Abstract
Transient receptor potential-melastatin 4 (TRPM4) is a Ca 2+ -activated, but Ca 2+ -impermeable, cation channel. Increasing [Ca 2+ ] 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 [Ca 2+ ] i in a dose-dependent manner. However, the rTRPM4b Ca 2+ -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
| Original language | English |
|---|---|
| Pages (from-to) | 806-811 |
| Number of pages | 6 |
| Journal | Biochemical and biophysical research communications |
| Volume | 391 |
| Issue number | 1 |
| DOIs | |
| Publication status | Published - 2010 Jan 1 |
| Externally published | Yes |
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Keywords
- hTRPM4
- Localization
- Patch-clamp recording
- Race-PCR
- rTRPM4
ASJC Scopus subject areas
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Cloning and characterization of rat transient receptor potential-melastatin 4 (TRPM4). / Yoo, Jae Cheal; Yarishkin, Oleg V.; Hwang, Eun Mi; Kim, Eunju; Kim, Dong Gyu; Park, Nammi; Hong, Seong Geun; Park, Jae-Yong.
In: Biochemical and biophysical research communications, Vol. 391, No. 1, 01.01.2010, p. 806-811.Research output: Contribution to journal › Article
}
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
PY - 2010/1/1
Y1 - 2010/1/1
N2 - Transient receptor potential-melastatin 4 (TRPM4) is a Ca 2+ -activated, but Ca 2+ -impermeable, cation channel. Increasing [Ca 2+ ] 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 [Ca 2+ ] i in a dose-dependent manner. However, the rTRPM4b Ca 2+ -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 Ca 2+ -activated, but Ca 2+ -impermeable, cation channel. Increasing [Ca 2+ ] 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 [Ca 2+ ] i in a dose-dependent manner. However, the rTRPM4b Ca 2+ -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 - hTRPM4
KW - Localization
KW - Patch-clamp recording
KW - Race-PCR
KW - rTRPM4
UR - http://www.scopus.com/inward/record.url?scp=73149121556&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=73149121556&partnerID=8YFLogxK
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 -