Extensive co‐localization and heteromultimer formation of the vanilloid receptor‐like protein TRPV2 and the capsaicin receptor TRPV1 in the adult rat cerebral cortex

Extensive co‐localization and heteromultimer formation of the vanilloid receptor‐like protein... The capsaicin receptor TRPV1, a member of the transient receptor potential (TRP) family of calcium‐selective ion channels, responds to noxious stimuli and is predominantly expressed in nociceptive neurons. The homologous receptor TRPV2 shows wide tissue distribution including some sensory neurons, where it is proposed to function as a heat sensor or a growth‐factor‐activated channel. Members of the TRP family of channels have been shown to interact, resulting in hybrid channels with new properties. We examined the possibility of multimer formation between TRPV1 and TRPV2, using biochemical techniques. We present evidence that TRPV1 and TRPV2 can heteromultimerize efficiently in vitro. By using immunohistochemistry we detected co‐localization of the two receptors in rat dorsal root ganglia. TRPC4 transcripts are also detected in capsaicin‐sensitive dorsal root ganglia neurons. We extended the search for TRPV1–TRPV2 co‐localization in the brain, where we detected extensive co‐expression of the two receptors in the IV, V and VI layer neurons of the adult rat cerebral cortex. Co‐immunoprecipitation experiments confirmed the interaction of the two receptors in vivo, indicating heteromultimer formation in native tissue. Formation of heteromultimers between vanilloid receptors may increase the functional diversity of this receptor family. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png European Journal of Neuroscience Wiley

Extensive co‐localization and heteromultimer formation of the vanilloid receptor‐like protein TRPV2 and the capsaicin receptor TRPV1 in the adult rat cerebral cortex

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Publisher
Wiley
Copyright
Copyright © 2005 Wiley Subscription Services, Inc., A Wiley Company
ISSN
0953-816X
eISSN
1460-9568
DOI
10.1111/j.1460-9568.2005.04270.x
pmid
16115206
Publisher site
See Article on Publisher Site

Abstract

The capsaicin receptor TRPV1, a member of the transient receptor potential (TRP) family of calcium‐selective ion channels, responds to noxious stimuli and is predominantly expressed in nociceptive neurons. The homologous receptor TRPV2 shows wide tissue distribution including some sensory neurons, where it is proposed to function as a heat sensor or a growth‐factor‐activated channel. Members of the TRP family of channels have been shown to interact, resulting in hybrid channels with new properties. We examined the possibility of multimer formation between TRPV1 and TRPV2, using biochemical techniques. We present evidence that TRPV1 and TRPV2 can heteromultimerize efficiently in vitro. By using immunohistochemistry we detected co‐localization of the two receptors in rat dorsal root ganglia. TRPC4 transcripts are also detected in capsaicin‐sensitive dorsal root ganglia neurons. We extended the search for TRPV1–TRPV2 co‐localization in the brain, where we detected extensive co‐expression of the two receptors in the IV, V and VI layer neurons of the adult rat cerebral cortex. Co‐immunoprecipitation experiments confirmed the interaction of the two receptors in vivo, indicating heteromultimer formation in native tissue. Formation of heteromultimers between vanilloid receptors may increase the functional diversity of this receptor family.

Journal

European Journal of NeuroscienceWiley

Published: Aug 1, 2005

References

  • RGA protein associates with a TRPV ion channel during biosynthesis and trafficking
    Barnhill, Barnhill; Stokes, Stokes; Koblan‐Huberson, Koblan‐Huberson; Shimoda, Shimoda; Muraguchi, Muraguchi; Adra, Adra; Turner, Turner
  • Actions of two naturally occurring saturated N‐acyldopamines on transient receptor potential vanilloid 1 (TRPV1) channels
    De Petrocellis, De Petrocellis; Chu, Chu; Moriello, Moriello; Kellner, Kellner; Walker, Walker; Di Marzo, Di Marzo
  • Homo‐ and heterotetrameric architecture of the epithelial Ca 2+ channels TRPV5 and TRPV6
    Hoenderop, Hoenderop; Voets, Voets; Hoefs, Hoefs; Weidema, Weidema; Prenen, Prenen; Nilius, Nilius; Bindels, Bindels
  • VR1 protein expression increases in undamaged DRG neurons after partial nerve injury
    Hudson, Hudson; Bevan, Bevan; Wotherspoon, Wotherspoon; Gentry, Gentry; Fox, Fox; Winter, Winter
  • TRPV2‐immunoreactive intrinsic neurons in the rat intestine
    Kashiba, Kashiba; Uchida, Uchida; Takeda, Takeda; Nishigori, Nishigori; Ueda, Ueda; Kuribayashi, Kuribayashi; Ohshima, Ohshima
  • Simultaneous reorganization in thalamocortical ensembles evolves over several hours after perioral capsaicin injections
    Katz, Katz; Simon, Simon; Moody, Moody; Nicolelis, Nicolelis
  • Capsaicin as a source for painful stimulation in functional MRI
    Malisza, Malisza; Docherty, Docherty
  • Characterisation using FLIPR of human vanilloid VR1 receptor pharmacology
    Smart, Smart; Jerman, Jerman; Gunthorpe, Gunthorpe; Brough, Brough; Ranson, Ranson; Cairns, Cairns; Hayes, Hayes; Randall, Randall; Davis, Davis
  • A TRPV2‐PKA signaling module for transduction of physical stimuli in mast cells
    Stokes, Stokes; Shimoda, Shimoda; Koblan‐Huberson, Koblan‐Huberson; Adra, Adra; Turner, Turner
  • Formation of a physiological complex between TRPV2 and RGA protein promotes cell surface expression of TRPV2
    Stokes, Stokes; Wakano, Wakano; Del Carmen, Del Carmen; Koblan‐Huberson, Koblan‐Huberson; Turner, Turner

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