Proteomics and phosphoproteomics datasets of a muscle-specific STIM1 loss-of-function mouse model

Lyons, Scott P.; Wilson, Rebecca J.; Muoio, Deborah M.; Grimsrud, Paul A.

doi:10.1016/j.dib.2022.108051

Cited by 3 publications

(2 citation statements)

References 16 publications

(22 reference statements)

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“…Immobilized metal affinity chromatography (IMAC) has been routinely used for phospho-peptide enrichment prior to MS analysis [243], with the use of positively charged metal ions including titanium (Ti 4+ ), gallium (Ga 3+ ) and iron (Fe 3+ ) being central to this process [244]. Anti-phospho-tyrosine (pTyr) antibodies are frequently used to enrich tyrosine-phosphorylated peptides, as pTyr is significantly lower in abundance compared to phospho-serine (pSer) and phospho-threonine (pThr) [245].…”

Section: Proteomic Analysis Of Post-translational Modificationsmentioning

confidence: 99%

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Dowling,

Swandulla,

Ohlendieck

2023

Cells

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Voluntary striated muscles are characterized by a highly complex and dynamic proteome that efficiently adapts to changed physiological demands or alters considerably during pathophysiological dysfunction. The skeletal muscle proteome has been extensively studied in relation to myogenesis, fiber type specification, muscle transitions, the effects of physical exercise, disuse atrophy, neuromuscular disorders, muscle co-morbidities and sarcopenia of old age. Since muscle tissue accounts for approximately 40% of body mass in humans, alterations in the skeletal muscle proteome have considerable influence on whole-body physiology. This review outlines the main bioanalytical avenues taken in the proteomic characterization of skeletal muscle tissues, including top-down proteomics focusing on the characterization of intact proteoforms and their post-translational modifications, bottom-up proteomics, which is a peptide-centric method concerned with the large-scale detection of proteins in complex mixtures, and subproteomics that examines the protein composition of distinct subcellular fractions. Mass spectrometric studies over the last two decades have decisively improved our general cell biological understanding of protein diversity and the heterogeneous composition of individual myofibers in skeletal muscles. This detailed proteomic knowledge can now be integrated with findings from other omics-type methodologies to establish a systems biological view of skeletal muscle function.

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Section: Proteomic Analysis Of Post-translational Modificationsmentioning

confidence: 99%

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Dowling,

Swandulla,

Ohlendieck

2023

Cells

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“…Samples from mice treated with and without metformin (n=5) underwent largescale analysis of relative protein abundance changes as described previously [22]. hydroxylamine (shaking for 15 min at RT).…”

Section: Proteomics Sample Preparationmentioning

confidence: 99%

Metformin Impairs Intestinal Fructose Metabolism

Tong

Hannou

Sargsyan

et al. 2023

Preprint

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Objective: To investigate the effects of metformin on intestinal carbohydrate metabolism in vivo. Method: Male mice preconditioned with a high-fat, high-sucrose diet were treated orally with metformin or a control solution for two weeks. Fructose metabolism, glucose production from fructose, and production of other fructose-derived metabolites were assessed using stably labeled fructose as a tracer. Results: Metformin treatment decreased intestinal glucose levels and reduced incorporation of fructose-derived metabolites into glucose. This was associated with decreased intestinal fructose metabolism as indicated by decreased enterocyte F1P levels and diminished labeling of fructose-derived metabolites. Metformin also reduced fructose delivery to the liver. Proteomic analysis revealed that metformin coordinately down-regulated proteins involved carbohydrate metabolism including those involved in fructolysis and glucose production within intestinal tissue. Conclusion: Metformin reduces intestinal fructose metabolism, and this is associated with broad-based changes in intestinal enzyme and protein levels involved in sugar metabolism indicating that metformin's effects on sugar metabolism are pleiotropic.

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Ketone flux through BDH1 supports metabolic remodeling of skeletal and cardiac muscles in response to intermittent time-restricted feeding

Williams,

Crown,

Lyons

et al. 2024

Cell Metabolism

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Proteomics and phosphoproteomics datasets of a muscle-specific STIM1 loss-of-function mouse model

Cited by 3 publications

References 16 publications

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Mass Spectrometry-Based Proteomic Technology and Its Application to Study Skeletal Muscle Cell Biology

Metformin Impairs Intestinal Fructose Metabolism

Ketone flux through BDH1 supports metabolic remodeling of skeletal and cardiac muscles in response to intermittent time-restricted feeding

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