Three ryanodine receptor isoforms exist in avian striated muscles

Judith A. Airey, Matthew M. Grinsell, Larry Jones, John L. Sutko, Derrick Witcher

Research output: Contribution to journalArticle

47 Citations (Scopus)

Abstract

Two isoforms of the ryanodine receptor (termed α and β) are coexpressed in avian fast twitch skeletal muscle, whereas a single isoform is expressed in avian cardiac muscle. We have investigated the relationship between these three proteins, comparing several different properties. First, the three receptor isoform subunits have different mobilities on SDS-polyacrylamide gels. Second, monoclonal antibodies against the chicken skeletal muscle receptor isoforms recognize shared and unique epitopes in each receptor protein, indicating there is not a simple antigenic relationship between the isoforms. Third, the three receptor isoforms exhibit different susceptibilities to proteolysis by trypsin, and limited tryptic digestion yields a different peptide map for each isoform. Fourth, in native sarcoplasmic reticulum membranes, the chicken muscle receptor isoforms are phosphorylated to different extents by the multifunctional calcium/ calmodulin-dependent protein kinase II (β > cardiac > α). Fifth, the sites phosphorylated by the calcium/ calmodulin-dependent protein kinase in the chicken cardiac and skeletal receptor isoforms are not equivalent. A polyclonal serum, produced against a synthetic peptide containing the site phosphorylated by this kinase in the mammalian cardiac muscle receptor, by immunoprecipitation showed markedly different avidities for the receptor isoforms, and recognized only the cardiac receptor isoform on Western blots. Sixth, the chicken ryanodine receptor isoforms differ in the extent to which they bind azido[125I]calmodulin (α > β > cardiac). These results indicate that three distinct ryanodine receptor proteins are expressed in chicken striated muscles.

Original languageEnglish
Pages (from-to)5739-5745
Number of pages7
JournalBiochemistry
Volume32
Issue number22
StatePublished - 1993

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Ryanodine Receptor Calcium Release Channel
Striated Muscle
Muscle
Protein Isoforms
Chickens
Calcium-Calmodulin-Dependent Protein Kinase Type 2
Calcium-Calmodulin-Dependent Protein Kinases
Myocardium
Skeletal Muscle
Proteolysis
Peptides
Proteins
Sarcoplasmic Reticulum
Calmodulin
Immunoprecipitation
Trypsin
Epitopes
Digestion
Phosphotransferases
Western Blotting

ASJC Scopus subject areas

  • Biochemistry

Cite this

Airey, J. A., Grinsell, M. M., Jones, L., Sutko, J. L., & Witcher, D. (1993). Three ryanodine receptor isoforms exist in avian striated muscles. Biochemistry, 32(22), 5739-5745.

Three ryanodine receptor isoforms exist in avian striated muscles. / Airey, Judith A.; Grinsell, Matthew M.; Jones, Larry; Sutko, John L.; Witcher, Derrick.

In: Biochemistry, Vol. 32, No. 22, 1993, p. 5739-5745.

Research output: Contribution to journalArticle

Airey, JA, Grinsell, MM, Jones, L, Sutko, JL & Witcher, D 1993, 'Three ryanodine receptor isoforms exist in avian striated muscles', Biochemistry, vol. 32, no. 22, pp. 5739-5745.
Airey JA, Grinsell MM, Jones L, Sutko JL, Witcher D. Three ryanodine receptor isoforms exist in avian striated muscles. Biochemistry. 1993;32(22):5739-5745.
Airey, Judith A. ; Grinsell, Matthew M. ; Jones, Larry ; Sutko, John L. ; Witcher, Derrick. / Three ryanodine receptor isoforms exist in avian striated muscles. In: Biochemistry. 1993 ; Vol. 32, No. 22. pp. 5739-5745.
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