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Dysfunction of the β2-spectrin-based pathway in human heart failure. | LitMetric

Dysfunction of the β2-spectrin-based pathway in human heart failure.

Am J Physiol Heart Circ Physiol

Dorothy M. Davis Heart and Lung Research Institute, The Ohio State University, Columbus, Ohio; Division of Cardiovascular Medicine, Department of Internal Medicine, The Ohio State University, Columbus, Ohio; Department of Physiology and Cell Biology, Columbus, Ohio;

Published: June 2016

AI Article Synopsis

  • * Defects in β2-spectrin, particularly its association with ankyrin-B, are linked to congenital heart issues, but its impact on common heart diseases remains unclear.
  • * Research shows that β2-spectrin levels are significantly reduced in heart failure and arrhythmia cases, with regulation influenced by calcium and calpain proteases.

Article Abstract

β2-Spectrin is critical for integrating membrane and cytoskeletal domains in excitable and nonexcitable cells. The role of β2-spectrin for vertebrate function is illustrated by dysfunction of β2-spectrin-based pathways in disease. Recently, defects in β2-spectrin association with protein partner ankyrin-B were identified in congenital forms of human arrhythmia. However, the role of β2-spectrin in common forms of acquired heart failure and arrhythmia is unknown. We report that β2-spectrin protein levels are significantly altered in human cardiovascular disease as well as in large and small animal cardiovascular disease models. Specifically, β2-spectrin levels were decreased in atrial samples of patients with atrial fibrillation compared with tissue from patients in sinus rhythm. Furthermore, compared with left ventricular samples from nonfailing hearts, β2-spectrin levels were significantly decreased in left ventricle of ischemic- and nonischemic heart failure patients. Left ventricle samples of canine and murine heart failure models confirm reduced β2-spectrin protein levels. Mechanistically, we identify that β2-spectrin levels are tightly regulated by posttranslational mechanisms, namely Ca(2+)- and calpain-dependent proteases. Furthermore, consistent with this data, we observed Ca(2+)- and calpain-dependent loss of β2-spectrin downstream effector proteins, including ankyrin-B in heart. In summary, our findings illustrate that β2-spectrin and downstream molecules are regulated in multiple forms of cardiovascular disease via Ca(2+)- and calpain-dependent proteolysis.

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Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4935521PMC
http://dx.doi.org/10.1152/ajpheart.00875.2015DOI Listing

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