Biochemical characterization and ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin)

C Michael Knudson; Kristin K Stang; Annelise O Jorgensen; Kevin P Campbell

doi:10.1016/S0021-9258(18)31436-4

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Biochemical characterization and ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin)

Journal article

Open access

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Biochemical characterization and ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin)

C Michael Knudson, Kristin K Stang, Annelise O Jorgensen and Kevin P Campbell

The Journal of biological chemistry, Vol.268(17), pp.12637-12645

1993

DOI: 10.1016/S0021-9258(18)31436-4

PMID: 8389762

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Abstract

Monoclonal antibodies were used to identify a 94-kDa protein that was greatly enriched in traids and junctional face membranes (9.3 +/- 0.2%) but not detected in the transverse tubular and nonjunctional sarcoplasmic reticulum membranes. The 94-kDa protein is a hydrophobic glycoprotein based on endoglycosidase H sensitivity, concanavalin A binding, and labelling with a hydrophobic probe. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis in the absence and presence of reducing agents suggests that this protein is present as a population of multimeric structures containing a variable number of the 94-kDa subunits. Immunofluorescent staining of serial transverse sections of skeletal muscle shows staining of all fiber types with preferential staining of type II fast fibers. Specific immunofluorescence staining in longitudinal sections of skeletal muscle is confined to the interface between the A- and I-bands where the triad structures are localized. Immunocolloidal gold labeling revealed the 94-kDa glycoprotein to be localized over a region of the junctional sarcoplasmic reticulum where the ryanodine receptor/Ca2+ release channel is localized. The distribution and high abundance of the 94-kDa glycoprotein in the junctional membrane suggest that it performs a structural or functional role in the storage or release of calcium from the junctional sarcoplasmic reticulum in skeletal muscle.

Fundamental and applied biological sciences. Psychology

Proteins

Biological and medical sciences

Glycoproteins

Analytical, structural and metabolic biochemistry

Details

Title: Subtitle: Biochemical characterization and ultrastructural localization of a major junctional sarcoplasmic reticulum glycoprotein (triadin)
Creators: C Michael Knudson - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. physiology biophysics, Iowa City IA 52242, United States
Kristin K Stang - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. physiology biophysics, Iowa City IA 52242, United States
Annelise O Jorgensen - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. physiology biophysics, Iowa City IA 52242, United States
Kevin P Campbell - Univ. Iowa coll. medicine, Howard Hughes medical inst., dep. physiology biophysics, Iowa City IA 52242, United States
Resource Type: Journal article
Publication Details: The Journal of biological chemistry, Vol.268(17), pp.12637-12645
DOI: 10.1016/S0021-9258(18)31436-4
PMID: 8389762
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: 1993
Academic Unit: Neurology; Molecular Physiology and Biophysics; Pathology; Iowa Neuroscience Institute; Radiation Oncology
Record Identifier: 9984047631502771

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