TY - JOUR
T1 - Spontaneous single-channel activity of neuronal TRP5 channel recombinantly expressed in HEK293 cells
AU - Yamada, Hisanobu
AU - Wakamori, Minoru
AU - Hara, Yuji
AU - Takahashi, Yasuo
AU - Konishi, Kazuhiko
AU - Imoto, Keiji
AU - Mori, Yasuo
N1 - Funding Information:
This study was supported by research grants from the Ministry of Education, Science, Sports, and Culture of Japan, and by ‘the Research for the Future Program’ of the Japan Society for the Promotion of Science, and by the research grant for cardiovascular diseases from the Ministry of Health and Welfare of Japan. We thank Drs Brian Seed and Gary Yellen for the CD8 expression plasmid.
PY - 2000/5/12
Y1 - 2000/5/12
N2 - Mammalian homologues of the Drosophila transient receptor potential (trp) protein (TRP) form Ca2+ permeable cation channels activated in response to stimulation of G-protein-coupled receptors. Establishing biophysical characteristics of basal TRP activity is of great importance in understanding modulatory processes, which underlie enhancement of TRP activity via receptor stimulation. We have examined spontaneous activity of the TRP5 channel recombinantly expressed in human embryonic kidney cells, using the conventional whole-cell mode of the patch-clamp technique in a low- Ca2+ external solution. The unitary Na+ conductance of the TRP5 channel was linear, being 47.6 pS. By contrast, the open probability of the TRP5 channel showed a voltage-dependent decrease below -50 mV. These biophysical properties are important hallmarks in distinguishing the TRP5 channel in native neuronal preparations, whose spontaneous activity may contribute to control of resting membrane potentials and generation of action potentials. (C) 2000 Elsevier Science Ireland Ltd.
AB - Mammalian homologues of the Drosophila transient receptor potential (trp) protein (TRP) form Ca2+ permeable cation channels activated in response to stimulation of G-protein-coupled receptors. Establishing biophysical characteristics of basal TRP activity is of great importance in understanding modulatory processes, which underlie enhancement of TRP activity via receptor stimulation. We have examined spontaneous activity of the TRP5 channel recombinantly expressed in human embryonic kidney cells, using the conventional whole-cell mode of the patch-clamp technique in a low- Ca2+ external solution. The unitary Na+ conductance of the TRP5 channel was linear, being 47.6 pS. By contrast, the open probability of the TRP5 channel showed a voltage-dependent decrease below -50 mV. These biophysical properties are important hallmarks in distinguishing the TRP5 channel in native neuronal preparations, whose spontaneous activity may contribute to control of resting membrane potentials and generation of action potentials. (C) 2000 Elsevier Science Ireland Ltd.
KW - Cation channel
KW - HEK293 cell
KW - Patch clamp
KW - Receptor-activated channel
KW - Single-channel recording
KW - Transient receptor potential protein
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U2 - 10.1016/S0304-3940(00)01033-8
DO - 10.1016/S0304-3940(00)01033-8
M3 - Article
C2 - 10793239
AN - SCOPUS:0034640157
SN - 0304-3940
VL - 285
SP - 111
EP - 114
JO - Neuroscience Letters
JF - Neuroscience Letters
IS - 2
ER -