Inhibitory glutamate receptor channels
Identifieur interne : 001068 ( Main/Curation ); précédent : 001067; suivant : 001069Inhibitory glutamate receptor channels
Auteurs : Thomas A. Cleland [États-Unis]Source :
- Molecular Neurobiology [ 0893-7648 ] ; 1996-10-01.
Abstract
Abstract: Inhibitory glutamate receptors (IGluRs) are a family of ion channel proteins closely related to ionotropic glycine and γ-aminobutyric acid (GABA) receptors; They are gated directly by glutamate; the open channel is permeable to chloride and sometimes potassium. Physiologically and pharmacologically, IGluRs most closely resemble GABA receptors; they are picrotoxin-sensitive and sometimes crossdesensitized by GABA. However, the amino acid sequences of cloned IGluRs are most similar to those of glycine receptors. Ibotenic acid, a conformationally restricted glutamate analog closely related to muscimol, activates all IGluRs. Quisqualate is not an IGluR agonist except among pulmonate molluscs and for a unique multiagonist receptor in the crayfishAustropotamobius torrentium. Other excitatory amino acid agonists are generally ineffective. Avermectins have several effects on IGluRs, depending on concentration: potentiation, direct gating, and blockade, both reversible and irreversible. Since IGluRs have only been clearly described in protostomes and pseudocoelomates, these effects may mediate the powerful antihelminthic and insecticidal action of avermectins, while explaining their low toxicity to mammals. IGluRs mediate synaptic inhibition in neurons and are expressed extrajunctionally in striated muscles. The presence of IGluRs in a neuron or muscle is independent of the presence or absence of excitatory glutamate receptors or GABA receptors in the cell. Generally, extrajunctional IGluRs in muscle have a higher sensitivity to glutamate than do neuronal synaptic receptors. Some extrajunctional receptors are sensitive in the range of circulating plasma glutamate levels, suggesting a role for IGluRs in regulating muscle excitability. The divergence of the IGlu/GABA/Gly/ACh receptor superfamily in protostomes could become a powerful model system for adaptive molecular evolution. Physiologically and pharmacologically, protostome receptors are considerably more diverse than their vertebrate counterparts. Antagonist profiles are only loosely correlated with agonist profiles (e.g., curare-sensitive GABA receptors, bicuculline-sensitive AChRs), and pharmacologically identical receptors may be either excitatory or inhibitory, and permeable to different ions. The assumption that agonist sensitivity reliably connotes discrete, homologous receptor families is contraindicated. Protostome ionotropic receptors are highly diverse and straightforward to assay; they provide an excellent system in which to study and integrate fundamental questions in molecular evolution and adaptation.
Url:
DOI: 10.1007/BF02740637
Links toward previous steps (curation, corpus...)
- to stream Istex, to step Corpus: Pour aller vers cette notice dans l'étape Curation :001805
- to stream Istex, to step Curation: Pour aller vers cette notice dans l'étape Curation :001232
- to stream Istex, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :000909
- to stream Main, to step Merge: Pour aller vers cette notice dans l'étape Curation :001107
Links to Exploration step
ISTEX:C4C61A61A15DF5662672ABD51CFB8DA721EBDA8ELe document en format XML
<record><TEI wicri:istexFullTextTei="biblStruct"><teiHeader><fileDesc><titleStmt><title xml:lang="en">Inhibitory glutamate receptor channels</title>
<author><name sortKey="Cleland, Thomas A" sort="Cleland, Thomas A" uniqKey="Cleland T" first="Thomas A." last="Cleland">Thomas A. Cleland</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">ISTEX</idno>
<idno type="RBID">ISTEX:C4C61A61A15DF5662672ABD51CFB8DA721EBDA8E</idno>
<date when="1996" year="1996">1996</date>
<idno type="doi">10.1007/BF02740637</idno>
<idno type="url">https://api.istex.fr/document/C4C61A61A15DF5662672ABD51CFB8DA721EBDA8E/fulltext/pdf</idno>
<idno type="wicri:Area/Istex/Corpus">001805</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Corpus" wicri:corpus="ISTEX">001805</idno>
<idno type="wicri:Area/Istex/Curation">001232</idno>
<idno type="wicri:Area/Istex/Checkpoint">000909</idno>
<idno type="wicri:explorRef" wicri:stream="Istex" wicri:step="Checkpoint">000909</idno>
<idno type="wicri:doubleKey">0893-7648:1996:Cleland T:inhibitory:glutamate:receptor</idno>
<idno type="wicri:Area/Main/Merge">001107</idno>
<idno type="wicri:Area/Main/Curation">001068</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title level="a" type="main" xml:lang="en">Inhibitory glutamate receptor channels</title>
<author><name sortKey="Cleland, Thomas A" sort="Cleland, Thomas A" uniqKey="Cleland T" first="Thomas A." last="Cleland">Thomas A. Cleland</name>
<affiliation wicri:level="2"><country xml:lang="fr">États-Unis</country>
<placeName><region type="state">Californie</region>
</placeName>
<wicri:cityArea>Biology Department 0357, UCSD, 92093-0357, La Jolla</wicri:cityArea>
</affiliation>
</author>
</analytic>
<monogr></monogr>
<series><title level="j">Molecular Neurobiology</title>
<title level="j" type="abbrev">Mol Neurobiol</title>
<idno type="ISSN">0893-7648</idno>
<idno type="eISSN">1559-1182</idno>
<imprint><publisher>Humana Press</publisher>
<pubPlace>Totowa</pubPlace>
<date type="published" when="1996-10-01">1996-10-01</date>
<biblScope unit="volume">13</biblScope>
<biblScope unit="issue">2</biblScope>
<biblScope unit="page" from="97">97</biblScope>
<biblScope unit="page" to="136">136</biblScope>
</imprint>
<idno type="ISSN">0893-7648</idno>
</series>
<idno type="istex">C4C61A61A15DF5662672ABD51CFB8DA721EBDA8E</idno>
<idno type="DOI">10.1007/BF02740637</idno>
<idno type="ArticleID">BF02740637</idno>
<idno type="ArticleID">Art1</idno>
</biblStruct>
</sourceDesc>
<seriesStmt><idno type="ISSN">0893-7648</idno>
</seriesStmt>
</fileDesc>
<profileDesc><textClass></textClass>
<langUsage><language ident="en">en</language>
</langUsage>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">Abstract: Inhibitory glutamate receptors (IGluRs) are a family of ion channel proteins closely related to ionotropic glycine and γ-aminobutyric acid (GABA) receptors; They are gated directly by glutamate; the open channel is permeable to chloride and sometimes potassium. Physiologically and pharmacologically, IGluRs most closely resemble GABA receptors; they are picrotoxin-sensitive and sometimes crossdesensitized by GABA. However, the amino acid sequences of cloned IGluRs are most similar to those of glycine receptors. Ibotenic acid, a conformationally restricted glutamate analog closely related to muscimol, activates all IGluRs. Quisqualate is not an IGluR agonist except among pulmonate molluscs and for a unique multiagonist receptor in the crayfishAustropotamobius torrentium. Other excitatory amino acid agonists are generally ineffective. Avermectins have several effects on IGluRs, depending on concentration: potentiation, direct gating, and blockade, both reversible and irreversible. Since IGluRs have only been clearly described in protostomes and pseudocoelomates, these effects may mediate the powerful antihelminthic and insecticidal action of avermectins, while explaining their low toxicity to mammals. IGluRs mediate synaptic inhibition in neurons and are expressed extrajunctionally in striated muscles. The presence of IGluRs in a neuron or muscle is independent of the presence or absence of excitatory glutamate receptors or GABA receptors in the cell. Generally, extrajunctional IGluRs in muscle have a higher sensitivity to glutamate than do neuronal synaptic receptors. Some extrajunctional receptors are sensitive in the range of circulating plasma glutamate levels, suggesting a role for IGluRs in regulating muscle excitability. The divergence of the IGlu/GABA/Gly/ACh receptor superfamily in protostomes could become a powerful model system for adaptive molecular evolution. Physiologically and pharmacologically, protostome receptors are considerably more diverse than their vertebrate counterparts. Antagonist profiles are only loosely correlated with agonist profiles (e.g., curare-sensitive GABA receptors, bicuculline-sensitive AChRs), and pharmacologically identical receptors may be either excitatory or inhibitory, and permeable to different ions. The assumption that agonist sensitivity reliably connotes discrete, homologous receptor families is contraindicated. Protostome ionotropic receptors are highly diverse and straightforward to assay; they provide an excellent system in which to study and integrate fundamental questions in molecular evolution and adaptation.</div>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Terre/explor/CobaltMaghrebV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001068 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 001068 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Terre |area= CobaltMaghrebV1 |flux= Main |étape= Curation |type= RBID |clé= ISTEX:C4C61A61A15DF5662672ABD51CFB8DA721EBDA8E |texte= Inhibitory glutamate receptor channels }}
This area was generated with Dilib version V0.6.32. |