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Received for publication August 30, 2004.
Revised November 18, 2004.
Accepted for publication November 18, 2004.
TRPM3, a member of the melastatin-like transient receptor potential channel subfamily (TRPM), is predominantly expressed in human kidney and brain. TRPM3 mediates spontaneous Ca2+ entry and nonselective cation currents in transiently transfected HEK293 cells. Using measurements with the Ca2+-sensitive fluorescent dye fura-2 and the whole-cell patch clamp technique, we found that D-erythro-sphingosine, a metabolite arising during the de novo synthesis of cellular sphingolipids, activated TRPM3. Other TRP channels tested (TRPC3, TRPC4, TRPC5, TRPV4, TRPV5, TRPV6 and TRPM2) did not significantly respond to application of sphingosine. Sphingosine-induced TRPM3 activation was not mediated by inhibition of protein kinase C, depletion of intracellular Ca2+ stores and intracellular conversion of sphingosine to sphingosine-1-phosphate. While sphingosine-1-phosphate and ceramides had no effect, two structural analogues of sphingosine, dihydro-D-erythro-sphingosine and N,N-dimethyl-D-erythro-sphingosine, also activated TRPM3. Sphingolipids, including sphingosine, are known to have inhibitory effects on a variety of ion channels. Thus, TRPM3 is the first ion channel activated by sphingolipids.
Key words:
Ion channel regulation, Sphingolipids, Ca imaging
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