Format

Send to

Choose Destination
Springerplus. 2016 Jun 21;5(1):808. doi: 10.1186/s40064-016-2469-x. eCollection 2016.

Global comparison of phosphoproteins in human and rodent hearts: implications for translational studies of myosin light chain and troponin phosphorylations.

Author information

1
Division of Cardiology, University of Illinois at Chicago, 840 S. Wood St, Chicago, IL 60612 USA.
2
The Cardiovascular Institute and the Department of Medicine, Loyola University Chicago Stritch School of Medicine, Building 110, Rm 5222, 2160 South First Avenue, Maywood, IL 60153 USA.
3
Division of Epidemiology and Biostatistics, University of Illinois at Chicago, Chicago, IL 60612 USA.
4
Department of Geography, University of Buffalo, 105 Wilkeson Quad, Buffalo, NY 14261 USA.
5
Division of Cardiology, University of Illinois at Chicago, 840 S. Wood St, Chicago, IL 60612 USA ; Jesse Brown Veterans Administration, 820 S. Damen, Chicago, IL 60612 USA.

Abstract

Cardiac remodeling and failure are regulated by a myriad of cardiac protein phosphorylations. In the present study, cardiac phosphoprotein patterns were examined in rodent and human hearts Left ventricular tissue samples were obtained from human systolic failing (n = 5) and control (n = 5) hearts and from two rat models of hypertensive heart failure, i.e., spontaneously hypertensive heart failure and Dahl salt-sensitive rats and corresponding controls. Phosphoproteins were separated by 2D-DIGE with Cydye staining, phosphoprotein patterns were analyzed using pixel intensity in rectified images. Specific phosphoproteins which were different in human versus rodent hearts were identified by MALDI-TOF/TOF Mass Spectrometry. Targeted pair-wise analyses showed differences (p < 0.05) in 26 % of the pixels, which included pixels containing phosphorylated troponin T, myosin light chain, peroxiredoxin, and haptoglobin. These results show differences in rodent versus human cardiac remodeling which will influence the translation rodent studies to humans in this area.

Supplemental Content

Full text links

Icon for Springer Icon for PubMed Central
Loading ...
Support Center