Reduced cardiac myofibrillar Mg-ATPase activity without changes in myosin isozymes in patients with end-stage heart failure

1990 ◽  
Vol 96 (1) ◽  
pp. 79-88 ◽  
Author(s):  
Adawia A. Alousi ◽  
Alison M. Grant ◽  
John R. Etzler ◽  
Barry R. Cofer ◽  
Joanna Van der Bel-Kahn ◽  
...  
Keyword(s):  
Heart Failure ◽  
Atpase Activity ◽  
Myosin Isozymes ◽  
End Stage Heart Failure ◽  
End Stage

Human heart failure: cAMP stimulation of SR Ca2+-ATPase activity and phosphorylation level of phospholamban

1999 ◽  
Vol 277 (2) ◽  
pp. H474-H480 ◽  
Author(s):  
Ulrich Schmidt ◽  
Roger J. Hajjar ◽  
Catherine S. Kim ◽  
Djamel Lebeche ◽  
Angelia A. Doye ◽  
...  
Keyword(s):  
Heart Failure ◽  
Atpase Activity ◽  
Human Heart ◽  
Human Myocardium ◽  
Human Heart Failure ◽  
Protein Levels ◽  
Phosphorylation Level ◽  
End Stage Heart Failure ◽  
End Stage ◽  
Camp Stimulation

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.

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

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).

562 The clinical improvement of end-stage heart failure is not accompanied by correction of anemia

2006 ◽  
Vol 5 (1) ◽  
pp. 126-126
Author(s):  
S DRAKOS ◽  
E KALDARA ◽  
M BONIOS ◽  
D KARAGEORGOPOULOS ◽  
C PIERRAKOS ◽  
...  
Keyword(s):  
Heart Failure ◽  
Clinical Improvement ◽  
End Stage Heart Failure ◽  
End Stage
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