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Properties of ω conotoxin MVIIC receptors associated with α1A calcium channel subunits in rat brain
Author(s) -
Martin-Moutot Nicole,
Leveque Christian,
Sato Kazuki,
Kato Rika,
Takahashi Masami,
Seagar Michael
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00467-n
Subject(s) - conotoxin , protein subunit , cerebellum , chemistry , receptor , calcium , calcium channel , biophysics , biochemistry , microbiology and biotechnology , biology , peptide , neuroscience , organic chemistry , gene
Solubilized 125 I‐ω conotoxin MVIIC receptors from rat cerebellum were immunoprecipitated by antibodies directed against the calcium channel α1A subunit. Anti‐αIA antibodies recognized a 240‐220, 180 and 160 kDa proteins in immunoblots of cerebellar membranes. Disuccinimidyl suberate cross‐linked 125 I‐ω conotoxin MVIIC to an α2δ‐like 200‐180 kDa subunit, which migrated at 150‐140 kDa after disulfide reduction. These observations are consistent with a heteromeric structure in which high affinity ω conotoxin MVIIC binding sites formed by α1A subunits are located in close proximity to peripheral α2 subunits.