Proteomic analysis of left ventricular diastolic dysfunction hearts in renovascular hypertensive rats.

Abstract:

: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 (r(2)=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.

journal_name

Int J Cardiol

authors

Junhong W,Jing Y,Jizheng M,Shushu Z,Xiangjian C,Hengfang W,Di Y,Jinan Z

doi

10.1016/j.ijcard.2007.07.003

subject

Has Abstract

pub_date

2008-07-04 00:00:00

pages

198-207

issue

2

eissn

0167-5273

issn

1874-1754

pii

S0167-5273(07)01039-X

journal_volume

127

pub_type

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