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Literature DB >> 25651173

Altered myocardial calcium cycling and energetics in heart failure--a rational approach for disease treatment.

Przemek A Gorski¹, Delaine K Ceholski¹, Roger J Hajjar².

Abstract

Cardiomyocyte function depends on coordinated movements of calcium into and out of the cell and the proper delivery of ATP to energy-utilizing enzymes. Defects in calcium-handling proteins and abnormal energy metabolism are features of heart failure. Recent discoveries have led to gene-based therapies targeting calcium-transporting or -binding proteins, such as the cardiac sarco(endo)plasmic reticulum calcium ATPase (SERCA2a), leading to improvements in calcium homeostasis and excitation-contraction coupling. Here we review impaired calcium cycling and energetics in heart failure, assessing their roles from both a mutually exclusive and interdependent viewpoint, and discuss therapies that may improve the failing myocardium.

Entities: Chemical Disease Gene Mutation Species

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Year: 2015 PMID： 25651173 PMCID： PMC4338997 DOI： 10.1016/j.cmet.2015.01.005

Source DB: PubMed Journal: Cell Metab ISSN： 1550-4131 Impact factor: 27.287

128 in total

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8. Ryanodine receptor/calcium release channel PKA phosphorylation: a critical mediator of heart failure progression.

Authors: Xander H T Wehrens; Stephan E Lehnart; Steven Reiken; John A Vest; Anetta Wronska; Andrew R Marks
Journal: Proc Natl Acad Sci U S A Date: 2006-01-06 Impact factor: 11.205

Review 9. Redox regulation of cardiac calcium channels and transporters.

Authors: Aleksey V Zima; Lothar A Blatter
Journal: Cardiovasc Res Date: 2006-03-06 Impact factor: 10.787

10. Analysis of calstabin2 (FKBP12.6)-ryanodine receptor interactions: rescue of heart failure by calstabin2 in mice.

Authors: Fannie Huang; Jian Shan; Steven Reiken; Xander H T Wehrens; Andrew R Marks
Journal: Proc Natl Acad Sci U S A Date: 2006-02-15 Impact factor: 11.205

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Review 4. Hemodynamic assessment of diastolic function for experimental models.

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6. Protein docking and steered molecular dynamics suggest alternative phospholamban-binding sites on the SERCA calcium transporter.

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