Fibroblasts were re-suspended and cultured in DMEM media containing 10% FBS, or used freshly for patch-clamp experiments (Du = is the effect at concentration is the Hill coefficient (Jiang 0


Fibroblasts were re-suspended and cultured in DMEM media containing 10% FBS, or used freshly for patch-clamp experiments (Du = is the effect at concentration is the Hill coefficient (Jiang 0.05 indicated statistical significance. Results SPH is a potent endogenous inhibitor of TRPM7 TRPM7 exhibits various physiological/pathological functions including embryonic development (Jin = 6). to that of SPH. In contrast, FTY720-P has no effect on TRPM7. It appears that SPH and FTY720 inhibit TRPM7 by reducing channel open probability. Furthermore, endogenous TRPM7 in cardiac fibroblasts was markedly inhibited by SPH, DMS and FTY720. Conclusions and Implications This is the first study demonstrating that SPH and FTY720 are potent inhibitors Entacapone sodium salt of TRPM7. Our results not only provide a new modulation mechanism of TRPM7, but also suggest that TRPM7 may serve as a direct target of SPH and FTY720, thereby mediating S1P-independent physiological/pathological functions of SPH and FTY720. Linked Article This article is commented on by Rohacs, pp. 1291C1293 of this issue. To view this commentary visit http://dx.doi.org/10.1111/bph.12070 and exerts its potential physiological/pathological functions, we investigated the effects of two bioactive sphingolipids, sphingosine (SPH) and its phosphorylated form sphingosine-1-phosphate (S1P), on TRPM7 currents over-expressed Entacapone sodium salt in HEK293 cells and on endogenous TRPM7 currents in cardiac fibroblasts. SPH and S1P are potent bioactive sphingolipids which are associated with Entacapone sodium salt a vast number of cellular and biological processes such as cell survival, apoptosis, senescence, differentiation, proliferation, mitogenesis, inflammation and angiogenesis (Hannun and Obeid, 2008; Pyne and Pyne, 2010). SPH is a metabolite generated during the de novo synthesis of cellular sphingolipids (Hannun by SK2 (Zemann (Nagaoka and functions independent of S1P receptors (Pyne and Pyne, 2010). Therefore, in addition to the functions mediated by S1PRs, FTY720 may exert physiological, pathological and therapeutic functions through its own targets. A previous study has demonstrated that SPH activates TRPM3 (Grimm for 10 min. Fibroblasts were re-suspended and cultured in DMEM media containing 10% FBS, or used freshly for patch-clamp experiments (Du = is the effect at concentration is the Hill coefficient (Jiang 0.05 indicated statistical significance. Results SPH is a potent endogenous inhibitor of TRPM7 TRPM7 exhibits various physiological/pathological functions including embryonic development (Jin = 6). No statistical difference was observed. (F) Concentration-dependent effects of SPH on TRPM7. The best fit of doseCresponse curve yielded IC50 = 0.59 0.02 M (= 6 at each concentration). Although it seems that the inward and outward currents were blocked in parallel (Figure 1C,D), we analysed whether there was a voltage-dependent block as we previously reported (Li = 5 cells were tested for each compound). SPH can be further Spry4 phosphorylated by sphingosine kinases 1 and 2 (SphK 1, SphK 2) to produce sphingosine-1-phosphate (S1P), Entacapone sodium salt a potent bioactive lipid that activates S1P receptors and exhibits a broad spectrum of biological activities including cell proliferation, survival, migration, cytoskeletal organization and morphogenesis. Thus, we determined to test whether S1P could directly inhibit TRPM7 activity. As shown in Figure 3E,F, S1P at 10 M failed to produce any noticeable effects on TRPM7 over-expressed in HEK-293 cells, indicating that SPH, but not its phosphorylated form S1P, is a potent inhibitor of TRPM7. Structurally related analogue of SPH strongly inhibited TRPM7 The Entacapone sodium salt inhibitory effects of SPH, but not S1P or ceramides, on TRPM7 suggest that there might be a structure requirement for SPH to block TRPM7. Therefore, we tested the effects of other structurally related analogues of SPH on TRPM7 (Figure 2). DMS is a competitive inhibitor of sphingosine kinase. Interestingly, we found that DMS completely blocked TRPM7 currents at 1 M (Figure 4). Both inward and outward currents of TRPM7 were efficiently inhibited by DMS (Figure 4B,C). The IC50 obtained from the best fit of the concentration-dependent curve was 0.3 M, similar to the IC50 of.