Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
2934204 | International Journal of Cardiology | 2008 | 10 Pages |
Abnormalities of diastolic function are common to virtually all forms of cardiac failure. However, the molecular events leading to diastolic dysfunction have not been fully elucidated. We performed a differential proteomic profiling study on diastolic dysfunction hearts induced by renovascular hypertension. Left ventricular diastolic dysfunction induced by renovascular hypertension (2K1C, two-kidneys, one clip) was performed in twelve Sprague–Dawley rats. 2D echocardiographic and cardiac protein patterns (2D-electrophoresis and mass spectroscopy) were compared with the sham operated rats. We described sixteen altered protein spots in 2K1C rats with left ventricular diastolic dysfunction. Calsarcin-1 (CS-1) was significantly down-regulated in 2K1C rats and it showed a negative correlation with calcineurin enzymatic activity (r2 = 0.72 p = 0.03). We also showed changes in cellular energy metabolism in 2K1C rats, and these changes go in parallel with alterations of the thin filament proteome responsible for actin-myosin cross-bridge. In conclusion, this study provides a new insight into the left ventricular proteome profile associated with systemic hypertension induced diastolic dysfunction in a renovascular hypertension rat model. The decreased CS-1 protein with a concomitant increased enzymatic activity of calcineurin, suggests an important role of CS-1 in the calcineurin-mediated left ventricular hypertrophy.