TY - JOUR
T1 - Genetic characterization of a new splice variant of the β2 subunit of the voltage-dependent calcium channel
AU - Murakami, Manabu
AU - Aoyama, Masahiro
AU - Suzuki, Takashi
AU - Sasano, Hironobu
AU - Nakayama, Shinnsuke
AU - Iijima, Toshihiko
N1 - Funding Information:
We would like to thank Mr. Hirotaka Tanabe for his technical assistance. This research was sponsored partly by grants-in-aid from the Ministry of Education, Science, and Culture, of Japan, and from the Japan Foundation for Cardiovascular Research.
PY - 2003/12
Y1 - 2003/12
N2 - This study reports a novel splice variant form of the voltage-dependent calcium channel β2 subunit (β2g): This variant is composed of the conserved amino-terminal sequences of the β2a subunit, but lacks the β-subunit interaction domain (BID), which is thought essential for interactions with the α1 subunit. Gene structure analysis revealed that this gene was composed of 13 translated exons spread over 107 kb of the genome. The gene structure of the β2 subunit was similar in exon-intron organization to the murine β3 and human β4 subunits. Electrophysiological evaluation revealed that β2a and β2g, affected channel properties in different ways. The β2a subunit increased the peak amplitude, but failed to increase channel inactivation, while β2g had no significant effects on either the peak current amplitude or channel inactivation. Other β subunits, such as β3 and β4, significantly increased the peak current and accelerated current inactivation.
AB - This study reports a novel splice variant form of the voltage-dependent calcium channel β2 subunit (β2g): This variant is composed of the conserved amino-terminal sequences of the β2a subunit, but lacks the β-subunit interaction domain (BID), which is thought essential for interactions with the α1 subunit. Gene structure analysis revealed that this gene was composed of 13 translated exons spread over 107 kb of the genome. The gene structure of the β2 subunit was similar in exon-intron organization to the murine β3 and human β4 subunits. Electrophysiological evaluation revealed that β2a and β2g, affected channel properties in different ways. The β2a subunit increased the peak amplitude, but failed to increase channel inactivation, while β2g had no significant effects on either the peak current amplitude or channel inactivation. Other β subunits, such as β3 and β4, significantly increased the peak current and accelerated current inactivation.
KW - Calcium current
KW - Gene structure
KW - Subunit interaction domain
KW - Voltage-dependent calcium channel
KW - β subunit
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U2 - 10.1023/A:1027316017156
DO - 10.1023/A:1027316017156
M3 - Article
C2 - 14674701
AN - SCOPUS:0344897229
VL - 254
SP - 217
EP - 225
JO - Enzymologia
JF - Enzymologia
SN - 0300-8177
IS - 1-2
ER -