| First Author | Nilius B | Year | 2004 |
| Journal | Am J Physiol Cell Physiol | Volume | 286 |
| Issue | 2 | Pages | C195-205 |
| PubMed ID | 14707014 | Mgi Jnum | J:87931 |
| Mgi Id | MGI:3028709 | Doi | 10.1152/ajpcell.00365.2003 |
| Citation | Nilius B, et al. (2004) TRPV4 calcium entry channel: a paradigm for gating diversity. Am J Physiol Cell Physiol 286(2):C195-205 |
| abstractText | The 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. |
