Amino acids regulate energy utilization through mammalian target of rapamycin complex 1 and adenosine monophosphate activated protein kinase pathway in porcine enterocytes
文献类型: 外文期刊
作者: Xiao, Hao 1 ; Zha, Cuifang 1 ; Shao, Fangyuan 3 ; Wang, Li 1 ; Tan, Bi'e 2 ;
作者机构: 1.Guangdong Acad Agr Sci, Key Lab Anim Nutr & Feed Sci South China,Minist A, Guangdong Publ Lab Anim Breeding & Nutr,State Key, Guangdong Key Lab Anim Breeding & Nutr,Inst Anim, Guangzhou 510640, Peoples R China
2.Chinese Acad Sci, Hunan Prov Key Lab Anim Nutr Physiol & Metab Proc, Natl Engn Lab Pollut Control & Waste Utilizat Liv, Key Lab Agroecol Proc Subtrop Reg,Inst Subtrop Ag, Changsha 410125, Peoples R China
3.Univ Macau, Fac Hlth Sci, Zhuhai, Macau, Peoples R China
4.Hunan Agr Univ, Coll Anim Sci & Technol, Changsha 410128, Peoples R China
关键词: Amino acids; Mammalian target of rapamycin; Adenosine monophosphate activated protein kinase; Mitochondrial respiration; Energy utilization
期刊名称:ANIMAL NUTRITION ( 影响因子:6.383; 五年影响因子:5.497 )
ISSN: 2405-6383
年卷期: 2020 年 6 卷 1 期
页码:
收录情况: SCI
摘要: As major fuels for the small intestinal mucosa, dietary amino acids (AA) are catabolized in the mitochondria and serve as sources of energy production. The present study was conducted to investigate AA metabolism that supply cell energy and the underlying signaling pathways in porcine enterocytes. Intestinal porcine epithelial cells (IPEC-J2) were treated with different concentrations of AA, inhibitor, or agonist of mammalian target of rapamycin complex 1 (mTORC1) and adenosine monophosphate activated protein kinase (AMPK), and mitochondrial respiration was monitored. The results showed that AA treatments resulted in enhanced mitochondrial respiration, increased intracellular content of pyruvic acid and lactic acid, and increased hormone-sensitive lipase mRNA expression. Meanwhile, decreased citrate synthase, isocitrate dehydrogenase alpha, and carnitine palmitoyltransferase 1 mRNA expression were also observed. We found that AA treatments increased the protein levels of phosphorylated mammalian target of rapamycin (p-mTOR), phosphorylated-p70 ribosomal protein S6 kinase, and phosphorylated-4E-binding protein 1. What is more, the protein levels of phosphorylated AMPK alpha (p-AMPK alpha) and nicotinamide adenine dinucleotide (NAD)-dependent protein deacetylase sirtuin-1 (SIRT1) were decreased by AA treatments in a time depending manner. Mitochondrial bioenergetics and the production of tricarboxylic acid cycle intermediates were decreased upon inhibition of mTORC1 or AMPK. Moreover, AMPK activation could up-regulate the mRNA expressions of inhibitor of nuclear factor kappa-B kinase subunit beta (Ikbk beta), integrin-linked protein kinase (ILK), unconventional myosin-Ic (Myo1c), ribosomal protein S6 kinase beta-2 (RPS6K beta 2), and vascular endothelial growth factor (VEGF)-beta, which are downstream effectors of mammalian target of rapamycin (mTOR). The mRNA expressions of phosphatidylinositol 4,5-bisphosphate 3-kinase catalytic subunit delta isoform (PIK3CD) and 50-AMP-activated protein kinase subunit gamma-1 (PRKAG1), which are upstream regulators of mTOR, were also up-regulated by AMPK activation. On the other hand, AMPK activation also down-regulated FK506-binding protein 1A (FKBP1A), serine/threonine-protein phosphatase 2A 55 kDa regulatory subunit B beta isoform, phosphatase and tensin homolog (PTEN), and unc-51 like autophagy activating kinase 1 (Ulk1), which are up-stream regulators of mTORC1. Taken together, these data indicated that AA regulated cellular energy metabolism through mTOR and AMPK pathway in porcine enterocytes. These results demonstrated interactions of AMPK and mTORC1 pathways in AA catabolism and energy metabolism in intestinal mucosa cells of piglets, and also provided reference for using AA to remedy human intestinal diseases. (c) 2020, Chinese Association of Animal Science and Veterinary Medicine. Production and hosting by Elsevier B.V. on behalf of KeAi Communications Co., Ltd.
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