Transient receptor potential protein as a novel non-voltage-gated Ca2+ entry channel involved in diverse pathophysiological functions.

In both excitable and non-excitable cells, many chemical and physical stimuli elicit continuous Ca2+ influx through yet poorly understood pathways distinct from voltage-gated Ca2+ channels, leading to activation and modulation of various cellular functions. The molecular entities of these pathways have long been enigmatic, but important clues have been obtained from recent investigations on the Drosophila transient receptor potential (TRP) protein and its mammalian homologues. TRP proteins function as non-voltage-gated Ca2+ channels that are constitutively active or gated by a multitude of stimuli including light, pheromones, lipids, temperature, acid, osmolarity, and oxidative stress; and thus they may play divergent roles in cell pathophysiology. This short paper briefly overviews the current knowledge about these channels with a main focus on their possible linkage with in vivo function.

[1]  K. Sanders,et al.  TRPC4 currents have properties similar to the pacemaker current in interstitial cells of Cajal. , 2002, American journal of physiology. Cell physiology.

[2]  B. Nilius,et al.  ECaC: the gatekeeper of transepithelial Ca2+ transport. , 2002, Biochimica et biophysica acta.

[3]  J. Cheung,et al.  Erythropoietin Modulates Calcium Influx through TRPC2* , 2002, The Journal of Biological Chemistry.

[4]  M. Caterina,et al.  Altered urinary bladder function in mice lacking the vanilloid receptor TRPV1 , 2002, Nature Neuroscience.

[5]  Makoto Tominaga,et al.  Heat-Evoked Activation of the Ion Channel, TRPV4 , 2002, The Journal of Neuroscience.

[6]  M. Freichel,et al.  Impairment of Store-Operated Ca2+ Entry in TRPC4−/− Mice Interferes With Increase in Lung Microvascular Permeability , 2002, Circulation research.

[7]  P. Anand,et al.  TRPV3 is a temperature-sensitive vanilloid receptor-like protein , 2002, Nature.

[8]  E. Haddad,et al.  Hypomagnesemia with secondary hypocalcemia is caused by mutations in TRPM6, a new member of the TRPM gene family , 2002, Nature Genetics.

[9]  A. Perraud,et al.  TRPM4 Is a Ca2+-Activated Nonselective Cation Channel Mediating Cell Membrane Depolarization , 2002, Cell.

[10]  M. Nowycky,et al.  TRPC4 Can Be Activated by G-protein-coupled Receptors and Provides Sufficient Ca2+ to Trigger Exocytosis in Neuroendocrine Cells* , 2002, The Journal of Biological Chemistry.

[11]  A. Randall,et al.  The diversity in the vanilloid (TRPV) receptor family of ion channels. , 2002, Trends in pharmacological sciences.

[12]  B. Minke,et al.  TRP channel proteins and signal transduction. , 2002, Physiological reviews.

[13]  E. Keverne.  Pheromones, Vomeronasal Function, and Gender-Specific Behavior , 2002, Cell.

[14]  P. McIntyre,et al.  A TRP Channel that Senses Cold Stimuli and Menthol , 2002, Cell.

[15]  M. Nelson,et al.  Transient Receptor Potential Channels Regulate Myogenic Tone of Resistance Arteries , 2002, Circulation research.

[16]  Craig Montell,et al.  A unified nomenclature for the superfamily of TRP cation channels. , 2002, Molecular cell.

[17]  C. Montell,et al.  Regulation of melastatin, a TRP-related protein, through interaction with a cytoplasmic isoform , 2001, Proceedings of the National Academy of Sciences of the United States of America.

[18]  C. Montell.  Physiology, Phylogeny, and Functions of the TRP Superfamily of Cation Channels , 2001, Science's STKE.

[19]  D. Clapham,et al.  The trp ion channel family , 2001, Nature Reviews Neuroscience.

[20]  A. Perraud,et al.  ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology , 2001, Nature.

[21]  M. Nadler,et al.  LTRPC7 is a Mg·ATP-regulated divalent cation channel required for cell viability , 2001, Nature.

[22]  M. Shapero,et al.  Trp-p8, a novel prostate-specific gene, is up-regulated in prostate cancer and other malignancies and shares high homology with transient receptor potential calcium channel proteins. , 2001, Cancer research.

[23]  Y. Hara,et al.  The Transient Receptor Potential Protein Homologue TRP6 Is the Essential Component of Vascular &agr;1-Adrenoceptor–Activated Ca2+-Permeable Cation Channel , 2001, Circulation research.

[24]  RyujiInoue,et al.  The Transient Receptor Potential Protein Homologue TRP6 Is the Essential Component of Vascular α1-Adrenoceptor–Activated Ca2+-Permeable Cation Channel , 2001 .

[25]  M. Biel,et al.  Lack of an endothelial store-operated Ca2+ current impairs agonist-dependent vasorelaxation in TRP4−/− mice , 2001, Nature Cell Biology.

[26]  D. Clapham,et al.  TRP-PLIK, a Bifunctional Protein with Kinase and Ion Channel Activities , 2001, Science.

[27]  G. Schultz,et al.  OTRPC4, a nonselective cation channel that confers sensitivity to extracellular osmolarity , 2000, Nature Cell Biology.

[28]  G. Schultz,et al.  From worm to man: three subfamilies of TRP channels , 2000, Trends in Neurosciences.

[29]  J. Pelletier,et al.  Identification and characterization of MTR1, a novel gene with homology to melastatin (MLSN1) and the trp gene family located in the BWS-WT2 critical region on chromosome 11p15.5 and showing allele-specific expression. , 2000, Human molecular genetics.

[30]  L M Duncan,et al.  Down-regulation of the novel gene melastatin correlates with potential for melanoma metastasis. , 1998, Cancer research.

[31]  E. Kohn,et al.  Structure-function analysis of signal and growth inhibition by carboxyamido-triazole, CAI. , 1994, Cancer research.

[32]  R. Hardie,et al.  Novel Ca2+ channels underlying transduction in Drosophila photoreceptors: implications for phosphoinositide-mediated Ca2+ mobilization , 1993, Trends in Neurosciences.

[33]  J. Fallon,et al.  The Journal of General Physiology , 1919, Botanical Gazette.

[34]  N. Shimizu,et al.  LTRPC2 Ca2+-permeable channel activated by changes in redox status confers susceptibility to cell death. , 2002, Molecular cell.

[35]  Liquan Huang,et al.  A transient receptor potential channel expressed in taste receptor cells , 2002, Nature Neuroscience.