1. TRPV3 is a temperature-sensitive vanilloid receptor-like protein
- Author
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Rosemary E. Kelsell, Andrew D. Randall, K. J. Charles, Jeffrey C. Jerman, James Wright, P. Reilly, Darren Smart, Praveen Anand, Julie Egerton, Paul Facer, Lezanne Ooi, Graham D Smith, Philip David Hayes, John B. Davis, Martin J. Gunthorpe, and Jean-Philippe Walhin
- Subjects
TRPV3 ,Hot Temperature ,Receptors, Drug ,Molecular Sequence Data ,TRPV2 ,TRPV1 ,Sequence Homology ,TRPV Cation Channels ,Biology ,TRPP ,TRPV ,Ion Channels ,Cell Line ,chemistry.chemical_compound ,Dorsal root ganglion ,Ganglia, Spinal ,medicine ,Humans ,Amino Acid Sequence ,RNA, Messenger ,Cloning, Molecular ,Receptor ,Cation Transport Proteins ,Multidisciplinary ,Gene Expression Profiling ,Precipitin Tests ,Cell biology ,Electrophysiology ,Protein Subunits ,medicine.anatomical_structure ,nervous system ,chemistry ,Biochemistry ,Capsaicin ,Calcium ,lipids (amino acids, peptides, and proteins) ,Protons ,Ion Channel Gating ,Protein Binding - Abstract
Vanilloid receptor-1 (VR1, also known as TRPV1) is a thermosensitive, nonselective cation channel that is expressed by capsaicin-sensitive sensory afferents and is activated by noxious heat, acidic pH and the alkaloid irritant capsaicin. Although VR1 gene disruption results in a loss of capsaicin responses, it has minimal effects on thermal nociception. This and other experiments--such as those showing the existence of capsaicin-insensitive heat sensors in sensory neurons--suggest the existence of thermosensitive receptors distinct from VR1. Here we identify a member of the vanilloid receptor/TRP gene family, vanilloid receptor-like protein 3 (VRL3, also known as TRPV3), which is heat-sensitive but capsaicin-insensitive. VRL3 is coded for by a 2,370-base-pair open reading frame, transcribed from a gene adjacent to VR1, and is structurally homologous to VR1. VRL3 responds to noxious heat with a threshold of about 39 degrees C and is co-expressed in dorsal root ganglion neurons with VR1. Furthermore, when heterologously expressed, VRL3 is able to associate with VR1 and may modulate its responses. Hence, not only is VRL3 a thermosensitive ion channel but it may represent an additional vanilloid receptor subunit involved in the formation of heteromeric vanilloid receptor channels.
- Published
- 2002