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(Received for publication, September 10, 1996, and in revised form, November 14, 1996)
From the Department of Pharmacology, University of Bern,
CH-3010 Bern, Switzerland
The pore-forming
Volume 272, Number 6,
Issue of February 7, 1997
pp. 3560-3566
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
ROLE OF THE CARBOXYL-TERMINAL REGION ENCODED BY EXONS 40-42 IN
1C SUBUNIT IN THE KINETICS AND Ca2+
DEPENDENCE OF INACTIVATION
1C subunit is the
principal component of the voltage-sensitive L-type Ca2+
channel. It has a long cytoplasmic carboxyl-terminal tail playing a
critical role in channel gating. The expression of 1C
subunits is characterized by alternative splicing, which generates its multiple isoforms. cDNA cloning points to a diversity of human hippocampus 1C transcripts in the region of exons 40-43
that encode a part of the 662-amino acid carboxyl terminus. We compared electrophysiological properties of the well defined 2138-amino acid
1C,77 channel isoform with two splice variants,
1C,72 and 1C,86. They contain alterations
in the carboxyl terminus due to alternative splicing of exons 40-42.
The 2157-amino acid 1C,72 isoform contains an insertion
of 19 amino acids at position 1575. The 2139-amino acid
1C,86 has 80 amino acids replaced in positions 1572-1651 of 1C,77 by a non-identical sequence of 81 amino acids. When expressed in Xenopus oocytes, all three
splice variants retained high sensitivity toward dihydropyridine
blockers but showed large differences in gating properties. Unlike
1C,77 and 1C,72, Ba2+
currents (IBa) through 1C,86
inactivated 8-10 times faster at +20 mV, and its inactivation rate was
strongly voltage-dependent. Compared to
1C,77, the inactivation curves of
IBa through 1C,86 and
1C,72 channels were shifted toward more negative
voltages by 11 and 6 mV, respectively. Unlike 1C,77 and
1C,72, the 1C,86 channel lacks a
Ca2+-dependent component of inactivation. Thus
the segment 1572-1651 of the cytoplasmic tail of 1C is
critical for the kinetics as well as for the Ca2+ and
voltage dependence of L-type Ca2+ channel gating.
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