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IS3 peptide‐formed ion channels in rat skeletal muscle cell membranes
Author(s) -
Bao Lin,
Miao Zhen-Wei,
Zhou Pei-Ai,
Jiang Yun,
Sha Yin-Lin,
Zhang Ren-Ji,
Tang You-Chi
Publication year - 1999
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)00249-5
Subject(s) - membrane , ion channel , chemistry , sodium channel , peptide , patch clamp , membrane potential , biophysics , ion , sodium , biochemistry , biology , receptor , organic chemistry
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 μM 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.