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Jon D Levine - One of the best experts on this subject based on the ideXlab platform.
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molecular cloning of an n terminal splice variant of the capsaicin Receptor loss of n terminal domain suggests functional divergence among capsaicin Receptor subtypes
Journal of Biological Chemistry, 2000Co-Authors: Mark Schumacher, Irene Moff, Sharmila P Sudanagunta, Jon D LevineAbstract:Recently a cDNA clone, Vanilloid Receptor subtype-1 (VR1), was isolated and found to encode an ion channel that is activated by both capsaicin, the pain producing compound in chili peppers, and by noxious thermal stimuli. Subsequently, two related cDNAs have been isolated, a stretch inactivating channel with mechanosensitive properties and a Vanilloid Receptor-like protein that is responsive to high temperatures (52-53 degrees C). Here, we report the isolation of a Vanilloid Receptor 5'-splice variant (VR.5'sv) which differs from VR1 by elimination of the majority of the intracellular N-terminal domain and ankyrin repeat elements. Both VR.5'sv and VR1 mRNA were shown to be expressed in tissues reportedly responsive to capsaicin including dorsal root ganglion, brain, and peripheral blood mononuclear cells. Functional expression of VR.5'sv in Xenopus oocytes and mammalian cells showed no sensitivity to capsaicin, the potent Vanilloid resiniferatoxin, hydrogen ions (pH 6.2), or noxious thermal stimuli (50 degrees C). Since VR.5'sv is otherwise identical to VR1 throughout its transmembrane spanning domains and C-terminal region, these results support the hypothesis that the N-terminal intracellular domain is essential for the formation of functional Receptors activated by Vanilloid compounds and noxious thermal stimuli.
Mark Schumacher - One of the best experts on this subject based on the ideXlab platform.
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molecular cloning of an n terminal splice variant of the capsaicin Receptor loss of n terminal domain suggests functional divergence among capsaicin Receptor subtypes
Journal of Biological Chemistry, 2000Co-Authors: Mark Schumacher, Irene Moff, Sharmila P Sudanagunta, Jon D LevineAbstract:Recently a cDNA clone, Vanilloid Receptor subtype-1 (VR1), was isolated and found to encode an ion channel that is activated by both capsaicin, the pain producing compound in chili peppers, and by noxious thermal stimuli. Subsequently, two related cDNAs have been isolated, a stretch inactivating channel with mechanosensitive properties and a Vanilloid Receptor-like protein that is responsive to high temperatures (52-53 degrees C). Here, we report the isolation of a Vanilloid Receptor 5'-splice variant (VR.5'sv) which differs from VR1 by elimination of the majority of the intracellular N-terminal domain and ankyrin repeat elements. Both VR.5'sv and VR1 mRNA were shown to be expressed in tissues reportedly responsive to capsaicin including dorsal root ganglion, brain, and peripheral blood mononuclear cells. Functional expression of VR.5'sv in Xenopus oocytes and mammalian cells showed no sensitivity to capsaicin, the potent Vanilloid resiniferatoxin, hydrogen ions (pH 6.2), or noxious thermal stimuli (50 degrees C). Since VR.5'sv is otherwise identical to VR1 throughout its transmembrane spanning domains and C-terminal region, these results support the hypothesis that the N-terminal intracellular domain is essential for the formation of functional Receptors activated by Vanilloid compounds and noxious thermal stimuli.
C.a. Maggi - One of the best experts on this subject based on the ideXlab platform.
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Ruthenium red as a capsaicin antagonist.
Life sciences, 1991Co-Authors: Rainer Amann, C.a. MaggiAbstract:Definition of the physiological and pharmacological properties of primary afferent neurons by the use of capsaicin and its analogues (e.g. resiniferatoxin) has represented one of the most active areas of research of the last decade (1-4 for reviews). In the past 3 years many important advancements have been made in this field, dealing with: a) discovery of the capsaicin (or 'Vanilloid' Receptor (5); b) discovery of capsazepine as a competitive Receptor antagonist at the Vanilloid Receptor (6); c) definition of the cation channel coupled with the Vanilloid Receptor and the ionic basis for excitation and "desensitization" of primary afferents by capsaicin and related substances (7,8) and d) discovery of ruthenium red as a functional capsaicin antagonist. The aim of the present article is to briefly review the pharmacology of ruthenium red as a capsaicin antagonist and attempting to define the usefulness and the limits of this substance as a tool in sensory neuron research.
Irene Moff - One of the best experts on this subject based on the ideXlab platform.
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molecular cloning of an n terminal splice variant of the capsaicin Receptor loss of n terminal domain suggests functional divergence among capsaicin Receptor subtypes
Journal of Biological Chemistry, 2000Co-Authors: Mark Schumacher, Irene Moff, Sharmila P Sudanagunta, Jon D LevineAbstract:Recently a cDNA clone, Vanilloid Receptor subtype-1 (VR1), was isolated and found to encode an ion channel that is activated by both capsaicin, the pain producing compound in chili peppers, and by noxious thermal stimuli. Subsequently, two related cDNAs have been isolated, a stretch inactivating channel with mechanosensitive properties and a Vanilloid Receptor-like protein that is responsive to high temperatures (52-53 degrees C). Here, we report the isolation of a Vanilloid Receptor 5'-splice variant (VR.5'sv) which differs from VR1 by elimination of the majority of the intracellular N-terminal domain and ankyrin repeat elements. Both VR.5'sv and VR1 mRNA were shown to be expressed in tissues reportedly responsive to capsaicin including dorsal root ganglion, brain, and peripheral blood mononuclear cells. Functional expression of VR.5'sv in Xenopus oocytes and mammalian cells showed no sensitivity to capsaicin, the potent Vanilloid resiniferatoxin, hydrogen ions (pH 6.2), or noxious thermal stimuli (50 degrees C). Since VR.5'sv is otherwise identical to VR1 throughout its transmembrane spanning domains and C-terminal region, these results support the hypothesis that the N-terminal intracellular domain is essential for the formation of functional Receptors activated by Vanilloid compounds and noxious thermal stimuli.
Sharmila P Sudanagunta - One of the best experts on this subject based on the ideXlab platform.
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molecular cloning of an n terminal splice variant of the capsaicin Receptor loss of n terminal domain suggests functional divergence among capsaicin Receptor subtypes
Journal of Biological Chemistry, 2000Co-Authors: Mark Schumacher, Irene Moff, Sharmila P Sudanagunta, Jon D LevineAbstract:Recently a cDNA clone, Vanilloid Receptor subtype-1 (VR1), was isolated and found to encode an ion channel that is activated by both capsaicin, the pain producing compound in chili peppers, and by noxious thermal stimuli. Subsequently, two related cDNAs have been isolated, a stretch inactivating channel with mechanosensitive properties and a Vanilloid Receptor-like protein that is responsive to high temperatures (52-53 degrees C). Here, we report the isolation of a Vanilloid Receptor 5'-splice variant (VR.5'sv) which differs from VR1 by elimination of the majority of the intracellular N-terminal domain and ankyrin repeat elements. Both VR.5'sv and VR1 mRNA were shown to be expressed in tissues reportedly responsive to capsaicin including dorsal root ganglion, brain, and peripheral blood mononuclear cells. Functional expression of VR.5'sv in Xenopus oocytes and mammalian cells showed no sensitivity to capsaicin, the potent Vanilloid resiniferatoxin, hydrogen ions (pH 6.2), or noxious thermal stimuli (50 degrees C). Since VR.5'sv is otherwise identical to VR1 throughout its transmembrane spanning domains and C-terminal region, these results support the hypothesis that the N-terminal intracellular domain is essential for the formation of functional Receptors activated by Vanilloid compounds and noxious thermal stimuli.
