Document Detail


Skeletal muscle protein metabolism in human heart failure.
MedLine Citation:
PMID:  23222707     Owner:  NLM     Status:  In-Data-Review    
Abstract/OtherAbstract:
PURPOSE OF REVIEW: This review considers evidence that the clinical condition of heart failure alters skeletal muscle protein synthesis and/or breakdown to promote skeletal muscle wasting and functional decrements that ultimately contribute to the symptomology of the disease.
RECENT FINDINGS: Advanced HF is frequently accompanied by muscle atrophy and a cachectic phenotype. Protein metabolic derangements that promote this phenotype are understudied and poorly understood. Instead, most investigations have evaluated regulatory hormones/signaling pathways thought to be reflective of protein synthesis and breakdown. Several of these recent studies have provided exciting data suggesting that the dysfunctional myocardium releases catabolic agents that could promote the skeletal muscle myopathic phenotype either directly or through modulation of other regulatory systems (e.g., energy balance).
SUMMARY: Although our understanding of skeletal muscle atrophy and dysfunction in heart failure is limited, recent studies have provided clues about the nature and timing of protein metabolic dysfunction. More specifically, skeletal muscle protein metabolic derangements likely evolve during periods of disease-related stress (i.e., acute disease exacerbation and hospitalization) and potentially derive in part, from signals promoted in the damaged/dysfunctional myocardium. Despite these compelling studies, there is a surprising lack of data regarding the nature or timing of specific protein metabolic defects in heart failure.
Authors:
Damien M Callahan; Michael J Toth
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Publication Detail:
Type:  Journal Article    
Journal Detail:
Title:  Current opinion in clinical nutrition and metabolic care     Volume:  16     ISSN:  1473-6519     ISO Abbreviation:  Curr Opin Clin Nutr Metab Care     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2012-12-10     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  9804399     Medline TA:  Curr Opin Clin Nutr Metab Care     Country:  England    
Other Details:
Languages:  eng     Pagination:  66-71     Citation Subset:  IM    
Affiliation:
Department of Medicine and Molecular Physiology and Biophysics, University of Vermont, College of Medicine, Burlington, Vermont, USA.
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