Molecular architecture of the vanilloid receptor. Insights for drug design.
作者： Antonio Ferrer-Montiel , Carolina Garcia-Martinez , Cruz Morenilla-Palao , Nuria Garcia-Sanz , Asia Fernandez-Carvajal
DOI: 10.1111/J.1432-1033.2004.04083.X
关键词: Chemistry 、 Hyperalgesia 、 Biochemistry 、 Biophysics 、 Nociceptor 、 Transient receptor potential channel 、 Ionotropic effect 、 Receptor 、 Druggability 、 Molecular model 、 TRPV1
摘要: The transient receptor potential channel vanilloid subunit 1 (TRPV1) is a molecular integrator of physical and chemical stimuli in the peripheral nociceptor terminals. TRPV1 an ionotropic that plays critical role both thermal nociception inflammatory hyperalgesia. Structure-function relationships are providing fundamental insights modular architecture this neuronal receptor. As result, determinants endow with its physiological properties, namely activation by heat, potentiation extracellular acidic pH, interaction vanilloid-like compounds, as well permeation properties being unveiled. This information can now be used to build up models for protein which, upon experimental validation, could tools thrust target-oriented design druggable ligands.
sci-hub.se 参考文章(31)
David Julius, Allan I. Basbaum, Molecular mechanisms of nociception Nature. ,vol. 413, pp. 203- 210 ,(2001) , 10.1038/35093019
Holger Husi, Seth G.N Grant, Proteomics of the nervous system Trends in Neurosciences. ,vol. 24, pp. 259- 266 ,(2001) , 10.1016/S0166-2236(00)01792-6
G. Bhave, H.-J. Hu, K. S. Glauner, W. Zhu, H. Wang, D. J. Brasier, G. S. Oxford, R. W. Gereau, Protein kinase C phosphorylation sensitizes but does not activate the capsaicin receptor transient receptor potential vanilloid 1 (TRPV1) Proceedings of the National Academy of Sciences of the United States of America. ,vol. 100, pp. 12480- 12485 ,(2003) , 10.1073/PNAS.2032100100
L. A. Birder, A. J. Kanai, W. C. de Groat, S. Kiss, M. L. Nealen, N. E. Burke, K. E. Dineley, S. Watkins, I. J. Reynolds, M. J. Caterina, Vanilloid receptor expression suggests a sensory role for urinary bladder epithelial cells. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 98, pp. 13396- 13401 ,(2001) , 10.1073/PNAS.231243698
Siân I. Jaggar, Helena C.F. Scott, Iain F. James, Andrew S.C. Rice, The capsaicin analogue SDZ249-665 attenuates the hyper-reflexia and referred hyperalgesia associated with inflammation of the rat urinary bladder. Pain. ,vol. 89, pp. 229- 235 ,(2001) , 10.1016/S0304-3959(00)00366-3
J. M. Welch, S. A. Simon, P. H. Reinhart, The activation mechanism of rat vanilloid receptor 1 by capsaicin involves the pore domain and differs from the activation by either acid or heat Proceedings of the National Academy of Sciences of the United States of America. ,vol. 97, pp. 13889- 13894 ,(2000) , 10.1073/PNAS.230146497
Marc Jenke, Araceli Sánchez, Francisco Monje, Walter Stühmer, Rüdiger M Weseloh, Luis A Pardo, C-terminal domains implicated in the functional surface expression of potassium channels The EMBO Journal. ,vol. 22, pp. 395- 403 ,(2003) , 10.1093/EMBOJ/CDG035
Kaori Inoue, Schuichi Koizumi, Shigeyoshi Fuziwara, Sumiko Denda, Kazuhide Inoue, Mitsuhiro Denda, Functional vanilloid receptors in cultured normal human epidermal keratinocytes Biochemical and Biophysical Research Communications. ,vol. 291, pp. 124- 129 ,(2002) , 10.1006/BBRC.2002.6393
Thomas Voets, Jean Prenen, Joris Vriens, Hiroyuki Watanabe, Annelies Janssens, Ulrich Wissenbach, Matthias Bödding, Guy Droogmans, Bernd Nilius, Molecular determinants of permeation through the cation channel TRPV4. Journal of Biological Chemistry. ,vol. 277, pp. 33704- 33710 ,(2002) , 10.1074/JBC.M204828200
Michela Rigoni, Marcello Trevisani, David Gazzieri, Riccardo Nadaletto, Michele Tognetto, Christophe Creminon, John B Davis, Barbara Campi, Silvia Amadesi, Pierangelo Geppetti, Selena Harrison, Neurogenic responses mediated by vanilloid receptor-1 (TRPV1) are blocked by the high affinity antagonist, iodo-resiniferatoxin. British Journal of Pharmacology. ,vol. 138, pp. 977- 985 ,(2003) , 10.1038/SJ.BJP.0705110