TRPV4


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TRPV4

A gene on chromosome 12q24.1 that encodes a calcium-permeable, non-selective cation channel thought to be involved in regulating systemic osmotic pressure. It is activated by exposure to hypotonicity within the physiological range, as well as by low pH, citrate and phorbol esters. Channel activity may be a calmodulin-dependent mechanism with a negative feedback control. TRPV4 promotes cell–cell junction formation in the skin and plays an important role in forming and maintaining intercellular barriers; it also regulates intracellular Ca2+ and hypotonic stimulation in synoviocytes and regulates production of IL-8.

Molecular pathology
TRPV4 mutations cause spondylometaphyseal and metatropic dysplasia, and hereditary motor and sensory neuropathy type IIC.
References in periodicals archive ?
Confocal imaging was conducted after immunocytochemical staining for acetylated [alpha]-tubulin, PLC[beta]3, TRPV4, and PAR-2.
After stringency washing, complexes were investigated by Western blotting using antibodies specific for TRPV4, PAR-2, or calmodulin.
Using MMP-1 reporter assays, we found that TRPV4-specific siRNA decreased MMP-1 transcriptional activation, thus implying that TRPV4 is critical for DEP/ OE-evoked [Ca.
TRPV4 activation by 4[alpha]-PDD or hypotonicity strongly increased MMP-1 secretion, indicating that in airway epithelia, TRPV4 activation is sufficient to up-regulate MMP-1 (Figure 3D).
Taken together, these findings point toward critical functioning of TRPV4 in [Ca.
TRPV4 signaling complex is located on motile cilia of primary human airway epithelia.
Because TRPV4 channels have been found in primary motile cilia of mouse tracheal epithelia (Lorenzo et al.
i]) via disinhibited TRPV4 and/or activation of PLC[beta]3, both of which have previously been shown to bind calmodulin.
2+] influx via TRPV4 causes MMP-1 activation rationalizes airway injury by MMP-1 as caused by TRPV4 channel activity, not by DN channels, we attempted to resolve these seemingly contradictory concepts.
2+] influx mediated by TRPV4 channels, via membrane phospholipid signaling involving PLC[beta]3 and PI3-K.
The critical participants of the DEP response, PAR-2, PLC[beta]3, and TRPV4, were localized to motile cilia of differentiated primary human respiratory epithelia.
Two possible causes for the slow kinetics are a) DEP-dependent PLC[beta]3 phosphorylation, and b) DEP-enhanced calmodulin binding to a receptor-signaling multiplex containing TRPV4 and PLC[beta]3 (Figures 5, 7), both of which attenuate signaling via known properties of the modified phospholipase or channel.