Properties of omega conotoxin MVIIC receptors associated with alpha 1A calcium channel subunits in rat brain

FEBS Lett. 1995 Jun 5;366(1):21-5. doi: 10.1016/0014-5793(95)00467-n.

Abstract

Solubilized 125I-omega conotoxin MVIIC receptors from rat cerebellum were immunoprecipitated by antibodies directed against the calcium channel alpha 1A subunit. Anti-alpha 1A antibodies recognized a 240-220, 180 and 160 kDa proteins in immunoblots of cerebellar membranes. Disuccinimidyl suberate cross-linked 125I-omega conotoxin MVIIC to an alpha 2 delta-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 omega conotoxin MVIIC binding sites formed by alpha 1A subunits are located in close proximity to peripheral alpha 2 subunits.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Affinity Labels
  • Animals
  • Binding Sites
  • Brain / metabolism*
  • Calcium Channels / chemistry
  • Calcium Channels / metabolism*
  • Cerebellum / metabolism
  • Cross-Linking Reagents
  • Immunoblotting
  • In Vitro Techniques
  • Membranes / metabolism
  • Molecular Structure
  • Molecular Weight
  • Mollusk Venoms / metabolism
  • Peptides / metabolism*
  • Precipitin Tests
  • Protein Conformation
  • Rats
  • Rats, Wistar
  • Solubility
  • Succinimides
  • omega-Conotoxins*

Substances

  • Affinity Labels
  • Calcium Channels
  • Cross-Linking Reagents
  • Mollusk Venoms
  • Peptides
  • Succinimides
  • omega-Conotoxins
  • omega-conotoxin receptor
  • omega-conotoxin-MVIIC
  • disuccinimidyl suberate