Calcium channels from Cyprinus carpio skeletal muscle.
AUTOR(ES)
Grabner, M
RESUMO
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.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=50886Documentos Relacionados
- Subunit structure of dihydropyridine-sensitive calcium channels from skeletal muscle.
- Single calcium channels in native sarcoplasmic reticulum membranes from skeletal muscle.
- Calcium channels and intracellular calcium release are pharmacologically different in frog skeletal muscle.
- Calcium-induced calcium release in crayfish skeletal muscle.
- Depletion of calcium from the sarcoplasmic reticulum during calcium release in frog skeletal muscle.