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lüll TRPV4 calcium entry channel: a paradigm for gating diversity Nilius B; Vriens J; Prenen J; Droogmans G; Voets TAm J Physiol Cell Physiol 2004[Feb]; 286 (2): C195-205The vanilloid receptor-1 (VR1, now TRPV1) was the founding member of a subgroup of cation channels within the TRP family. The TRPV subgroup contains six mammalian members, which all function as Ca2+ entry channels gated by a variety of physical and chemical stimuli. TRPV4, which displays 45% sequence identity with TRPV1, is characterized by a surprising gating promiscuity: it is activated by hypotonic cell swelling, heat, synthetic 4alpha-phorbols, and several endogenous substances including arachidonic acid (AA), the endocannabinoids anandamide and 2-AG, and cytochrome P-450 metabolites of AA, such as epoxyeicosatrienoic acids. This review summarizes data on TRPV4 as a paradigm of gating diversity in this subfamily of Ca2+ entry channels.|Amino Acid Sequence/genetics[MESH]|Animals[MESH]|Calcium/metabolism[MESH]|Cation Transport Proteins/agonists/genetics/*metabolism/physiology[MESH]|Gene Expression[MESH]|Hot Temperature[MESH]|Humans[MESH]|Ion Channel Gating/*physiology[MESH]|Ion Channels/agonists/genetics/*metabolism/physiology[MESH]|Mechanoreceptors/physiology[MESH]|Molecular Sequence Data[MESH]|Osmotic Pressure[MESH]|Phosphorylation[MESH]|TRPV Cation Channels[MESH] |