Identification of N-terminal protein acetylation and arginine methylation of the voltage-gated sodium channel in end-stage heart failure human heart

Failing human myocardium has been associated with decreased sarcoplasmic reticulum (SR) Ca2+-ATPase activity. There remains controversy as to whether the regulation of SR Ca2+-ATPase activity is altered in heart failure or whether decreased SR Ca2+-ATPase activity is due to changes in SR Ca2+-ATPase or phospholamban expression. We therefore investigated whether alterations in cAMP-dependent phosphorylation of phospholamban may be responsible for the reduced SR Ca2+-ATPase activity in human heart failure. Protein levels of phospholamban and SR Ca2+-ATPase, detected by Western blot, were unchanged in failing compared with nonfailing human myocardium. There was decreased responsiveness to the direct activation of the SR Ca2+-ATPase activity by either cAMP (0.01–100 μmol/l) or protein kinase A (1–30 μg) in failing myocardium. Using the backphosphorylation technique, we observed a decrease of the cAMP-dependent phosphorylation level of phospholamban by 20 ± 2%. It is concluded that the impaired SR function in human end-stage heart failure may be due, in part, to a reduced cAMP-dependent phosphorylation of phospholamban.

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Molecular cloning of an atypical voltage-gated sodium channel expressed in human heart and uterus: evidence for a distinct gene family.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.89.11.4893 ◽

1992 ◽

Vol 89 (11) ◽

pp. 4893-4897 ◽

Cited By ~ 94

Author(s):

A. L. George ◽

T. J. Knittle ◽

M. M. Tamkun

Keyword(s):

Sodium Channel ◽

Gene Family ◽

Molecular Cloning ◽

Human Heart ◽

Voltage Gated Sodium Channel ◽

Voltage Gated ◽

Distinct Gene

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INTERPLAY OF AUTOPHAGY WITH APOPTOSIS AND NECROSIS IN THE HUMAN HEART WITH END-STAGE HEART FAILURE

Journal of the American College of Cardiology ◽

10.1016/s0735-1097(11)60287-8 ◽

2011 ◽

Vol 57 (14) ◽

pp. E287

Author(s):

Carol Chen-Scarabelli ◽

Louis Saravolatz ◽

Diego Vasquez ◽

Kadija Abounit ◽

David Lanfear ◽

...

Keyword(s):

Heart Failure ◽

Human Heart ◽

End Stage Heart Failure ◽

End Stage ◽

Apoptosis And Necrosis

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Troponin phosphorylation and regulatory function in human heart muscle: Dephosphorylation of Ser23/24 on troponin I could account for the contractile defect in end-stage heart failure

Journal of Molecular and Cellular Cardiology ◽

10.1016/j.yjmcc.2006.08.017 ◽

2007 ◽

Vol 42 (1) ◽

pp. 247-259 ◽

Cited By ~ 134

Author(s):

Andrew E. Messer ◽

Adam M. Jacques ◽

Steven B. Marston

Keyword(s):

Heart Failure ◽

Heart Muscle ◽

Human Heart ◽

Troponin I ◽

Regulatory Function ◽

End Stage Heart Failure ◽

End Stage

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Localization of endothelial nitric oxide synthase in the normal and failing human atrial myocardium

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100166397 ◽

1996 ◽

Vol 54 ◽

pp. 786-787

Author(s):

Chi-Ming Wei ◽

Margarita Bracamonte ◽

Shi-Wen Jiang ◽

Richard C. Daly ◽

Christopher G.A. McGregor ◽

...

Keyword(s):

Nitric Oxide ◽

Heart Failure ◽

Nitric Oxide Synthase ◽

Endothelial Nitric Oxide Synthase ◽

Cardiac Tissues ◽

Mammalian Tissues ◽

End Stage Heart Failure ◽

End Stage ◽

Oxide Synthase ◽

Endothelial Nitric Oxide

Nitric oxide (NO) is a potent endothelium-derived relaxing factor which also may modulate cardiomyocyte inotropism and growth via increasing cGMP. While endothelial nitric oxide synthase (eNOS) isoforms have been detected in non-human mammalian tissues, expression and localization of eNOS in the normal and failing human myocardium are poorly defined. Therefore, the present study was designed to investigate eNOS in human cardiac tissues in the presence and absence of congestive heart failure (CHF).Normal and failing atrial tissue were obtained from six cardiac donors and six end-stage heart failure patients undergoing primary cardiac transplantation. ENOS protein expression and localization was investigated utilizing Western blot analysis and immunohistochemical staining with the polyclonal rabbit antibody to eNOS (Transduction Laboratories, Lexington, Kentucky).

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