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Publication : Identification and characterization of the murine TRPM4 channel.

First Author  Murakami M Year  2003
Journal  Biochem Biophys Res Commun Volume  307
Issue  3 Pages  522-8
PubMed ID  12893253 Mgi Jnum  J:84948
Mgi Id  MGI:2670842 Doi  10.1016/s0006-291x(03)01186-0
Citation  Murakami M, et al. (2003) Identification and characterization of the murine TRPM4 channel. Biochem Biophys Res Commun 307(3):522-8
abstractText  The transient receptor potential (TRP) channels form a superfamily with six transmembrane structures, which is common in other types of voltage-dependent channels. The TRP-melastatin (TRPM) subfamily includes the putative tumor-suppressor melastatin, which was originally found as a down-regulated protein in melanoma tumor cell lines. Here, we report a novel TRP-related protein that is a murine orthologue of human TRPM4. The function of the novel murine TRPM4 was studied in HEK-293 cells using a fluorescent calcium indicator, fura-2. The removal and re-introduction of extracellular calcium triggered changes in the intracellular calcium only in cells expressing TRPM4a, which suggests that this novel channel plays a role in the calcium entry process. We also isolated a splice variant of TRPM4 that was proven to be non-functional. Both TRPM4 variants integrated into the plasma membrane. Furthermore, FRET analysis revealed that TRPM4a and TRPM4b localized close together, suggesting a multimerization of the two molecules.
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