Role of liver AMPK and GCN2 kinases in the control of postprandial protein metabolism in response to mid-term high or low protein intake in mice
Author:
Publisher
Springer Science and Business Media LLC
Subject
Nutrition and Dietetics,Medicine (miscellaneous)
Link
https://link.springer.com/content/pdf/10.1007/s00394-022-02983-z.pdf
Reference35 articles.
1. Morrison CD, Laeger T (2015) Protein-dependent regulation of feeding and metabolism. Trends Endocrinol Metab TEM 26:256–262. https://doi.org/10.1016/j.tem.2015.02.008
2. Hursel R, Martens EAP, Gonnissen HKJ et al (2015) Prolonged adaptation to a low or high protein diet does not modulate basal muscle protein synthesis rates—a substudy. PLoS ONE 10:e0137183. https://doi.org/10.1371/journal.pone.0137183
3. Batistela E, Pereira MP, Siqueira JT et al (2014) Decreased rate of protein synthesis, caspase-3 activity, and ubiquitin–proteasome proteolysis in soleus muscles from growing rats fed a low-protein, high-carbohydrate diet. Can J Physiol Pharmacol 92:445–454. https://doi.org/10.1139/cjpp-2013-0290
4. dos Santos MP, Batistela E, Pereira MP et al (2016) Higher insulin sensitivity in EDL muscle of rats fed a low-protein, high-carbohydrate diet inhibits the caspase-3 and ubiquitin-proteasome proteolytic systems but does not increase protein synthesis. J Nutr Biochem 34:89–98. https://doi.org/10.1016/j.jnutbio.2016.04.008
5. Wykes LJ, Fiorotto M, Burrin DG et al (1996) Chronic low protein intake reduces tissue protein synthesis in a pig model of protein malnutrition. J Nutr 126:1481
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