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Modulation of cardiac contractility by serine/threonine protein phosphatase type 5.

Authors: Gergs, U  Boknik, P  Buchwalow, IB  Fabritz, L  Grundker, N  Kucerova, D  Matus, M  Werner, F  Schmitz, W  Neumann, J 
Citation: Gergs U, etal., Int J Cardiol. 2012 Jan 26;154(2):116-21. doi: 10.1016/j.ijcard.2010.09.009. Epub 2010 Sep 28.
Pubmed: (View Article at PubMed) PMID:20875921
DOI: Full-text: DOI:10.1016/j.ijcard.2010.09.009

BACKGROUND: Protein phosphatase 5 (PP5) a serine/threonine phosphatase is ubiquitously expressed in mammalian tissues including the heart, but its physiological role in the heart is still unknown. Therefore, we used a transgenic mouse model to get a first insight into the cardiac role of PP5. METHODS AND RESULTS: We generated transgenic mice with cardiac myocyte specific overexpression of PP5. Successful overexpression of PP5 was demonstrated by Western blotting, immunohistochemistry and enhanced arachidonic acid-stimulated protein phosphatase activity in transgenic hearts. Cardiac function was examined on the level of isolated cardiac myocytes, isolated organs and in intact animals. Whereas Ca(2+) transients and cell shortening remained unchanged, L-type Ca(2+) currents were decreased in isolated cardiac myocytes from transgenic mice. Ventricular contractility was reduced in isolated perfused hearts under basal conditions and after beta-adrenergic stimulation. In intact animals, echocardiography revealed increased left ventricular diameters and decreased contractility and invasively measured hemodynamic performance by left ventricular catheterization demonstrated a reduced response to beta-adrenergic stimulation in transgenic mice compared to wild type. CONCLUSIONS: Overexpression of PP5 affected contractility and beta-adrenergic signaling in the hearts of transgenic mice. Taken together, these findings are indicative of a regulatory role of PP5 in cardiac function.

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CRRD Object Information
CRRD ID: 8693745
Created: 2014-07-22
Species: All species
Last Modified: 2014-07-22
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.