Parallel comparative proteomics and phosphoproteomics reveal that cattle<i>myostatin</i>regulates phosphorylation of key enzymes in glycogen metabolism and glycolysis pathway

Yang, Shuping; Li, Xin; Liu, Xinfeng; Ding, Xiangbin; Xin, Xiangbo; Jin, Congfei; Zhang, Sheng; Li, Guangpeng; Guo, Hong

doi:10.18632/oncotarget.24250

Cited by 37 publications

(36 citation statements)

References 81 publications

(97 reference statements)

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In both of our study ( Fig. 5) and other reports, all results showed that the metabolic and oxidative phosphorylation pathways were significantly associated with the development of muscle [40][41][42] . In a word, the metabolism provided not only energy in whole embryonic skeletal muscle development but also fine modulation of embryonic muscle development styles [43][44][45] .…”

Section: Discussionsupporting

confidence: 83%

Proteomic analyses of sheep (ovis aries) embryonic skeletal muscle

Wang

Shi

Zhao

et al. 2020

Sci Rep

View full text Add to dashboard Cite

The growth and development of embryonic skeletal muscle plays a crucial role in sheep muscle mass. But proteomic analyses for embryonic skeletal development in sheep had been little involved in the past research. In this study, we explored differential abundance proteins during embryonic skeletal muscle development by the tandem mass tags (TMT) and performed a protein profile analyses in the longissimus dorsi of Chinese merino sheep at embryonic ages Day85 (D85N), Day105 (D105N) and Day135 (D135N). 5,520 proteins in sheep embryonic skeletal muscle were identified, and 1,316 of them were differential abundance (fold change ≥1.5 and p-value < 0.05). After the KEGG enrichment analyses, these differential abundance proteins were significant enriched in the protein binding, muscle contraction and energy metabolism pathways. After validation of the protein quantification with the parallel reaction monitoring (PRM), 41% (16/39) significant abundance proteins were validated, which was similar to the results of protein quantification with TMT. All results indicated that D85N to D105N was the stage of embryonic muscle fibers proliferation, while D105N to D135N was the stage of their hypertrophy. These findings provided a deeper understanding of the function and rules of proteins in different phases of sheep embryonic skeletal muscle growth and development.

show abstract

Section: Discussionsupporting

confidence: 83%

Proteomic analyses of sheep (ovis aries) embryonic skeletal muscle

Wang

Shi

Zhao

et al. 2020

Sci Rep

View full text Add to dashboard Cite

show abstract

“…Tandem Mass Tag (TMT) Labeling-TMT labeling of proteins was performed according to Thermo-Fisher Scientific's TMT Mass Tagging Kits and Reagents protocol (http://www.piercenet.com/ instructions/2162073.pdf) with a slight modification as described in previous publications (40,41) (see the supplementary Methods for additional details on the proteomics methods). Briefly, 110 g protein for each sample was alkylated in iodoacetamide in the dark for 1 h, then precipitated in ice-cold acetone overnight at Ϫ20°C.…”

Section: Methodsmentioning

confidence: 99%

Calcineurin-dependent Protein Phosphorylation Changes During Egg Activation in Drosophila melanogaster

Zhang¹,

Ahmed-Braimah²,

Goldberg³

et al. 2019

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Phosphoproteomic and global proteomic changes that occur during egg activation were quantified for the oocytes and eggs of Drosophila melanogaster with normal (control) or perturbed (CanB2 knockdown) calcineurin functions. We discovered broad influences of calcineurin on protein phosphorylation states in maturing oocytes and activating eggs. Our results illuminate the molecular mechanisms through which calcineurin regulates meiosis progression, protein translation, and signaling pathways during this critical developmental transition.

show abstract

“…The LC-MS/MS analysis was carried out using an Orbitrap Fusion (Thermo Fisher Scientific) mass spectrometer equipped with a nanospray Flex Ion Source similar to previous reports (51,52). The mass spectrometer was coupled to an Ulti-Mate3000 RSLCnano HPLC (Thermo Scientific).…”

Section: Proteomics Analysis Using Nano-scale Reverse Phase Lc and Tamentioning

confidence: 99%

Multi-omics analysis unravels a segregated metabolic flux network that tunes co-utilization of sugar and aromatic carbons in Pseudomonas putida

Kukurugya

Mendonca

Solhtalab

et al. 2019

Journal of Biological Chemistry

View full text Add to dashboard Cite

Pseudomonas species thrive in different nutritional environments and can catabolize divergent carbon substrates. These capabilities have important implications for the role of these species in natural and engineered carbon processing. However, the metabolic phenotypes enabling Pseudomonas to utilize mixed substrates remain poorly understood. Here, we employed a multi-omics approach involving stable isotope tracers, metabolomics, fluxomics, and proteomics in Pseudomonas putida KT2440 to investigate the constitutive metabolic network that achieves co-utilization of glucose and benzoate, respectively a monomer of carbohydrate polymers and a derivative of lignin monomers. Despite nearly equal consumption of both substrates, metabolite isotopologues revealed nonuniform assimilation throughout the metabolic network. Gluconeogenic flux of benzoate-derived carbons from the tricarboxylic acid cycle did not reach the upper Embden-Meyerhof-Parnas pathway nor the pentose-phosphate pathway. These latter two pathways were populated exclusively by glucose-derived carbons through a cyclic connection with the Entner-Doudoroff pathway. We integrated the 13 C-metabolomics data with physiological parameters for quantitative flux analysis, demonstrating that the metabolic segregation of the substrate carbons optimally sustained biosynthetic flux demands and redox balance. Changes in protein abundance partially predicted the metabolic flux changes in cells grown on the glucose:benzoate mixture versus on glucose alone. Notably, flux magnitude and directionality were also maintained by metabolite levels and regulation of phosphorylation of key metabolic enzymes. These findings provide new insights into the metabolic architecture that affords adaptability of P. putida to divergent carbon substrates and highlight regulatory points at different metabolic nodes that may underlie the high nutritional flexibility of Pseudomonas species. This work was supported by an Integrative Graduate Education and Research Traineeship Fellowship from the National Science Foundation (to M. A. K.), graduate fellowships from Cornell University (to M. S. and R. A. W.), and a start-up package from Cornell University. The authors declare that they have no conflicts of interest with the contents of this article. This article contains Tables S1-S4 and Figs. S1-S6.

show abstract

Parallel comparative proteomics and phosphoproteomics reveal that cattlemyostatinregulates phosphorylation of key enzymes in glycogen metabolism and glycolysis pathway

Cited by 37 publications

References 81 publications

Proteomic analyses of sheep (ovis aries) embryonic skeletal muscle

Proteomic analyses of sheep (ovis aries) embryonic skeletal muscle

Calcineurin-dependent Protein Phosphorylation Changes During Egg Activation in Drosophila melanogaster

Multi-omics analysis unravels a segregated metabolic flux network that tunes co-utilization of sugar and aromatic carbons in Pseudomonas putida

Contact Info

Product

Resources

About