Identification and characterization of the murine TRPM4 channel |
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Authors: | Murakami Manabu Xu Feng Miyoshi Ichiro Sato Eisaku Ono Kyoichi Iijima Toshihiko |
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Affiliation: | Department of Pharmacology, Akita University School of Medicine, 1-1-1, Hondou, Akita 010-8543, Japan. manabumurakami@excite.co.jp |
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Abstract: | 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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Keywords: | Melastatin Transient receptor potential Gene structure Calcium entry cDNA |
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