Open AccessCalcium channels from Cyprinus carpio skeletal muscle.
Author(s) -
Manfred Grabner,
K. Friedrich,
HansGünther Knaus,
Jörg Striessnig,
F Scheffauer,
Robert Staudinger,
Walter J. Koch,
Arnold Schwartz,
Hartmut Glossmann
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.3.727
Subject(s) - biology , complementary dna , peptide sequence , carp , skeletal muscle , microbiology and biotechnology , biochemistry , amino acid , protein subunit , scn3a , g alpha subunit , gene , anatomy , fishery , fish <actinopterygii>
The complete amino acid sequence of the L-type calcium channel alpha 1 subunit from the carp (Cyprinus carpio) white skeletal muscle was deduced by cDNA cloning and sequence analysis. The open reading frame encodes 1852 amino acids (Mr 210,060). A 155-amino acid COOH-terminal sequence (after the fourth internal repeat) is evolutionarily preserved (90% homology) and may represent an important functional domain of L-type calcium channels. The photolabeled, membrane-bound, and purified carp alpha 1 subunits have masses of 211 and 190 kDa. The purified channel could not be phosphorylated by cAMP-dependent protein kinase. Two glycoproteins (alpha 2 subunits) are associated with the alpha 1 subunit and change their apparent masses from 235 and 220 kDa to 159 kDa upon reduction of disulfide bonds. Nucleic acid hybridization with alpha 2 cDNA revealed an 8.0-kilobase transcript in carp skeletal muscle. Evidence for a copurification of subunits similar in size to mammalian beta or gamma subunits was not obtained.