Loading…

Spontaneous single-channel activity of neuronal TRP5 channel recombinantly expressed in HEK293 cells

Mammalian homologues of the Drosophila transient receptor potential ( trp) protein (TRP) form Ca 2+ 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 mo...

Full description

Saved in:
Bibliographic Details
Published in:Neuroscience letters 2000-05, Vol.285 (2), p.111-114
Main Authors: Yamada, Hisanobu, Wakamori, Minoru, Hara, Yuji, Takahashi, Yasuo, Konishi, Kazuhiko, Imoto, Keiji, Mori, Yasuo
Format: Article
Language:English
Subjects:
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Mammalian homologues of the Drosophila transient receptor potential ( trp) protein (TRP) form Ca 2+ 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-Ca 2+ 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.
ISSN:0304-3940
1872-7972
DOI:10.1016/S0304-3940(00)01033-8