Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum

Wei Guo; Annelise O Jorgensen; Kevin P Campbell

doi:10.1016/S0021-9258(18)46936-0

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Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum

Journal article

Open access

Peer reviewed

Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum

Wei Guo, Annelise O Jorgensen and Kevin P Campbell

The Journal of biological chemistry, Vol.269(45), pp.28359-28365

11/11/1994

DOI: 10.1016/S0021-9258(18)46936-0

PMID: 7961775

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Abstract

Monoclonal antibodies were used to identify and characterize a novel 90 kDa protein that was specifically localized to the junctional sarcoplasmic reticulum of rabbit skeletal muscle. Biochemical experiments show that the 90 kDa protein is an integral membrane protein of the junctional face membrane and is a substrate for the intrinsic protein kinase in triads. Immunofluorescence staining of serial transverse sections of skeletal muscle with a monoclonal antibody to the 90 kDa protein showed preferential staining of type II "fast" fibers. Specific labeling was confined to the interphase between the A- and I-bands, where the triad structure is localized. Immunoelectron microscopical labeling further indicates that the 90 kDa protein, like the ryanodine receptor/Ca(2+)-release channel and triadin, is confined to the terminal cisternae of the sarcoplasmic reticulum. Western blot analysis with a combination of monoclonal antibodies against the 90 kDa protein shows that it is specifically expressed in skeletal muscle but not in cardiac muscle or brain. Similarly, specific immunofluorescence labeling to the 90 kDa protein was not detected in ventricular myocytes or vascular smooth muscle cells. The junctional localization and phosphorylation of this protein suggest that it may play an important regulatory or structural role in the skeletal muscle triad junction.

Phosphorylation

Rabbits

Cell Fractionation

Molecular Weight

Phosphoproteins - biosynthesis

Muscles - ultrastructure

Electrophoresis, Polyacrylamide Gel

Antibodies, Monoclonal

Microscopy, Electron

Phosphoproteins - metabolism

Blotting, Western

Microscopy, Immunoelectron

Muscle Proteins - biosynthesis

Brain - metabolism

Animals

Phosphoproteins - analysis

Muscle Fibers, Skeletal - ultrastructure

Muscle Proteins - analysis

Myocardium - metabolism

Muscle Proteins - metabolism

Sarcoplasmic Reticulum - ultrastructure

Sarcoplasmic Reticulum - metabolism

Muscles - metabolism

Details

Title: Subtitle: Characterization and ultrastructural localization of a novel 90-kDa protein unique to skeletal muscle junctional sarcoplasmic reticulum
Creators: Wei Guo - Howard Hughes Medical Institute, University of Iowa, College of Medicine, Iowa City 52242
Annelise O Jorgensen
Kevin P Campbell
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.269(45), pp.28359-28365
DOI: 10.1016/S0021-9258(18)46936-0
PMID: 7961775
NLM abbreviation: J Biol Chem
ISSN: 0021-9258
eISSN: 1083-351X
Publisher: United States
Language: English
Date published: 11/11/1994
Academic Unit: Neurology; Molecular Physiology and Biophysics; Iowa Neuroscience Institute
Record Identifier: 9984068367902771

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