Evidence for the association of dystrophin with the transverse tubular system in skeletal muscle

C. M KNUDSON; Eric P Hoffman; S. D KAHL; L. M KUNKEL; Kevin P Campbell

doi:10.1016/S0021-9258(18)68503-5

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Evidence for the association of dystrophin with the transverse tubular system in skeletal muscle

Journal article

Open access

Peer reviewed

Evidence for the association of dystrophin with the transverse tubular system in skeletal muscle

C. M KNUDSON, Eric P Hoffman, S. D KAHL, L. M KUNKEL and Kevin P Campbell

The Journal of biological chemistry, Vol.263(17), pp.8480-8484

1988

DOI: 10.1016/S0021-9258(18)68503-5

PMID: 3286650

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Abstract

Polyclonal antibodies to dystrophin (the protein product of the human Duchenne muscular dystrophy gene) were used to identify and characterize dystrophin in isolated triads from rabbit skeletal muscle. Anti-dystrophin antibodies recognize an approximately 400,000-Da protein in isolated triads or heavy microsomes from skeletal muscle. Treatment of heavy microsomes with buffers containing high salt or EDTA to remove peripheral or extrinsic membrane proteins does not remove dystrophin; however, treatment of intact triads with trypsin shows that dystrophin is extremely sensitive to mild proteolytic digestion. Isolation of junctional complexes from skeletal muscle triads indicates that dystrophin is tightly associated with the triadic junction. Fractionation of the triadic junction into junctional transverse tubular membranes and junctional sarcoplasmic reticulum membranes has shown that dystrophin is enriched in junctional transverse tubular membranes. Thus, our results suggest that dystrophin is a component of the triad junction which is exposed to the cytoplasm and embedded in or attached to the transverse tubular membrane.

Cell Physiology

Fundamental and applied biological sciences. Psychology

Biological and medical sciences

Molecular and cellular biology

Muscle contraction

Details

Title: Subtitle: Evidence for the association of dystrophin with the transverse tubular system in skeletal muscle
Creators: C. M KNUDSON - Univ. Iowa coll. medicine, dep. physiology biophysics, Iowa City IA 52242, United States
Eric P Hoffman - Harvard Medical School
S. D KAHL - Univ. Iowa coll. medicine, dep. physiology biophysics, Iowa City IA 52242, United States
L. M KUNKEL - Univ. Iowa coll. medicine, dep. physiology biophysics, Iowa City IA 52242, United States
Kevin P Campbell - Univ. Iowa coll. medicine, dep. physiology biophysics, Iowa City IA 52242, United States
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.263(17), pp.8480-8484
DOI: 10.1016/S0021-9258(18)68503-5
PMID: 3286650
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: 1988
Academic Unit: Neurology; Molecular Physiology and Biophysics; Pathology; Iowa Neuroscience Institute; Radiation Oncology
Record Identifier: 9984047700802771

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