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The Journal of Neuroscience, January 15, 1999, 19(2):684-691
Molecular Diversity of the Calcium Channel 2
Subunit
Norbert
Klugbauer,
Lubica
Lacinová,
Elsé
Marais,
Muriel
Hobom, and
Franz
Hofmann
Institut für Pharmakologie und Toxikologie der Technischen
Universität München, 80802 München, Germany
Sequence database searches with the 2 subunit as
probe led to the identification of two new genes encoding proteins with the essential properties of this calcium channel subunit. Primary structure comparisons revealed that the novel 2 -2 and
2 -3 subunits share 55.6 and 30.3% identity with the
2 -1 subunit, respectively. The number of putative
glycosylation sites and cysteine residues, hydropathicity profiles, and
electrophysiological character of the 2 -3 subunit
indicates that these proteins are functional calcium channel subunits.
Coexpression of 2 -3 with 1C and
cardiac 2a or 1E and 3 subunits shifted the
voltage dependence of channel activation and inactivation in a
hyperpolarizing direction and accelerated the kinetics of current
inactivation. The kinetics of current activation were altered only when
2 -1 or 2 -3 was expressed with
1C. The effects of 2 -3 on
1C but not 1E are indistinguishable from
the effects of 2 -1. Using Northern blot analysis, it
was shown that 2 -3 is expressed exclusively in brain,
whereas 2 -2 is found in several tissues. In
situ hybridization of mouse brain sections showed mRNA
expression of 2 -1 and 2 -3 in the
hippocampus, cerebellum, and cortex, with 2 -1
strongly detected in the olfactory bulb and 2 -3 in
the caudate putamen.
Key words:
2 subunit; voltage-activated channel; calcium channel subunit; neuron; gene diversity; electrophysiology
Copyright © 1999 Society for Neuroscience 0270-6474/99/192684-08$05.00/0
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