive GABA receptor antagonists which do not compete
directly with GABA for its recognition site(s) but, instead, bind to a separate and
distinct recognition site(s) associated with the receptor complex (44). Not
surprisingly, both classes of GABAA receptor antagonists produce seizures when
administered to laboratory animals. The affinity of cage convulsants such as TBPS for
GABAA receptors is so high that they have proven to be useful radioligands for
measuring GABAA receptors in vitro and for their subsequent biochemical and
pharmacological characterization (44). These studies have revealed that
GABAA receptors have multiple allosteric binding sites for drugs which, when
occupied, modulate (positively or negatively) the inhibitory actions of GABA.
Ethanol, one of the most commonly used (and abused) sedative-hypnotic agents, has
been shown by several investigatiors to augment GABA-activated Cl - ion conductance
in a variety of intact and isolated neuronal membrane preparations (46). To date,
however, electrophysiological studies of ethanol's actions in augmenting GABA-
activated Cl- ion conductance have yielded somewhat mixed results (see ref. 31 for
review). More recent studies have generally confirmed that pharmacologically-
relevant concentrations of ethanol (10–100 mM) weakly (but significantly) augment
GABA-activated Cl- ion conductance (31) as do longer chain-length alcohols and
general anesthetics (31, 51). Moreover, several imidazobenzodiazepine inverse
agonists of the benzodiazepine receptor (see below) have been reported to
ùantagonizeú the sedative/ataxic effects of ethanol (47)—further implicating the
GABAA receptor as one of the key central sites mediating at least some of ethanol's
neuropharmacological effects. The effects of ethanol on GABA A receptors, coupled
with its more recently described actions in inhibiting glutamate (NMDA) receptor-
mediated depolarizing events (51), likely contribute to the anxiolytic and sedative
effects of alcohols.
Since the discovery of the benzodiazepine receptor (recognition site), a large number
of benzodiazepine and nonbenzodiazepine drugs have been found to interact with
these receptors—and in unexpected ways. In addition to those receptor ligands which
augment GABA responses (now called agonists), two other broad classes of ligands
have now been characterized. Selective antagonists such as the
imidazobenzodiazepine Ro15-1788 (flumazenil) bind with high affinity to
GABAA receptors but are devoid of intrinsic activity of their own (22). However,
these antagonists completely block the actions of benzodiazepine receptor agonists in
augmenting GABA-mediated responses. Selective antagonists like flumazenil also
block (or reverse) the actions of inverse agonists. The latter are benzodiazepine
receptor ligands which decrease GABA-activated Cl- ion conductance (by decreasing
the frequency of channel openings). The GABAA receptor can thus
be positively or negatively modulated by compounds which range in activity from full
agonists to full inverse agonists (22). Along this continuum lie compounds with
different degrees of intrinsic efficacy—that is, compounds with only partial agonist or
inverse agonist actions. Behaviorally, full agonists have sedative– anesthetic
properties, whereas full inverse agonists are convulsants (14). Partial benzodiazepine
receptor agonists (now in development by several pharmaceutical companies) may
prove to be effective anxiolytics, devoid of the sedative effects generally observed
with full agonists (22). The fact that benzodiazepine receptor agonists reduce anxiety
and that inverse agonists are profoundly anxiogenic, coupled with recent observations
that the "sensitivity" of animals to inverse agonists can be altered (in some cases
increased) by pharmacological or environmental factors, has prompted considerable
speculation that GABAA receptors are involved in at least some forms of human
anxiety (see refs. 24 and 54 for reviews).
The large number of drug recognition sites associated with GABA A receptors (which
are clearly distinct from those which recognize GABA itself) have led several
investigators to propose the existence of endogenous receptor ligands. Several such
"candidate" ligands have been identified; however, with the possible exception of two,
there is little compelling evidence at present that any interact with GABA A receptors
in vivo. One of these ligands is an endogenous peptide called diazepam-binding
inhibitor (DBI), which was initially isolated by Guidotti et al. (21) and was shown to
interact with GABAA receptors and to have anxiogenic properties (similar to inverse
agonists). The other postulated endogenous ligand(s) include two natural reduced
steroid metabolites of progesterone and deoxycorticosterone (allopregnanalone and
allotetrahydro-DOC) (29). These neuroactive steroids bind with high affinity to
GABAA receptors and have "barbiturate-like" actions in augmenting GABA-mediated
responses (for review see ref. 35). The plasma and brain levels of these neuroactive
steroids increase dramatically following exposure of rats to various stressors. Plasma
allopregnanolone levels are also quite high during the third trimester of pregnancy,
and they decrease dramatically following parturition (35). None of these putative
natural ligands, however, have yet been unequivocally demonstrated to subserve any
physiological function.
In 1987, Barnard, Seeburg, and colleagues (4, 41), using partial amino acid sequences
from purified bovine brain GABAA receptors succeeded in cloning several of the
subunits which comprise the GABAA receptor(s). The deduced amino acid sequences
of the - and -subunit cDNAs isolated by these investigators indicated that each
subunit was approximately 50–60 kDa in size and had four -helical hydrophobic
membrane-spanning sequences of approximately 20–30 amino acids. The predicted
structure of the receptor was based on strong evidence that the GABA A receptor is a
member of a large superfamily of ligand-gated ion channels which includes the
nicotinic-cholinergic, ionotropic glutamate, and glycine receptors (there is
approximately 10–20% sequence identity between members of this superfamily) (4,
33).
GABAB RECEPTORS
Glycine is the major inhibitory neurotransmitter in the brainstem and spinal cord,
where it participates in a variety of motor and sensory functions. Glycine is also
present in the forebrain, where it has recently been shown to function as a coagonist at
the N-methyl-D-aspartate (NMDA) subtype of glutamate receptor. In the latter, context
glycine promotes the actions of glutamate, the major excitatory neurotransmitter (for a
discussion of glycine's role as a coagonist of the NMDA receptor, see Excitatory Amino
Acid Neurotransmission). Thus, glycine subserves both inhibitory and excitatory
functions within the CNS.
Recently, two glycine transporters have been cloned and shown to be expressed in the
CNS as well as in various peripheral tissues (11, 19). These glycine transporters are
members of the large family of Na +/Cl--dependent neurotransmitter transporters, and
both share approximately 50% sequence identity with the GABA transporters
discussed above. The deduced amino acid sequence of both cDNAs predicts the
typical 12 transmembrane domains characteristic of these transporters. The two
glycine cloned transporters have been named GLYT-1 and GLYT-2 in the order that
they were reported (11). These transporter cDNAs are transcribed from the same gene
and are quite similar in their 3 nucleotide sequences. They differ in their 5 noncoding
regions as well as in the first 44 nucleotides of their coding sequence. Expression of
GLYT-1 and GLYT-2 yield transporters with similar kinetic and pharmacological
properties. Interestingly, however, the distribution of GLYT-1 and GLYT-2
transcripts measured by in situ hybridization are different. GLYT-1 mRNA also
closely parallels the distribution of the glycine receptor. These data suggest that
GLYT-1 is primarily a glial glycine transporter whereas GLYT-2 is primarily a
neuronal transporter. The mapping of both glycine transporter mRNAs, as well as the
glycine receptor subunit mRNAs, confirm the importance of this neurotransmitter in
the brainstem and spinal cord, but support a more widespread distribution in
supraspinal brain regions than was previously suspected.
GLYCINE RECEPTORS
Inhibitory glycine receptors are blocked by the plant alkaloid strychnine, which was
also first used to label glycine receptors in spinal cord membranes (52, 53).
Strychnine poisoning results in muscular contractions and tetany as a result of
glycinergic disinhibition and overexcitation. Electrophysiological studies primarily
carried out in rodent spinal cord neurons have demonstrated that glycine activates
Cl- ion conductance (8). Like GABA, this increase in Cl - ion conductance results in a
hyperpolarization of the neuronal membrane and an antagonism of other depolarizing
stimuli. Other - and -amino acids, including -alanine and taurine, also activate
glycine receptors, but with lower potency (6, 8).
The glycine receptor was first successfully solubilized and purified by Betz and
colleagues using affinity purification over an affinity matrix derivatized with
aminostrychnine (8). The affinity-purified glycine receptor was shown to consist of
two polypeptide subunits of approximately 48 kD () and 58 kD (), respectively.
Reconstitution of these polypeptide subunits into lipid vesicles resulted in functional
receptors, and intramolecular cross-linking experiments suggested that the native
glycine receptor is a pentameric structure. Photoaffinity labeling of the glycine
receptor with [3H]strychnine revealed that both the strychnine and glycine binding
sites are located on the 48-kD subunit. Purification of the -and -receptor subunits
was followed closely by their molecular cloning (7).
CONCLUSIONS
the Glycine Receptor (GlyR). It can either be protonating or protonated, depending on pH. neurotransmitter. The neurotransmitter's
effect on mood is also why it's often a target of medications that are used to treat depression, anxiety, and other mood disorders. 21,
NO. Since the late 1970s glycine has been considered an important inhibitory neurotransmitter in brain stem and medulla. 25:21
Glycine synthesis is almost entirely dependent on folate utilization and generates about 3 grams per day. Functional expression and
purification of a homomeric human alpha 1 glycine receptor in baculovirus-infected insect cells.. Journal of Biological Chemistry, Vol.
Safety Data Sheet according to 29CFR1910/1200 and GHS Rev. Abstract. System neurotransmitter systems amino acids Together
with hydroxyproline, glycine makes up the helical structure of collagen. neurotransmitters. 1978). The neurotransmitter glycine has
been shown to serve a metabolic role in brain tumor formation (Jain et al., 2012). includes glycine receptor, another amino acid
neurotransmitter suggested to be derived from the GABAA receptor family (Vassilatis et al, 1997). Glycine neurotransmitter
transporters: an update ... PDF Abstract. When released into a synapse, glycine binds to a receptor which makes the post-synaptic
membrane more permeable to Cl-ion. Glycine is also very important for … In higher eukaryotes, glycine is involved in the synthesis
of a precursor to porphyrins. Glycine is the starting point for several metabolites — necessary for metabolism — occurring in the
body, including glutathione and creatine. It’s an inhibitory neurotransmitter in the central nervous system, especially in the spinal
cord, brainstem, and retina Glycine is an organic compound most commonly found in animal proteins. They are produced in the cell
body of the neuron and transported to the axon terminal. Significant improvments were also induced in depressive and cognitive
symptoms. A glycine site NMDA antagonist, L-701324, however, has a neuroleptic-like action in several animal models of psychosis
(Bristow et al. Pages 76 This preview shows page 19 - 25 out of 76 pages. This study aimed to investigate the … Take drugs
exactly as prescribed by a trustworthy doctor, and do not fear necessary prescription drugs because of terrible side effects on this
chart (which, by the way, may be inapplicable or extremely rare in … Glycine uptake in cancer cell studies supports the … Glycine is
an inhibitory neurotransmitter that is mainly active in the caudal areas of the CNS. a p < 0.05. Glycine accomplishes several
functions as a transmitter in the central nervous system(CNS). Users can perform simple and advanced searches based on
annotations relating to sequence, structure and function. It was reported very recently that the acute signs of phencyclidine
intoxication in the rat can be reversed by the Group II metabotropic agonist LY 354740 (Moghaddam and Adams 1998). (A) Average
current traces of glycinergic and GABAergic mIPCs were recorded in whole-cell configuration in the presence strychnine or
SR95331 and decays fitted with a single exponential (orange and blue) respectively. Glycine was well tolerated, resulted in
significantly increased serum glycine levels and induced a mean 36 (7%) reduction in negative symptoms (P < 0.0001). GABA
SYNTHESIS,RELEAS E, STORAGE,RECEPTO R 2. Send me a copy of this email ... Glycine, inhibitory neurotransmitter
(ab120050) 2D chemical structure image of ab120050, Glycine, inhibitory neurotransmitter. The RCSB PDB also provides a variety
of tools and resources. Glycine is the major inhibitory neurotransmitter in the spinal cord and brain stem. glycine concentrations
(>10 µM), macroscopic NMDA receptor currents elicited with seconds-long glutamate exposures relax slowly ( D of 1–2 s) to a
steady-state current that is 20–40% lower than the peak current. One of the most powerful effects of alcohol is to reduce the pace of
brain activity by a combin-ation of effects that reduces the excitatory actions of the neurotransmitter glutamate and enhances the
inhibitory actions of the neurotransmitters gamma-aminobutyric acid (GABA) and glycine examined the function of the NMDA
receptor subunit combination GluN1/GluN3A in the medial habenula (MHb) of adult mice. A neurotransmitter sodium symporter
(NSS) is type of neurotransmitter transporter that catalyzes the uptake of a variety of neurotransmitters, amino acids, osmolytes and
related nitrogenous substances by a solute:Na + symport mechanism. The vertebrate neuromuscular junction is the best studied
cholinergic synapse, but the mechanisms by which acetylcholine is matched with acetylcholine receptors are not fully understood.
Scribd is the world's largest social reading and publishing site. 106. Summary: Elevated levels of glycine in the CSF have recently
been documented in van der Knaap syndrome (diffuse leukoencephalopathy associated with cystic degeneration of the white
matter). Glycine is a non-essential amino acid that is produced naturally by the body. Dopamine is a hormone involved mainly in
controlling movement, but it also plays a role in the brain’s reward system, helping to reinforce certain behaviors. Benzodiazepines
influence on a number of neurotransmitters such as acetylcholine, catecholamines, serotonin, glycine and gamma-aminobutyric acid
(GABA), but during recent years the major interest has been focused on the inhibitory transmitter GABA. It may be useful for
supporting quality sleep and a … BIOCHEMISTRY A neurotransmitter is a chemical substance that is released from a nerve cell
and then transmits an impulse from a nerve cell to its target.A target can be another nerve, muscle, organ, or other tissue. When
glycine was added to culture media containing cells from the 97-year-old, the mitochondria in these cells became like new. "Glycine
is recognized as an “inhibitory” neurotransmitter, and promotes natural sleep. Glycine serves as an anti-inflammatory agent, calms
aggression, improves sleep Alcohol has been shown to increase the func-tion of glycine receptors in laboratory VOL. Otsu et al. ...
Glycine is the other inhibitory amino acid, but is less common. Glycine is one of several so-called nonessential amino acids for
mammals; i.e., In cancer cells, glycine consumption is highly correlated to cancer cell proliferation via purine synthesis. Users can
perform simple and advanced searches based on annotations relating to sequence, structure and function. The human glycine
transporter 1 (GlyT1) regulates glycine mediated neuronal excitation and inhibition through sodium- and chloride-dependent
reuptake of the neurotransmitter1-3. But in every type of cell, it apparently has the same kind of quieting, protective antistress
action. Glycine is abundant in oviduct fluid and is reported to be critical for preimplantation development of fertilized eggs in
mammals. To define the origin, course, and distribution of the major transmitter-specific systems of the CNS: glutamatergic, GABA-
ergic, cholinergic (ACh), noradrenergic (NE), dopaminergic (DA), and serotonergic (5-HT). Do not use drugs for fun. In caudal areas
of central nervous system (CNS) such as spinal cord and brainstem, glycine acts as a powerful inhibitory neurotransmitter through
binding to its receptor, i.e. Glycine is a conditionally essential amino acid with a dual role in the central nervous system (CNS).
Aprison and Werman first proposed that glycine acts as a neurotransmitter in mammalian central nervous system (CNS).They noted
that the concentration of glycine in the spinal cord is higher than elsewhere in the brain. Export to PDF. Download PDF. Figure
2.GABA, glycine and mIPSCs were defined on the basis of their peak current and charge transfer. Glycine is thought to be primarily
an inhibitory neurotransmitter. BioVision’s Glycine Assay Kit provides a simple, sensitive, and high-throughput adaptable assay that
detects physiological Ab, example whole‐cell recording from a L2/3 pyramidal cell depicting miniature excitatory postsynaptic
currents (mEPSCs) recorded at baseline, during bath application of 1 … May contribute to poor sleep, poor cognitive function and
issues with memory. In caudal areas of central nervous system (CNS) such as spinal cord and brainstem, glycine acts as a powerful
inhibitory neurotransmitter through binding to its receptor, i.e. Glycine's function as a neurotransmitter is also fairly simple. Glycine
as an Inhibitory Neurotransmitter. In many of these neurons, glycine coexists with γ-aminobutyric acid (GABA). Activation of NMDA
receptors by the neuro-transmitter glutamate requires glycine as an essential coagonist. Glycine is the simplest (and the only
achiral) proteinogenic amino acid, with a hydrogen atom as its side chain. Gingival epithelial cells (GECs) represent a physical
barrier against bacteria and are involved in the processes of innate immunity. glycine neurotransmitter pdf Localization of Glycine
Neurotransmitter Transporter.Brain organization labels derive from development. (v) L-Glycine-is a non-essential amino acid.
Glycine (Gly) The eighth neurotransmitter that we have included in this list is glycine, which also has inhibitory effects in the central
nervous system but, contrary to GABA, its activity is more important in the spine than in the brain. 8. It can also have a role in the
treatment of psychiatric disorders, blood sugar regulation and building muscle. C. decrease in action potential amplitude. Methods
Patients with a positive serum GlyRα1-IgG were identified during a 2-year period from July 2016 to December 2018 at 2 academic
centers and followed prospectively. An experimental study with a … glycine-inhibitory-neurotransmitter-ab120050.pdf. This
hyperpolarizes the membrane, making it less likely to depolarize. Glycine is also a major inhibitory neurotransmitter in the adult
vertebrate central nervous system (CNS). ... Glycine can function as a calming neurotransmitter and helps combat occasional stress
by promoting relaxation. Thus, glycine is an inhibitory neurotransmitter. Glycine is a neurotransmitter with the ability to be both
excitatory and inhibitory, meaning it can function both to stimulate brain and nervous system activity, or to quiet it. 19:27 Roles of
glycine include detoxification, glutathione synthesis, heme synthesis, creatine synthesis, collagen synthesis, removal of
intermediates when metabolic pathways are backed up, and it acts as a calming neurotransmitter. Glycine is the simplest amino
acid and is amphoteric. It acts as a classical neurotransmitter at inhibitory glycinergic synapses, where it … Glycine possesses both
inhibitory and excitatory neurotransmitter functions in the brain stem and spinal cord. The ligand for the glycine receptor is the
protein building block (amino acid) glycine. Glycine is an amino acid neurotransmitter that elicits both neuronal inhibition and
excitation in the central nervous system. The embryonic developing cerebral cortex is characterized by the presence of distinctive
cell types such as progenitor pools, immature projection neurons and interneurons. This molecule also acts as a neurotransmitter,
which is a chemical messenger that transmits signals in the nervous system. Glycine has been well characterized in spinal cord as
an inhibitory neurotransmitter which activates a glycine-gated chloride channel (GlyR) expressed in postsynaptic membranes.