Document Detail

Heteromerization and colocalization of TrpV1 and TrpV2 in mammalian cell lines and rat dorsal root ganglia.
MedLine Citation:
PMID:  16237318     Owner:  NLM     Status:  MEDLINE    
Coassociation of the vanilloid transient receptor potential (Trp) ion channels, TrpV1 and TrpV2, was investigated by immunoprecipitation and immunofluorescence in transfected mammalian cell lines, rat dorsal root ganglia and spinal cord. TrpV1/TrpV2 heteromeric complexes were coimmunoprecipitated from human embryonic kidney cells and F-11 dorsal root ganglion hybridoma cells following their transient coexpression. Immunofluorescent labelling of transfected F-11 cells revealed colocalization of TrpV1 and TrpV2 at the cell surface. Immunoprecipitation from rat dorsal root ganglion lysates identified a minor population of receptor complexes composed of TrpV1/TrpV2 heteromers, consistent with a small proportion of cells double-labelled with TrpV1 and TrpV2 antibodies in rat dorsal root ganglion sections. TrpV1/TrpV2 receptor complexes may represent a functionally distinct ion channel complex that may increase the diversity observed within the Trp ion channel family.
A Richard Rutter; Qing-Ping Ma; Mathew Leveridge; Timothy P Bonnert
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Publication Detail:
Type:  Comparative Study; Journal Article    
Journal Detail:
Title:  Neuroreport     Volume:  16     ISSN:  0959-4965     ISO Abbreviation:  Neuroreport     Publication Date:  2005 Nov 
Date Detail:
Created Date:  2005-10-20     Completed Date:  2006-02-07     Revised Date:  2006-11-15    
Medline Journal Info:
Nlm Unique ID:  9100935     Medline TA:  Neuroreport     Country:  England    
Other Details:
Languages:  eng     Pagination:  1735-9     Citation Subset:  IM    
Department of Molecular and Cellular Neuroscience, Neuroscience Research Centre, Merck Sharp and Dohme Research Laboratories, Harlow, Essex, UK.
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MeSH Terms
Blotting, Western / methods
Cell Line / metabolism
Cells, Cultured
Fluorescent Antibody Technique / methods
Ganglia, Spinal / cytology,  metabolism*
Gene Expression Regulation / physiology*
Immunoprecipitation / methods
Subcellular Fractions / metabolism
TRPV Cation Channels / metabolism*
Transfection / methods
Reg. No./Substance:
0/TRPV Cation Channels; 0/Trpv1 protein, rat; 0/Trpv2 protein, rat

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine

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