IS3 peptide-formed ion channels in rat skeletal muscle cell membranes.
A 22-mer peptide, identical to the primary sequence of domain I segment 3 (IS3) of rat brain sodium channel I, was synthesized. With the patch clamp cell-attached technique, single channel currents could be recorded from the patches of cultured rat myotube membranes when the patches were held at hyperpolarized potentials and the electrode solution contained NaCl and 1 microM IS3, indicating that IS3 incorporated into the membranes and formed ion channels. The single channel conductances of IS3 channels were distributed heterogeneously, but mainly in the range of 10-25 pS. There was a tendency that the mean open time and open probability of IS3 channels increased and the mean close time decreased with the increasing of hyperpolarized membrane potentials. IS3 channels are highly selective for Na+ and Li+ but not for Cl- and K+, similar to the authentic Na+ channels.
Bao
L
L
College of Life Sciences, Peking University, Beijing, PR China.
Miao
Z W
ZW
Zhou
P A
PA
Jiang
Y
Y
Sha
Y L
YL
Zhang
R J
RJ
Tang
Y C
YC
D000595:Amino Acid Sequence; D000818:Animals; D002462:Cell Membrane / Q000502:physiology; D008564:Membrane Potentials; D008969:Molecular Sequence Data; D018482:Muscle, Skeletal / Q000166:cytology; D010455:Peptides / Q000502:physiology*; D051381:Rats; D017207:Rats, Sprague-Dawley; D015222:Sodium Channels / Q000502:physiology*
D010455:Peptides; D015222:Sodium Channels