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Comparative analysis of mouse muscles types

ABSTRACT: The dataset presents FASP- and LC-MS/MS-based analysis of whole lysates of tree types of mouse muscle tissue: white and red muscle fibers and heart muscle. The measurements were performed using five biological replicates for each tissue type. The dataset cover 7200 proteins. The data were used for calculation of protein titers using the 'total protein method' (TPA) method.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (ncbitaxon:10090)

SUBMITTER: Jacek R Wisniewski

PROVIDER: MSV000084934 | MassIVE | Fri Feb 07 14:01:00 GMT 2020

SECONDARY ACCESSION(S): PXD002152

REPOSITORIES: MassIVE

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Proteomics Unveils Fibroblast-Cardiomyocyte Lactate Shuttle and Hexokinase Paradox in Mouse Muscles.

Rakus Dariusz D Rakus Dariusz D Gizak Agnieszka A Wiśniewski Jacek R JR

Journal of proteome research 20160624 8

Quantitative mapping, given in biochemically interpretable units such as mol per mg of total protein, of tissue-specific proteomes is prerequisite for the analysis of any process in cells. We applied label- and standard-free proteomics to characterize three types of striated muscles: white, red, and cardiac muscle. The analysis presented here uncovers several unexpected and novel features of striated muscles. In addition to differences in protein expression levels, the three muscle types substan ...[more]

PMID: 27302655

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Comparative analysis of mouse muscles types

Project description:The dataset presents FASP- and LC-MS/MS-based analysis of whole lysates of tree types of mouse muscle tissue: white and red muscle fibers and heart muscle. The measurements were performed using five biological replicates for each tissue type. The dataset cover 7200 proteins. The data were used for calculation of protein titers using the 'total protein method' (TPA) method.

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Expression data from mouse neonatal hindlimb muscles

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RNA-seq from tibialis muscles from rats aged 15 months (adult) and 27 months (old)

Project description:To gain new insights into molecular changes in skeletal muscle aging and disease with a special focus on differential alternative splicing and senescence, we performed RNA-seq on tibialis muscles from 15 months old (adult, a) and 27 months old (old, o) rats. Whole (w) muscle samples were prepared for both age groups (w/a and w/o). Additionally, for both age groups, muscle fibers were isolated. For adult rats, this resulted in one group (f/a). For old rats, fibers were subjected to Laser capture microdissection guided by expression of aging markers Tmem158 and Cdkn1a, giving rise to two groups, aging marker-positive fibers (f/o+) and aging marker-negative fibers (f/o-). The entire experiment comprises 5 groups (w/a, w/o, f/a, f/o+, f/o-), with 5 animals per group, ie. 25 samples total.

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Loss of lysosomal acid lipase results in mitochondrial dysfunction and fiber switch in skeletal muscles of mice

Project description:Objective: Lysosomal acid lipase (LAL) is the only enzyme known to hydrolyze cholesteryl esters (CE) and triacylglycerols in lysosomes at an acidic pH. Despite the importance of lysosomal hydrolysis in skeletal muscle (SM), research in this area is limited. We hypothesized that LAL may play an important role in SM development, function, and metabolism as a result of lipid and/or carbohydrate metabolism disruptions. Results: Mice with systemic LAL deficiency (Lal-/-) had markedly lower SM mass, cross-sectional area, and Feret diameter despite unchanged proteolysis or protein synthesis markers in all SM examined. In addition, Lal-/- SM showed increased total cholesterol and CE concentrations, especially during fasting and maturation. Regardless of increased glucose uptake, expression of the slow oxidative fiber marker MYH7 was markedly increased in Lal-/-SM, indicating a fiber switch from glycolytic, fast-twitch fibers to oxidative, slow-twitch fibers. Proteomic analysis of the oxidative and glycolytic parts of the SM confirmed the transition between fast- and slow-twitch fibers, consistent with the decreased Lal-/- muscle size due to the “fiber paradox”. Decreased oxidative capacity and ATP concentration were associated with reduced mitochondrial function of Lal-/- SM, particularly affecting oxidative phosphorylation, despite unchanged structure and number of mitochondria. Impairment in muscle function was reflected by increased exhaustion in the treadmill peak effort test in vivo. Conclusion: We conclude that whole-body loss of LAL is associated with a profound remodeling of the muscular phenotype, manifested by fiber type switch and a decline in muscle mass, most likely due to dysfunctional mitochondria and impaired energy metabolism, at least in mice.

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