TY - JOUR
T1 - Cloning and characterization of rat transient receptor potential-melastatin 4 (TRPM4)
AU - Yoo, Jae Cheal
AU - Yarishkin, Oleg V.
AU - Hwang, Eun Mi
AU - Kim, Eunju
AU - Kim, Dong Gyu
AU - Park, Nammi
AU - Hong, Seong Geun
AU - Park, Jae Yong
N1 - Funding Information:
This work was supported by the Basic Research Program of the Korea Science & Engineering Foundation (R13-2005-012-02002-0) and a National Research Foundation of Korea Grant (2009-0067148). J.C.Y., E.K., D.K., and N.P. were supported by the Brain Korea 21 Programs.
PY - 2010/1/1
Y1 - 2010/1/1
N2 - Transient receptor potential-melastatin 4 (TRPM4) is a Ca2+-activated, but Ca2+-impermeable, cation channel. Increasing [Ca2+]i induce current activation and reduction through TRPM4 channels. Several TRPM4 isoforms are expressed in mice and humans, but rat TRPM4 (rTRPM4) has not been previously identified. Here, we identified, cloned, and characterized two rTRPM4 isoforms, rTRPM4a and rTRPM4b, using 5′-RACE-PCR. rTRPM4b channel activity increased with [Ca2+]i in a dose-dependent manner. However, the rTRPM4b Ca2+-dependent activity at negative potentials differed from that of human TRPM4b (hTRPM4b), even though both represent full-length proteins. Additionally, rTRPM4b showed a slightly different single-channel current amplitude and open time distribution than hTRPM4b. However, rTRPM4a, which lacks the N-terminal region of rTRPM4b, and hTRPM4a had no similar functional channel activities. Furthermore, we characterized splicing regions, tissue distribution, and cellular localization of these isoforms. Unlike rTRPM4a, rTRPM4b was localized to the membrane at high levels, suggesting that rTRPM4b is the functionally active channel. Crown
AB - Transient receptor potential-melastatin 4 (TRPM4) is a Ca2+-activated, but Ca2+-impermeable, cation channel. Increasing [Ca2+]i induce current activation and reduction through TRPM4 channels. Several TRPM4 isoforms are expressed in mice and humans, but rat TRPM4 (rTRPM4) has not been previously identified. Here, we identified, cloned, and characterized two rTRPM4 isoforms, rTRPM4a and rTRPM4b, using 5′-RACE-PCR. rTRPM4b channel activity increased with [Ca2+]i in a dose-dependent manner. However, the rTRPM4b Ca2+-dependent activity at negative potentials differed from that of human TRPM4b (hTRPM4b), even though both represent full-length proteins. Additionally, rTRPM4b showed a slightly different single-channel current amplitude and open time distribution than hTRPM4b. However, rTRPM4a, which lacks the N-terminal region of rTRPM4b, and hTRPM4a had no similar functional channel activities. Furthermore, we characterized splicing regions, tissue distribution, and cellular localization of these isoforms. Unlike rTRPM4a, rTRPM4b was localized to the membrane at high levels, suggesting that rTRPM4b is the functionally active channel. Crown
KW - Localization
KW - Patch-clamp recording
KW - Race-PCR
KW - hTRPM4
KW - rTRPM4
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U2 - 10.1016/j.bbrc.2009.11.142
DO - 10.1016/j.bbrc.2009.11.142
M3 - Article
C2 - 19945433
AN - SCOPUS:73149121556
VL - 391
SP - 806
EP - 811
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 1
ER -