Acetylation and phosphorylation changes to cardiac proteins in experimental HFpEF due to metabolic risk reveal targets for treatment
Key result
In a rat model of HFpEF, the cardiac acetylome was more severely altered (21% of proteins changed) than the phosphoproteome (9%) or proteome (3%) in obese versus lean hearts.
Why the study?
Pathomechanisms of HFpEF remain elusive and specific therapy is lacking, with proteomic changes poorly understood despite metabolic risk factors such as obesity.
Population
ZSF1 obese and lean rats
Comparison
ZSF1 obese vs lean heart tissues
Design
Preclinical animal model study
Follow-up
Up to the onset of HFpEF in the obese animals
Authors
Discussion
Loading...
Member takes
Implication
Protein acetylation may predominate in obese HFpEF; rat data leave open human translation and therapeutic targeting.
Structured PICO
P
Population
ZSF1 obese and lean rats evaluated for cardiac protein expression, phosphorylation, and acetylation changes up to the onset of HFpEF.
E
Exposure
Purina diet up to the onset of HFpEF (observational comparison of obese vs lean)
C
Comparator
ZSF1 lean rats
O
Outcome
Changes in cardiac protein expression, phosphorylation, and acetylation (proteome, phosphoproteome, and acetylome)surrogate
In a rat model of HFpEF, metabolic syndrome significantly alters the cardiac acetylome, highlighting titin stiffness and mitochondrial metabolism as potential therapeutic targets.
Cite This Study
Koser et al. (2022) studied Heart failure with preserved ejection fraction (HFpEF). Metabolic syndrome / obesity (ZSF1 obese rats) vs. ZSF1 lean rats was evaluated on Proteome, phosphoproteome, and acetylome changes in heart tissues. In a rat model of HFpEF, the cardiac acetylome was more severely altered (21% of proteins changed) than the phosphoproteome (9%) or proteome (3%) in obese versus lean hearts.