The diversity in the vanilloid (TRPV) receptor family of ion channels

MJ Gunthorpe, CD Benham, A Randall… - Trends in pharmacological …, 2002 - cell.com
Trends in pharmacological sciences, 2002cell.com
Following cloning of the vanilloid receptor 1 (VR1) at least four other related proteins have
been identified. Together, these form a distinct subgroup of the transient receptor potential
(TRP) family of ion channels. Members of the vanilloid receptor family (TRPV) are activated
by a diverse range of stimuli, including heat, protons, lipids, phorbols, phosphorylation,
changes in extracellular osmolarity and/or pressure, and depletion of intracellular Ca 2+
stores. However, VR1 remains the only channel activated by vanilloids such as capsaicin …
Abstract
Following cloning of the vanilloid receptor 1 (VR1) at least four other related proteins have been identified. Together, these form a distinct subgroup of the transient receptor potential (TRP) family of ion channels. Members of the vanilloid receptor family (TRPV) are activated by a diverse range of stimuli, including heat, protons, lipids, phorbols, phosphorylation, changes in extracellular osmolarity and/or pressure, and depletion of intracellular Ca2+ stores. However, VR1 remains the only channel activated by vanilloids such as capsaicin. These channels are excellent molecular candidates to fulfil a range of sensory and/or cellular roles that are well characterized physiologically. Furthermore, as novel pharmacological targets, the vanilloid receptors have potential for the development of many future disease treatments.
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