Activation of protein kinase C sensitizes human VR1 to capsaicin and to moderate decreases in pH at physiological temperatures inXenopusoocytes
- 1 July 2002
- journal article
- Published by Wolters Kluwer Health
- Vol. 98 (1-2) , 109-117
- https://doi.org/10.1016/s0304-3959(02)00034-9
Abstract
The two-electrode voltage-clamp technique was used to evaluate the effect of protein kinase C (PKC) activation on ion current flow in Xenopus laevis oocytes injected with cRNA coding for the human vanilloid receptor (VR1). In the presence of 30 nM phorbol-12,13-dibutyrate (PDBu), current evoKeywords
This publication has 24 references indexed in Scilit:
- Bradykinin and nerve growth factor release the capsaicin receptor from PtdIns(4,5)P2-mediated inhibitionNature, 2001
- The Tissue Distribution and Functional Characterization of Human VR1Biochemical and Biophysical Research Communications, 2001
- Chronic Hypersensitivity For Inflammatory Nociceptor Sensitization Mediated by the ε Isozyme of Protein Kinase CJournal of Neuroscience, 2000
- Vanilloid receptor-1 is essential for inflammatory thermal hyperalgesiaNature, 2000
- Impaired Nociception and Pain Sensation in Mice Lacking the Capsaicin ReceptorScience, 2000
- Sense and specificity: a molecular identity for nociceptorsCurrent Opinion in Neurobiology, 1999
- Specific Involvement of PKC-ε in Sensitization of the Neuronal Response to Painful HeatNeuron, 1999
- A capsaicin-receptor homologue with a high threshold for noxious heatNature, 1999
- The capsaicin receptor: a heat-activated ion channel in the pain pathwayNature, 1997
- A novel heat-activated current in nociceptive neurons and its sensitization by bradykininProceedings of the National Academy of Sciences, 1996