TY - JOUR
T1 - Identification and characterization of the murine TRPM4 channel
AU - Murakami, Manabu
AU - Xu, Feng
AU - Miyoshi, Ichiro
AU - Sato, Eisaku
AU - Ono, Kyoichi
AU - Iijima, Toshihiko
N1 - Funding Information:
This research was partly sponsored by Grants-in-Aid from the Ministry of Education, Science and Culture, Japan, and from the Japan Foundation for Cardiovascular Research.
PY - 2003/8/1
Y1 - 2003/8/1
N2 - 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.
AB - 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.
KW - Calcium entry
KW - Gene structure
KW - Melastatin
KW - Transient receptor potential
KW - cDNA
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U2 - 10.1016/S0006-291X(03)01186-0
DO - 10.1016/S0006-291X(03)01186-0
M3 - Article
C2 - 12893253
AN - SCOPUS:0042171503
VL - 307
SP - 522
EP - 528
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 3
ER -