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- W1673752552 abstract "Impaired diastolic function is an early cardiac manifestation of type-2 diabetes, and increases the risk of developing heart failure [ [1] From A.M. Scott C.G. Chen H.H. The development of heart failure in patients with diabetes mellitus and pre-clinical diastolic dysfunction a population-based study. J. Am. Coll. Cardiol. 2010; 55: 300-305 Abstract Full Text Full Text PDF PubMed Scopus (340) Google Scholar ]. Recently, we showed that right atrial (RA) muscles from diabetic patients with preserved ejection fraction (EF) and coronary artery disease (CAD) had preserved contractile function with impaired relaxation [ [2] Lamberts R.R. Lingam S.J. Wang H.Y. Bollen I.A. Hughes G. Galvin I.F. et al. Impaired relaxation despite upregulated calcium-handling protein atrial myocardium from type 2 diabetic patients with preserved ejection fraction. Cardiovasc. Diabetol. 2014; 13: 72 Crossref PubMed Scopus (36) Google Scholar ]. This occurred despite an unexpectedly increased sarcoplasmic reticulum calcium ATPase (SERCA2a)/phospholamban (PLB) protein ratio [ [2] Lamberts R.R. Lingam S.J. Wang H.Y. Bollen I.A. Hughes G. Galvin I.F. et al. Impaired relaxation despite upregulated calcium-handling protein atrial myocardium from type 2 diabetic patients with preserved ejection fraction. Cardiovasc. Diabetol. 2014; 13: 72 Crossref PubMed Scopus (36) Google Scholar ], which would promote an increased cytosolic calcium removal and hence improved relaxation. The observed changes in calcium-handling proteins in the RA cannot simply be translated to the left ventricle (LV), as differences in ultrastructure and calcium dynamics exist [ [3] Bootman M.D. Higazi D.R. Coombes S. Roderick H.L. Calcium signalling during excitation–contraction coupling in mammalian atrial myocytes. J. Cell Sci. 2006; 119: 3915-3925 Crossref PubMed Scopus (117) Google Scholar ]. Therefore, we determined the SERCA2a/PLB ratio in tissue samples from the LV (and the RA) of non-diabetic and diabetic CAD patients with preserved EF. As PLB phosphorylation results in an increase in SERCA2a activity, we also determined phosphorylation of PLB by protein kinase A at serine-16 (PLB-S16) and by calcium/calmodulin dependent kinase II at threonine-17 (PLB-T17). Protein expression profiles were correlated with the patients' metabolic and functional parameters." @default.
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- W1673752552 date "2015-08-01" @default.
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- W1673752552 title "Chamber-specific changes in calcium-handling proteins in the type 2 diabetic human heart with preserved ejection fraction" @default.
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- W1673752552 doi "https://doi.org/10.1016/j.ijcard.2015.05.053" @default.
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