蛋氨酸调控动物主要生理功能的机制
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摘要
蛋氨酸是动物机体的必需氨基酸,同时也是饲粮中的限制性氨基酸.蛋氨酸可作为底物参与蛋白质的合成,同时也可作为甲基供体参与DNA, RNA和蛋白质等的甲基化,或通过转巯基途径发挥抗氧化功能以及参与多胺的形成.这些代谢途径对动物的生产性能、抗氧化能力、免疫功能以及肠道健康等方面有着重要的调控作用.本文对近年来关于蛋氨酸调控生理功能的机制进行综述,以期为蛋氨酸代谢机制的研究及科学应用提供参考.
Methionine is an essential amino acid in animals and it is also a limited amino acid in the diet. Methionine can be used as a substrate to participate in protein synthesis. It can also be used as a methyl donor involved in the methylation of DNA, RNA and protein, or through the transfer of sulfhydryl pathways to play anti-oxidative roles and participate in the formation of polyamines. These metabolic pathways have important regulatory effects on animal performance, antioxidant capacity, immune function, and intestinal health. This article reviews the mechanism of methionine modulating physiological functions in recent years in order to provide reference for the study and scientific application of methionine metabolism mechanism.
Methionine is an essential amino acid in animals and it is also a limited amino acid in the diet. Methionine can be used as a substrate to participate in protein synthesis. It can also be used as a methyl donor involved in the methylation of DNA, RNA and protein, or through the transfer of sulfhydryl pathways to play anti-oxidative roles and participate in the formation of polyamines. These metabolic pathways have important regulatory effects on animal performance, antioxidant capacity, immune function, and intestinal health. This article reviews the mechanism of methionine modulating physiological functions in recent years in order to provide reference for the study and scientific application of methionine metabolism mechanism.
引文
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2 Lu S C. S-adenosylmethionine. Int J Biochem Cell Biol, 2000, 32:391–395
3 Lu S C, Mato J M. S-adenosylmethionine in liver health, injury, and cancer. Physiol Rev, 2012, 92:1515–1542
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5 Brosnan J T, Brosnan M E. The sulfur-containing amino acids:an overview. J Nutrition, 2006, 136:1636S–1640S
6 Miller D, Xu H, White R H. S-inosyl-L-homocysteine hydrolase, a novel enzyme involved in S-adenosyl-L-methionine recycling. J Bacteriol,2015, 197:2284–2291
7 Anderson O S, Sant K E, Dolinoy D C. Nutrition and epigenetics:an interplay of dietary methyl donors, one-carbon metabolism and DNA methylation. J Nutritional Biochem, 2012, 23:853–859
8 Waterland R A. Assessing the effects of high methionine intake on DNA methylation. J Nutrition, 2006, 136:1706S–1710S
9 Wen C, Chen X, Chen G Y, et al. Methionine improves breast muscle growth and alters myogenic gene expression in broilers. J Animal Sci,2014, 92:1068–1073
10 Liu G, Zong K, Zhang L, et al. Dietary methionine affect meat Qulity and Myostatin gene exon 1 region methylation in skeletal muscle tissues of broilers. Agric Sci China, 2010, 9:1338–1346
11 Wen C, Chen Y, Wu P, et al. MSTN, mTOR and FoxO4 are involved in the enhancement of breast muscle growth by methionine in broilers with lower hatching weight. PLoS ONE, 2014, 9:e114236
12 Liu H H. Effects of IGF-1 on duck embryonic muscle development and its molecular mechanism(in Chinese). Dissertation for Doctoral Degree.Chengdu:Sichuan Agricultural University, 2012[刘贺贺. IGF-1对鸭胚肌肉发育影响及其分子机理研究.博士学位论文.成都:四川农业大学, 2012]
13 Yang Z Q, Qing Y, Zhu Q, et al. Genetic effects of polymorphisms in myogenic regulatory factors on chicken muscle fiber traits. Asian Australas J Anim Sci, 2015, 28:782–787
14 Estrella N L, Desjardins C A, Nocco S E, et al. MEF2 transcription factors regulate distinct gene programs in mammalian skeletal muscle differentiation. J Biol Chem, 2015, 290:1256–1268
15 Wen C, Jiang X, Ding L, et al. Effects of dietary methionine on breast muscle growth, myogenic gene expression and IGF-I signaling in fast-and slow-growing broilers. Sci Rep, 2017, 7:1924
16 Jiang X Y. Effect of methionine on growth, pectoral muscle development and meat quality of Green-footed chicken(in Chinese). Dissertation for Master’s Degree. Nanjing:Nanjing Agricultural University, 2016[蒋雪樱.蛋氨酸对青脚麻鸡生长、胸肌发育及肉品质的影响.硕士学位论文.南京:南京农业大学, 2016]
17 Han B, Tong J, Zhu M J, et al. Insulin-like growth factor-1(IGF-1)and leucine activate pig myogenic satellite cells through mammalian target of rapamycin(mTOR)pathway. Mol Reprod Dev, 2008, 75:810–817
18 Stitt T N, Drujan D, Clarke B A, et al. The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell, 2004, 14:395–403
19 Amirouche A, Durieux A C, Banzet S, et al. Down-regulation of Akt/mammalian target of rapamycin signaling pathway in response to myostatin overexpression in skeletal muscle. Endocrinology, 2009, 150:286–294
20 Reed S A, Sandesara P B, Senf S M, et al. Inhibition of FoxO transcriptional activity prevents muscle fiber atrophy during cachexia and induces hypertrophy. FASEB J, 2012, 26:987–1000
21 Ge Y, Chen J. Mammalian target of rapamycin(mTOR)signaling network in skeletal myogenesis. J Biol Chem, 2012, 287:43928–43935
22 Cai S, Ye Q H, Zeng X F. Effects of methionine on reproductive performance of livestock and its mechanism(in Chinese). Chin J Anim Nutr,2018, 30:881–887[蔡爽,叶倩红,曾祥芳.蛋氨酸对畜禽繁殖性能的影响及机制.动物营养学报, 2018, 30:881–887]
23 Zeng X, Wang F, Fan X, et al. Dietary arginine supplementation during early pregnancy enhances embryonic survival in rats. J Nutrition, 2008,138 :1421–1425
24 Ramathal C Y, Bagchi I C, Taylor R N, et al. Endometrial decidualization:of mice and men. Semin Reprod Med, 2010, 28:17–26
25 Bazer F W, Song G, Kim J, et al. Mechanistic mammalian target of rapamycin(MTOR)cell signaling:effects of select nutrients and secreted phosphoprotein 1 on development of mammalian conceptuses. Mol Cellular Endocrinol, 2012, 354:22–33
26 Ikeda S, Sugimoto M, Kume S. Importance of methionine metabolism in morula-to-blastocyst transition in bovine preimplantation embryos. J Reprod Dev, 2012, 58:91–97
27 Toledo M Z, Baez G M, Garcia-Guerra A, et al. Effect of feeding rumen-protected methionine on productive and reproductive performance of dairy cows. PLoS ONE, 2017, 12:e0189117
28 Drazic A, Winter J. The physiological role of reversible methionine oxidation. Biochim Biophys Acta(BBA)-Proteins Proteom, 2014, 1844:1367–1382
29 Teng Z W. Effects of embryonic methionine on growth performance, antioxidant performance and chest muscle development of Landes goose(in Chinese). Dissertation for Master’s Degree. Changchun:Jilin Agricultural University, 2017[滕战伟.胚胎给养蛋氨酸对朗德鹅生长性能、抗氧化性能和胸肌发育的影响.硕士学位论文.长春:吉林农业大学, 2017]
30 Wang Q F, Zhao S F, Zhang X C. Effects of methionine on rat embryo development(in Chinese). Inner Mongolia Med J, 2000, 1:1–3[王秋枫,赵树芬,张秀池.蛋氨酸对大鼠胚胎发育影响的研究.内蒙古医学杂志, 2000, 1:1–3]
31 Leung K Y, Pai Y J, Chen Q, et al. Partitioning of One-Carbon units in folate and methionine metabolism is essential for neural tube closure. Cell Rep, 2017, 21:1795–1808
32 Han C X, Miao C. Function and metabolic absorption process of methionine(in Chinese). Mode J Anim Husbandr Vet Med, 2013, 9:75–80[韩春晓,苗翠.蛋氨酸的功能及代谢吸收过程.现代畜牧兽医, 2013, 9:75–80]
33 Komarnisky L A, Christopherson R J, Basu T K. Sulfur:its clinical and toxicologic aspects. Nutrition, 2003, 19:54–61
34 Stadtman E R, Moskovitz J, Berlett B S, et al. Cyclic oxidation and reduction of protein methionine residues is an important antioxidant mechanism. Mol Cellular Biochem, 2002, 234/235:3–9
35 Kim G, Weiss S J, Levine R L. Methionine oxidation and reduction in proteins. Biochim Biophys Acta(BBA)-General Subjects, 2014, 1840:901 –905
36 Pérez J A M, Fregosoaguilar T A. Chemistry of Natural Antioxidants and Studies Performed with Different Plants Collected in Mexico. In:Morales-Gonzalez J A. Oxidative Stress and Chronic Degenerative Diseases. London:InTech, 2013
37 Salmon A B, Kim G, Liu C, et al. Effects of transgenic methionine sulfoxide reductase A(MsrA)expression on lifespan and age-dependent changes in metabolic function in mice. Redox Biol, 2016, 10:251–256
38 Kim S K, Kim Y C. Effects of betaine supplementation on hepatic metabolism of sulfur-containing amino acids in mice. J Hepatol, 2005, 42:907 –913
39 Reeds P, Jahoor F. The amino acid requirements of disease. Clinical Nutrition, 2001, 20:15–22
40 Chen Y, Dong H, Thompson D C, et al. Glutathione defense mechanism in liver injury:insights from animal models. Food Chem Toxicol, 2013,60 :38–44
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