Abstract
Sarcopenia corresponds to the loss of muscle mass occurring during aging, and is associated with a loss of muscle functionality. Proteomic links the muscle functional changes with protein expression pattern. To better understand the mechanisms involved in muscle aging, we performed a proteomic analysis of Vastus lateralis muscle in mature and older women. For this, a shotgun proteomic method was applied to identify soluble proteins in muscle, using a combination of high performance liquid chromatography and mass spectrometry. A label-free protein profiling was then conducted to quantify proteins and compare profiles from mature and older women. This analysis showed that 35 of the 366 identified proteins were linked to aging in muscle. Most of the proteins were under-represented in older compared with mature women. We built a functional interaction network linking the proteins differentially expressed between mature and older women. The results revealed that the main differences between mature and older women were defined by proteins involved in energy metabolism and proteins from the myofilament and cytoskeleton. This is the first time that label-free quantitative proteomics has been applied to study of aging mechanisms in human skeletal muscle. This approach highlights new elements for elucidating the alterations observed during aging and may lead to novel sarcopenia biomarkers.
Highlights
From the ‡INRA, Plateforme d’Exploration du Metabolisme (PFEM), composante proteomique, F-63122 Saint Genes Champanelle, France; §INRA, UMR 1019, Unitede Nutrition Humaine, CRNH Auvergne, F-63122 Saint Genes Champanelle, France; ¶Department of Internal Medicine, Groene Hart Hospital, Gouda, The Netherlands; ʈTherapie des maladies du muscle strie, Institut de Myologie UM76, UPMC Universite Paris 6, U974-Inserm, UMR7215-CNRS/AIM, GH Pitie -Salpetriere, 47 bd de l’Hopital, F-75651 Paris cedex 13, France; **Department of Internal Medicine, Section of Gerontology and Geriatrics, VU University Medical Center, Amsterdam, The Netherlands; ‡‡Clermont Universite, Universited’Auvergne, F-63000 ClermontFerrand, France
We compared the protein profiling of muscle low ionic strength (LIS) extracts between two groups of mature and older women to determine the proteins differentially expressed during muscle aging
All the differentially expressed proteins that we identified as differentially expressed by shotgun proteomics can be classified according to their main biological function: energy metabolism, myofibrillar proteins, actin microfilament, detoxification and cytoprotection, protein turnover, signal transduction, and serum proteins
Summary
From the ‡INRA, Plateforme d’Exploration du Metabolisme (PFEM), composante proteomique, F-63122 Saint Genes Champanelle, France; §INRA, UMR 1019, Unitede Nutrition Humaine, CRNH Auvergne, F-63122 Saint Genes Champanelle, France; ¶Department of Internal Medicine, Groene Hart Hospital, Gouda, The Netherlands; ʈTherapie des maladies du muscle strie , Institut de Myologie UM76, UPMC Universite Paris 6, U974-Inserm, UMR7215-CNRS/AIM, GH Pitie -Salpetriere, 47 bd de l’Hopital, F-75651 Paris cedex 13, France; **Department of Internal Medicine, Section of Gerontology and Geriatrics, VU University Medical Center, Amsterdam, The Netherlands; ‡‡Clermont Universite , Universited’Auvergne, F-63000 ClermontFerrand, France. The few proteomic studies available on human skeletal muscle are mostly based on the 2DGE approach, which implies focusing on a specific pH range [7, 8]. Despite its power of high-resolution, 2DGE presents a limited dynamic range and scarcely resolves low abundance regulatory proteins, hydrophobic proteins, and proteins with extreme pI and/or Mr [14] To circumvent these limitations, we propose in the present study to apply a label-free protein profiling based on a shotgun proteomics approach. We propose in the present study to apply a label-free protein profiling based on a shotgun proteomics approach This technique permits to identify proteins in a complex mixture after trypsin hydrolysis, using a combination of high performance liquid chromatography and mass spectrometry. The functional interactions network linking these proteins showed that the two main biological processes were represented by proteins involved in energy metabolism and contractile proteins
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