Secondary Logo

Journal Logo

Institutional members access full text with Ovid®

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

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

doi: 10.1097/01.wnr.0000185958.03841.0f
SOMATOSENSORY SYSTEMS, PAIN
Buy

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.

Department of Molecular and Cellular Neuroscience, Neuroscience Research Centre, Merck Sharp and Dohme Research Laboratories, Harlow, Essex, UK

Correspondence and requests for reprints to Dr A. Richard Rutter, Department of Molecular and Cellular Neuroscience, Neuroscience Research Centre, Merck Sharp and Dohme Research Laboratories, Terlings Park, Harlow, Essex CM20 2QR, UK

Tel: +44 1279 440000; fax: +44 1279 440390; e-mail: richard_rutter@merck.com

Received 18 August 2005; accepted 1 September 2005

© 2005 Lippincott Williams & Wilkins, Inc.