title: The Human Skeletal Muscle Proteome Project: a reappraisal of the current literature.
abstract: Skeletal muscle is a large organ that accounts for up to half the total mass of the human body. A progressive decline in muscle mass and strength occurs with ageing and in some individuals configures the syndrome of 'sarcopenia', a condition that impairs mobility, challenges autonomy, and is a risk factor for mortality. The mechanisms leading to sarcopenia as well as myopathies are still little understood. The Human Skeletal Muscle Proteome Project was initiated with the aim to characterize muscle proteins and how they change with ageing and disease. We conducted an extensive review of the literature and analysed publically available protein databases. A systematic search of peer-reviewed studies was performed using PubMed. Search terms included 'human', 'skeletal muscle', 'proteome', 'proteomic(s)', and 'mass spectrometry', 'liquid chromatography-mass spectrometry (LC-MS/MS)'. A catalogue of 5431 non-redundant muscle proteins identified by mass spectrometry-based proteomics from 38 peer-reviewed scientific publications from 2002 to November 2015 was created. We also developed a nosology system for the classification of muscle proteins based on localization and function. Such inventory of proteins should serve as a useful background reference for future research on changes in muscle proteome assessed by quantitative mass spectrometry-based proteomic approaches that occur with ageing and diseases. This classification and compilation of the human skeletal muscle proteome can be used for the identification and quantification of proteins in skeletal muscle to discover new mechanisms for sarcopenia and specific muscle diseases that can be targeted for the prevention and treatment.
authors.affiliation: National Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
authors.forename: Marta
authors.initials: M
authors.lastname: Gonzalez-Freire
authors.affiliation: Wilmer Eye Institute, Johns Hopkins University School of Medicine, Baltimore, MD, USA.
authors.forename: Richard D
authors.initials: RD
authors.lastname: Semba
authors.affiliation: National Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
authors.forename: Ceereena
authors.initials: C
authors.lastname: Ubaida-Mohien
authors.affiliation: National Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
authors.forename: Elisa
authors.initials: E
authors.lastname: Fabbri
authors.affiliation: National Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
authors.forename: Paul
authors.initials: P
authors.lastname: Scalzo
authors.affiliation: Department of Endocrinology, Odense University Hospital, Odense, Denmark.|Institute of Clinical Research and Institute of Molecular Medicine, University of Southern Denmark, Odense, Denmark.
authors.forename: Kurt
authors.initials: K
authors.lastname: Højlund
authors.affiliation: Thermo Fisher Scientific, West Palm Beach, FL, USA.
authors.forename: Craig
authors.initials: C
authors.lastname: Dufresne
authors.affiliation: National Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
authors.forename: Alexey
authors.initials: A
authors.lastname: Lyashkov
authors.affiliation: National Institute on Aging, National Institutes of Health, Baltimore, MD, USA.
authors.forename: Luigi
authors.initials: L
authors.lastname: Ferrucci
mesh_terms: D006801:Humans; D009124:Muscle Proteins / Q000378:metabolism*; D018482:Muscle, Skeletal / Q000378:metabolism*; D020543:Proteome
chemical_list: D009124:Muscle Proteins; D020543:Proteome
keywords: Ageing; Mass spectrometry; Post-translational modifications; Proteomics; Skeletal muscle