Muscle-Type Specific Autophosphorylation of CaMKII Isoforms after Paced Contractions

W. Eilers, W. Gevers, D. van Overbeek, A. de Haan, R.T. Jaspers, P.A. Hilbers, A.C.R. van Riel, M. Flueck

    Research output: Contribution to JournalArticleAcademicpeer-review

    Abstract

    We explored to what extent isoforms of the regulator of excitation-contraction and excitation-transcription coupling, calcium/calmodulin protein kinase II (CaMKII) contribute to the specificity of myocellular calcium sensing between muscle types and whether concentration transients in its autophosphorylation can be simulated. CaMKII autophosphorylation at Thr287 was assessed in three muscle compartments of the rat after slow or fast motor unit-type stimulation and was compared against a computational model (CaMuZclE) coupling myocellular calcium dynamics with CaMKII Thr287 phosphorylation. Qualitative differences existed between fast- (gastrocnemius medialis) and slow-type muscle (soleus) for the expression pattern of CaMKII isoforms. Phospho-Thr287 content of δA CaMKII, associated with nuclear functions, demonstrated a transient and compartment-specific increase after excitation, which contrasted to the delayed autophosphorylation of the sarcoplasmic reticulum-associated βM CaMKII. In soleus muscle, excitation-induced δA CaMKII autophosphorylation demonstrated frequency dependence (P = 0.02). In the glycolytic compartment of gastrocnemius medialis, CaMKII autophosphorylation after excitation was blunted. In silico assessment emphasized the importance of mitochondrial calcium buffer capacity for excitation-induced CaMKII autophosphorylation but did not predict its isoform specificity. The findings expose that CaMKII autophosphorylation with paced contractions is regulated in an isoform and muscle type-specific fashion and highlight properties emerging for phenotype-specific regulation of CaMKII. © 2014 Wouter Eilers et al.
    Original languageEnglish
    Article number943806
    Number of pages20
    JournalBiomed research international
    Volume2014
    Issue number2014
    DOIs
    Publication statusPublished - 2014

    Fingerprint

    Calcium-Calmodulin-Dependent Protein Kinases
    Calmodulin
    Protein Kinases
    Muscle
    Protein Isoforms
    Muscles
    Calcium
    Skeletal Muscle
    Calcium-Calmodulin-Dependent Protein Kinase Type 2
    Excitation Contraction Coupling
    Phosphorylation
    Sarcoplasmic Reticulum
    Transcription
    Computer Simulation
    Rats
    Buffers
    Phenotype

    Cite this

    Eilers, W., Gevers, W., van Overbeek, D., de Haan, A., Jaspers, R. T., Hilbers, P. A., ... Flueck, M. (2014). Muscle-Type Specific Autophosphorylation of CaMKII Isoforms after Paced Contractions. Biomed research international, 2014(2014), [943806]. https://doi.org/10.1155/2014/943806
    Eilers, W. ; Gevers, W. ; van Overbeek, D. ; de Haan, A. ; Jaspers, R.T. ; Hilbers, P.A. ; van Riel, A.C.R. ; Flueck, M. / Muscle-Type Specific Autophosphorylation of CaMKII Isoforms after Paced Contractions. In: Biomed research international. 2014 ; Vol. 2014, No. 2014.
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    abstract = "We explored to what extent isoforms of the regulator of excitation-contraction and excitation-transcription coupling, calcium/calmodulin protein kinase II (CaMKII) contribute to the specificity of myocellular calcium sensing between muscle types and whether concentration transients in its autophosphorylation can be simulated. CaMKII autophosphorylation at Thr287 was assessed in three muscle compartments of the rat after slow or fast motor unit-type stimulation and was compared against a computational model (CaMuZclE) coupling myocellular calcium dynamics with CaMKII Thr287 phosphorylation. Qualitative differences existed between fast- (gastrocnemius medialis) and slow-type muscle (soleus) for the expression pattern of CaMKII isoforms. Phospho-Thr287 content of δA CaMKII, associated with nuclear functions, demonstrated a transient and compartment-specific increase after excitation, which contrasted to the delayed autophosphorylation of the sarcoplasmic reticulum-associated βM CaMKII. In soleus muscle, excitation-induced δA CaMKII autophosphorylation demonstrated frequency dependence (P = 0.02). In the glycolytic compartment of gastrocnemius medialis, CaMKII autophosphorylation after excitation was blunted. In silico assessment emphasized the importance of mitochondrial calcium buffer capacity for excitation-induced CaMKII autophosphorylation but did not predict its isoform specificity. The findings expose that CaMKII autophosphorylation with paced contractions is regulated in an isoform and muscle type-specific fashion and highlight properties emerging for phenotype-specific regulation of CaMKII. {\circledC} 2014 Wouter Eilers et al.",
    author = "W. Eilers and W. Gevers and {van Overbeek}, D. and {de Haan}, A. and R.T. Jaspers and P.A. Hilbers and {van Riel}, A.C.R. and M. Flueck",
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    Eilers, W, Gevers, W, van Overbeek, D, de Haan, A, Jaspers, RT, Hilbers, PA, van Riel, ACR & Flueck, M 2014, 'Muscle-Type Specific Autophosphorylation of CaMKII Isoforms after Paced Contractions' Biomed research international, vol. 2014, no. 2014, 943806. https://doi.org/10.1155/2014/943806

    Muscle-Type Specific Autophosphorylation of CaMKII Isoforms after Paced Contractions. / Eilers, W.; Gevers, W.; van Overbeek, D.; de Haan, A.; Jaspers, R.T.; Hilbers, P.A.; van Riel, A.C.R.; Flueck, M.

    In: Biomed research international, Vol. 2014, No. 2014, 943806, 2014.

    Research output: Contribution to JournalArticleAcademicpeer-review

    TY - JOUR

    T1 - Muscle-Type Specific Autophosphorylation of CaMKII Isoforms after Paced Contractions

    AU - Eilers, W.

    AU - Gevers, W.

    AU - van Overbeek, D.

    AU - de Haan, A.

    AU - Jaspers, R.T.

    AU - Hilbers, P.A.

    AU - van Riel, A.C.R.

    AU - Flueck, M.

    PY - 2014

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    N2 - We explored to what extent isoforms of the regulator of excitation-contraction and excitation-transcription coupling, calcium/calmodulin protein kinase II (CaMKII) contribute to the specificity of myocellular calcium sensing between muscle types and whether concentration transients in its autophosphorylation can be simulated. CaMKII autophosphorylation at Thr287 was assessed in three muscle compartments of the rat after slow or fast motor unit-type stimulation and was compared against a computational model (CaMuZclE) coupling myocellular calcium dynamics with CaMKII Thr287 phosphorylation. Qualitative differences existed between fast- (gastrocnemius medialis) and slow-type muscle (soleus) for the expression pattern of CaMKII isoforms. Phospho-Thr287 content of δA CaMKII, associated with nuclear functions, demonstrated a transient and compartment-specific increase after excitation, which contrasted to the delayed autophosphorylation of the sarcoplasmic reticulum-associated βM CaMKII. In soleus muscle, excitation-induced δA CaMKII autophosphorylation demonstrated frequency dependence (P = 0.02). In the glycolytic compartment of gastrocnemius medialis, CaMKII autophosphorylation after excitation was blunted. In silico assessment emphasized the importance of mitochondrial calcium buffer capacity for excitation-induced CaMKII autophosphorylation but did not predict its isoform specificity. The findings expose that CaMKII autophosphorylation with paced contractions is regulated in an isoform and muscle type-specific fashion and highlight properties emerging for phenotype-specific regulation of CaMKII. © 2014 Wouter Eilers et al.

    AB - We explored to what extent isoforms of the regulator of excitation-contraction and excitation-transcription coupling, calcium/calmodulin protein kinase II (CaMKII) contribute to the specificity of myocellular calcium sensing between muscle types and whether concentration transients in its autophosphorylation can be simulated. CaMKII autophosphorylation at Thr287 was assessed in three muscle compartments of the rat after slow or fast motor unit-type stimulation and was compared against a computational model (CaMuZclE) coupling myocellular calcium dynamics with CaMKII Thr287 phosphorylation. Qualitative differences existed between fast- (gastrocnemius medialis) and slow-type muscle (soleus) for the expression pattern of CaMKII isoforms. Phospho-Thr287 content of δA CaMKII, associated with nuclear functions, demonstrated a transient and compartment-specific increase after excitation, which contrasted to the delayed autophosphorylation of the sarcoplasmic reticulum-associated βM CaMKII. In soleus muscle, excitation-induced δA CaMKII autophosphorylation demonstrated frequency dependence (P = 0.02). In the glycolytic compartment of gastrocnemius medialis, CaMKII autophosphorylation after excitation was blunted. In silico assessment emphasized the importance of mitochondrial calcium buffer capacity for excitation-induced CaMKII autophosphorylation but did not predict its isoform specificity. The findings expose that CaMKII autophosphorylation with paced contractions is regulated in an isoform and muscle type-specific fashion and highlight properties emerging for phenotype-specific regulation of CaMKII. © 2014 Wouter Eilers et al.

    U2 - 10.1155/2014/943806

    DO - 10.1155/2014/943806

    M3 - Article

    VL - 2014

    JO - Biomed research international

    JF - Biomed research international

    SN - 2314-6133

    IS - 2014

    M1 - 943806

    ER -