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Diabetic hyperglycaemia activates CaMKII and arrhythmias by O-linked glycosylation

Author

Listed:
  • Jeffrey R. Erickson

    (University of California, Davis, 451 Health Sciences Drive, Davis, California 95616, USA
    University of Otago, Dunedin 9054, New Zealand)

  • Laetitia Pereira

    (University of California, Davis, 451 Health Sciences Drive, Davis, California 95616, USA)

  • Lianguo Wang

    (University of California, Davis, 451 Health Sciences Drive, Davis, California 95616, USA)

  • Guanghui Han

    (Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, USA)

  • Amanda Ferguson

    (University of California, Davis, 451 Health Sciences Drive, Davis, California 95616, USA)

  • Khanha Dao

    (University of California, Davis, 451 Health Sciences Drive, Davis, California 95616, USA)

  • Ronald J. Copeland

    (Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, USA)

  • Florin Despa

    (University of California, Davis, 451 Health Sciences Drive, Davis, California 95616, USA
    University of Kentucky, 900 S. Limestone, Lexington, Kentucky 40536, USA)

  • Gerald W. Hart

    (Johns Hopkins University School of Medicine, 725 North Wolfe Street, Baltimore, Maryland 21205, USA)

  • Crystal M. Ripplinger

    (University of California, Davis, 451 Health Sciences Drive, Davis, California 95616, USA)

  • Donald M. Bers

    (University of California, Davis, 451 Health Sciences Drive, Davis, California 95616, USA)

Abstract

CaMKII is known to be pathologically activated in heart failure and arrhythmias; here it is shown that glucose-induced CaMKII activation via O-linked glycosylation might contribute to cardiac pathology in diabetes.

Suggested Citation

  • Jeffrey R. Erickson & Laetitia Pereira & Lianguo Wang & Guanghui Han & Amanda Ferguson & Khanha Dao & Ronald J. Copeland & Florin Despa & Gerald W. Hart & Crystal M. Ripplinger & Donald M. Bers, 2013. "Diabetic hyperglycaemia activates CaMKII and arrhythmias by O-linked glycosylation," Nature, Nature, vol. 502(7471), pages 372-376, October.
    • Handle: RePEc:nat:nature:v:502:y:2013:i:7471:d:10.1038_nature12537
    DOI: 10.1038/nature12537
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