Identification of three subunits of the high affinity ω-conotoxin MVIIC-sensitive Ca 2 + channel

Hongyan Liu, Michel De Waard, Victoria E.S. Scott, Christina A. Gurnett, Vanda A. Lennon, Kevin P. Campbell

Research output: Contribution to journalArticlepeer-review

120 Scopus citations


N-, P- and Q-type voltage-dependent Ca2+ channels control neurotransmitter release in the nervous system and are blocked by ω-conotoxin MVIIC. In this study, both a high affinity and a low affinity binding site for ω-conotoxin MVIIC were detected in rabbit brain. The low affinity binding site is shown to be present on the N-type Ca2+ channel. Using optimized conditions for specific labeling of the high affinity ω-conotoxin MVIIC receptor and a panel of subunit specific antibodies, the molecular structure of the high affinity receptor was investigated. We demonstrate for the first time that this receptor is composed of at least α1A, α2δ, and any one of the four brain β subunits. Such association of different β subunits with α1A and α2δ components may produce Ca2+ channels with distinct functional properties, such as P- and Q-type.

Original languageEnglish (US)
Pages (from-to)13804-13810
Number of pages7
JournalJournal of Biological Chemistry
Issue number23
StatePublished - 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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