Identification and characterization of the dihydropyridine-binding subunit of the skeletal muscle dihydropyridine receptor

Alan H Sharp; Toshiaki Imagawa; Albert T Leung; Kevin P Campbell

doi:10.1016/S0021-9258(18)45353-7

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Identification and characterization of the dihydropyridine-binding subunit of the skeletal muscle dihydropyridine receptor

Journal article

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Identification and characterization of the dihydropyridine-binding subunit of the skeletal muscle dihydropyridine receptor

Alan H Sharp, Toshiaki Imagawa, Albert T Leung and Kevin P Campbell

The Journal of biological chemistry, Vol.262(25), pp.12309-12315

1987

DOI: 10.1016/S0021-9258(18)45353-7

PMID: 3040737

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Abstract

Photoaffinity labeling of isolated triads and purified dihydropyridine receptor with [3H]azidopine and (+)-[3H]PN200-110 has been used to identify and characterize the dihydropyridine-binding subunit of the 1,4-dihydropyridine receptor of rabbit skeletal muscle. The 1,4-dihydropyridine receptor purified from rabbit skeletal muscle triads contains four protein subunits of 175,000, 170,000, 52,000, and 32,000 Da (Leung, A., Imagawa, T., and Campbell, K. P. (1987) J. Biol. Chem. 262, 7943-7946). Photoaffinity labeling of isolated triads with [3H]azidopine resulted in specific and covalent incorporation of [3H]azidopine into only the 170,000-Da subunit of the dihydropyridine receptor and not into the 175,000-Da glycoprotein subunit of the receptor. The [3H]azidopine-labeled 170,000-Da subunit was separated from the 175,000-Da glycoprotein subunit by sequential elution from a wheat germ agglutinin-Sepharose column with 1% sodium dodecyl sulfate followed by 200 mM N-acetylglucosamine. Photoaffinity labeling of purified dihydropyridine receptor with [3H]azidopine or (+)-[3H]PN200-110 also resulted in the specific and covalent incorporation of either ligand into only the 170,000-Da subunit. Therefore, our results show that the dihydropyridine-binding subunit of the skeletal muscle 1,4-dihydropyridine receptor is the 170,000-Da subunit and not the 175,000-Da glycoprotein subunit.

Fundamental and applied biological sciences. Psychology

Biological and medical sciences

Cell receptors

Molecular and cellular biology

Cell structures and functions

Details

Title: Subtitle: Identification and characterization of the dihydropyridine-binding subunit of the skeletal muscle dihydropyridine receptor
Creators: Alan H Sharp - 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
Kevin P Campbell - Univ. Iowa, dep. physiology biophysics, Iowa City IA 52242, United States
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.262(25), pp.12309-12315
DOI: 10.1016/S0021-9258(18)45353-7
PMID: 3040737
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; Iowa Neuroscience Institute
Record Identifier: 9984068261202771

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