High molecular weight proteins in cardiac and skeletal muscle junctional sarcoplasmic reticulum vesicles bind calmodulin, are phosphorylated, and are degraded by Ca2+-activated protease

S. Seiler, A. D. Wegener, D. D. Whang, D. R. Hathaway, Larry Jones

Research output: Contribution to journalArticle

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Abstract

A unique set of high molecular weight proteins was identified in junctional sarcoplasmic reticulum (SR) vesicles isolated from both cardiac muscle and skeletal muscle. These high M(r) proteins were not present in free SR vesicles isolated from either tissue, nor were they observed in purified sarcolemmal fractions. The junctional SR high M(r) proteins migrated as doublets in sodium dodecyl sulfate-polyacrylamide gels and exhibited apparent M(r) values between 290,000 and 350,000. The high M(r) proteins bound calmodulin; they were the principal proteins labeled in the cardiac and skeletal muscle SR subfractions by azido-125I-calmodulin. The high M(r) proteins were also substrates for an endogenous Ca2+-calmodulin-dependent protein kinase activity, as well as exogenously added catalytic subunit of cAMP-dependent protein kinase. In addition, the junctional SR high M(r) proteins were the major SR proteins degraded by a Ca2+-activated protease purified from smooth muscle. Control experiments verified the separation of junctional SR vesicles and free SR vesicles from both muscle types. Junctional SR vesicles were enriched in calsequestrin, and they exhibited Ca2+ uptake which was stimulated up to 10-fold by either ryanodine or ruthenium red. Free SR vesicles were deficient in calsequestrin and were insensitive to these two agents. Localization of the cardiac and skeletal muscle high M(r) proteins to the junctional SR, coupled with demonstration of their nearly identical biochemical properties, suggests that the proteins are homologous and are likely to have similar functions in both types of striated muscle.

Original languageEnglish (US)
Pages (from-to)8550-8557
Number of pages8
JournalJournal of Biological Chemistry
Volume259
Issue number13
StatePublished - 1984
Externally publishedYes

Fingerprint

Calpain
Sarcoplasmic Reticulum
Calmodulin
Muscle
Myocardium
Skeletal Muscle
Molecular Weight
Molecular weight
Proteins
Calsequestrin
Ruthenium Red
Ryanodine
Calcium-Calmodulin-Dependent Protein Kinases
Striated Muscle
Cyclic AMP-Dependent Protein Kinases
Sodium Dodecyl Sulfate
Smooth Muscle
Demonstrations
Catalytic Domain
Tissue

ASJC Scopus subject areas

  • Biochemistry

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High molecular weight proteins in cardiac and skeletal muscle junctional sarcoplasmic reticulum vesicles bind calmodulin, are phosphorylated, and are degraded by Ca2+-activated protease. / Seiler, S.; Wegener, A. D.; Whang, D. D.; Hathaway, D. R.; Jones, Larry.

In: Journal of Biological Chemistry, Vol. 259, No. 13, 1984, p. 8550-8557.

Research output: Contribution to journalArticle

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