Identification and characterization of the high affinity [3H]ryanodine receptor of the junctional sarcoplasmic reticulum Ca2+ release channel

Kevin P Campbell; C Michael Knudson; Toshiaki Imagawa; Albert T Leung; John L Sutko; Steven D Kahl; Carol Reynolds Raab; Linda Madson

doi:10.1016/S0021-9258(18)48263-4

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Identification and characterization of the high affinity [3H]ryanodine receptor of the junctional sarcoplasmic reticulum Ca2+ release channel

Journal article

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Identification and characterization of the high affinity [3H]ryanodine receptor of the junctional sarcoplasmic reticulum Ca2+ release channel

Kevin P Campbell, C Michael Knudson, Toshiaki Imagawa, Albert T Leung, John L Sutko, Steven D Kahl, Carol Reynolds Raab and Linda Madson

The Journal of biological chemistry, Vol.262(14), pp.6460-6463

1987

DOI: 10.1016/S0021-9258(18)48263-4

PMID: 2437119

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Abstract

The high affinity ryanodine receptor of the Ca2+ release channel from junctional sarcoplasmic reticulum of rabbit skeletal muscle has been identified and characterized using monoclonal antibodies. Anti-ryanodine receptor monoclonal antibody XA7 specifically immunoprecipitated [3H]ryanodine-labeled receptor from digitonin-solubilized triads in a dose-dependent manner. [3H]Ryanodine binding to the immunoprecipitated receptor from unlabeled digitonin-solubilized triads was specific, Ca2+-dependent, stimulated by millimolar ATP, and inhibited by micromolar ruthenium red. Indirect immunoperoxidase staining of nitrocellulose blots of various skeletal muscle membrane fractions has demonstrated that anti-ryanodine receptor monoclonal antibody XA7 recognizes a high molecular weight protein (approximately 350,000 Da) which is enriched in isolated triads but absent from light sarcoplasmic reticulum vesicles and transverse tubular membrane vesicles. Thus, our results demonstrate that monoclonal antibodies to the approximately 350,000-Da junctional sarcoplasmic reticulum protein immunoprecipitated the ryanodine receptor with properties identical to those expected for the ryanodine receptor of the Ca2+ release channel.

Cell Physiology

Fundamental and applied biological sciences. Psychology

Biological and medical sciences

Molecular and cellular biology

Muscle contraction

Details

Title: Subtitle: Identification and characterization of the high affinity [3H]ryanodine receptor of the junctional sarcoplasmic reticulum Ca2+ release channel
Creators: Kevin P Campbell - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
C Michael Knudson - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
Toshiaki Imagawa - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
Albert T Leung - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
John L Sutko - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
Steven D Kahl - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
Carol Reynolds Raab - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
Linda Madson - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.262(14), pp.6460-6463
DOI: 10.1016/S0021-9258(18)48263-4
PMID: 2437119
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: American Society for Biochemistry and Molecular Biology; Bethesda, MD
Language: English
Date published: 1987
Academic Unit: Neurology; Molecular Physiology and Biophysics; Psychiatry; Pathology; Iowa Neuroscience Institute; Radiation Oncology
Record Identifier: 9984047868202771

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