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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
1998-10-2
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pubmed:abstractText |
Comparison of the pharmacological effects of a range of sulphur-containing amino acids on human mGluR1alpha and mGluR5a has been undertaken. cDNAs of each mGluR were transfected into a Syrian hamster tumour cell line AV12-664 that was previously transfected with the rat glutamate-aspartate transporter protein (GLAST). The L-isomers of cysteine sulphinic acid (CSA), homocysteine sulphinic acid (HCSA), cysteic acid (CA) and serine-O-sulphate (SOS) stimulated PI hydrolysis in human mGluR1alpha and mGluR5a cells with full agonist effects. D-CSA, the only active D-isomer, was a partial agonist for mGluR5a whereas L-sulphocysteine (S-CYS) showed weak agonist-like effects at high concentrations on both mGluR1alpha and mGluR5a. L-Homocysteic acid was inactive on both mGluR1alpha and mGluR5a cells. Treatment of mGluR cultures with glutamate pyruvate transaminase did not alter the potencies of the S-amino acids on PI hydrolysis responses. Inhibitor constants (Ki) obtained for L-HCSA, L-CSA, L-CA and L-SOS in [3H]glutamate receptor binding studies with mGluR1alpha cells indicated that L-HCSA, L-CSA, L-CA and L-SOS can bind specifically to mGluR1 with L-HCSA showing the highest affinity. These results confirm that certain endogenously produced S-amino acids may interact directly with group 1 mGluRs.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Amino Acids, Sulfur,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Cysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamic Acid,
http://linkedlifedata.com/resource/pubmed/chemical/Homocysteine,
http://linkedlifedata.com/resource/pubmed/chemical/Neurotransmitter Agents,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphatidylinositols,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Metabotropic Glutamate,
http://linkedlifedata.com/resource/pubmed/chemical/Serine,
http://linkedlifedata.com/resource/pubmed/chemical/cysteine sulfinic acid,
http://linkedlifedata.com/resource/pubmed/chemical/homocysteinesulfinic acid,
http://linkedlifedata.com/resource/pubmed/chemical/metabotropic glutamate receptor 5,
http://linkedlifedata.com/resource/pubmed/chemical/metabotropic glutamate receptor...,
http://linkedlifedata.com/resource/pubmed/chemical/serine O-sulfate
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pubmed:status |
MEDLINE
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pubmed:issn |
0028-3908
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
37
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
277-87
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9681926-Amino Acids, Sulfur,
pubmed-meshheading:9681926-Animals,
pubmed-meshheading:9681926-Cell Line,
pubmed-meshheading:9681926-Cricetinae,
pubmed-meshheading:9681926-Cysteic Acid,
pubmed-meshheading:9681926-Cysteine,
pubmed-meshheading:9681926-Glutamic Acid,
pubmed-meshheading:9681926-Homocysteine,
pubmed-meshheading:9681926-Humans,
pubmed-meshheading:9681926-Mesocricetus,
pubmed-meshheading:9681926-Neurotransmitter Agents,
pubmed-meshheading:9681926-Phosphatidylinositols,
pubmed-meshheading:9681926-Receptors, Metabotropic Glutamate,
pubmed-meshheading:9681926-Serine
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pubmed:year |
1998
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pubmed:articleTitle |
Sulphur-containing amino acids are agonists for group 1 metabotropic receptors expressed in clonal RGT cell lines.
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pubmed:affiliation |
Lilly Research Centre, Eli Lilly, Windlesham, Surrey, UK.
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pubmed:publicationType |
Journal Article,
Comparative Study
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