Heteromerization and colocalization of TrpV1 and TrpV2 in mammalian cell lines and rat dorsal root ganglia

A. Richard Rutter, Qing Ping Ma, Mathew Leveridge, Timothy P. Bonnert

Research output: Journal PublicationArticlepeer-review

73 Citations (Scopus)


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-II dorsal root ganglion hybridoma cells following their transient coexpression. Immunofluorescent labelling of transfected F-II 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 theTrp ion channel family.

Original languageEnglish
Pages (from-to)1735-1739
Number of pages5
Issue number16
Publication statusPublished - 7 Nov 2005
Externally publishedYes


  • Dorsal root ganglion
  • Heat transduction
  • Pain
  • Transient receptor potential
  • Vanilloid receptors

ASJC Scopus subject areas

  • General Neuroscience


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