Source:http://linkedlifedata.com/resource/pubmed/id/17881091
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2008-1-18
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pubmed:abstractText |
The presence and roles of N-glycosylation of the human (h) 5-ht(5A) receptor were investigated using a heterologous expression system. Following transient transfection of COS-7 cells with h5-ht(5A) receptor cDNA, SDS-PAGE/Western blot analysis of immunoreactivity demonstrated two protein species; a predominant species with a molecular weight of approximately 35-45 kDa and a minor species of approximately 45-55 kDa. Transfected cells grown in the presence of the N-glycosylation inhibitor tunicamycin, failed to express the minor immunoreactive species indicating this represented the N-glycosylated form of the h5-ht(5A) receptor. Comparison of the molecular weights of immunoreactive bands arising from the wild-type and each of the mutant 5-ht(5A) receptors with disruption of the predicted N-glycosylation sites (N6S and N21S) demonstrated that both identified asparagines were N-glycosylated. Immunocytochemical and ELISA studies demonstrated that the [N6S]h5-ht(5A) receptor mutation, but not the [N21S]h5-ht(5A) receptor mutation, reduced protein expression in the cell membrane, indicating that N-glycosylation of the N6 residue is important for the membrane expression of this neurotransmitter receptor; a requirement for receptor function.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Nitrogen,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Isoforms,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Serotonin,
http://linkedlifedata.com/resource/pubmed/chemical/Serotonin,
http://linkedlifedata.com/resource/pubmed/chemical/Tunicamycin,
http://linkedlifedata.com/resource/pubmed/chemical/serotonin 5 receptor
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pubmed:status |
MEDLINE
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pubmed:month |
Feb
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pubmed:issn |
0197-0186
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
52
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
419-25
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pubmed:meshHeading |
pubmed-meshheading:17881091-Animals,
pubmed-meshheading:17881091-Brain,
pubmed-meshheading:17881091-COS Cells,
pubmed-meshheading:17881091-Cercopithecus aethiops,
pubmed-meshheading:17881091-Glycosylation,
pubmed-meshheading:17881091-Humans,
pubmed-meshheading:17881091-Molecular Weight,
pubmed-meshheading:17881091-Mutation,
pubmed-meshheading:17881091-Neurons,
pubmed-meshheading:17881091-Nitrogen,
pubmed-meshheading:17881091-Protein Isoforms,
pubmed-meshheading:17881091-Receptors, Serotonin,
pubmed-meshheading:17881091-Serotonin,
pubmed-meshheading:17881091-Synaptic Transmission,
pubmed-meshheading:17881091-Transfection,
pubmed-meshheading:17881091-Tunicamycin
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pubmed:year |
2008
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pubmed:articleTitle |
Identification and functional significance of N-glycosylation of the 5-ht5A receptor.
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pubmed:affiliation |
Cellular and Molecular Neuropharmacology Research Group, Division of Neuroscience, The Medical School, University of Birmingham, Edgbaston, Birmingham B15 2TT, UK.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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