Journal article
Identification of Three Subunits of the High Affinity ω-Conotoxin MVIIC-sensitive Ca2+ Channel
The Journal of biological chemistry, Vol.271(23), pp.13804-13810
06/07/1996
DOI: 10.1074/jbc.271.23.13804
PMID: 8662888
Abstract
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.
Details
- Title: Subtitle
- Identification of Three Subunits of the High Affinity ω-Conotoxin MVIIC-sensitive Ca2+ Channel
- Creators
- Hongyan Liu - Howard Hughes Medical Institute, Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Michel De Waard - Howard Hughes Medical Institute, Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Victoria E.S Scott - Howard Hughes Medical Institute, Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Christina A Gurnett - Howard Hughes Medical Institute, Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242Vanda A Lennon - Neuroimmunology Laboratory, Departments of Immunology and Neurology, Mayo Clinic, Rochester, Minnesota 55905Kevin P Campbell - Howard Hughes Medical Institute, Department of Physiology and Biophysics, University of Iowa College of Medicine, Iowa City, Iowa 52242
- Resource Type
- Journal article
- Publication Details
- The Journal of biological chemistry, Vol.271(23), pp.13804-13810
- DOI
- 10.1074/jbc.271.23.13804
- PMID
- 8662888
- NLM abbreviation
- J Biol Chem
- ISSN
- 0021-9258
- eISSN
- 1083-351X
- Publisher
- Elsevier Inc
- Language
- English
- Date published
- 06/07/1996
- Academic Unit
- Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
- Record Identifier
- 9984068271502771
Metrics
13 Record Views