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Amino acid transportation, sensing and signal transduction in the mammary gland: key molecular signalling pathways in the regulation of milk synthesis

Published online by Cambridge University Press:  10 March 2020

Zhihui Wu
Affiliation:
Guangdong Province Key Laboratory of Animal Nutrition Control, College of Animal Science, South China Agricultural University, Guangzhou, 510642, China
Jinghui Heng
Affiliation:
Guangdong Province Key Laboratory of Animal Nutrition Control, College of Animal Science, South China Agricultural University, Guangzhou, 510642, China
Min Tian
Affiliation:
Guangdong Province Key Laboratory of Animal Nutrition Control, College of Animal Science, South China Agricultural University, Guangzhou, 510642, China
Hanqing Song
Affiliation:
Guangdong Province Key Laboratory of Animal Nutrition Control, College of Animal Science, South China Agricultural University, Guangzhou, 510642, China
Fang Chen
Affiliation:
Guangdong Province Key Laboratory of Animal Nutrition Control, College of Animal Science, South China Agricultural University, Guangzhou, 510642, China College of Animal Science and National Engineering Research Center for Breeding Swine Industry, South China Agricultural University, Guangzhou510642, China
Wutai Guan*
Affiliation:
Guangdong Province Key Laboratory of Animal Nutrition Control, College of Animal Science, South China Agricultural University, Guangzhou, 510642, China College of Animal Science and National Engineering Research Center for Breeding Swine Industry, South China Agricultural University, Guangzhou510642, China
Shihai Zhang*
Affiliation:
Guangdong Province Key Laboratory of Animal Nutrition Control, College of Animal Science, South China Agricultural University, Guangzhou, 510642, China College of Animal Science and National Engineering Research Center for Breeding Swine Industry, South China Agricultural University, Guangzhou510642, China Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX, USA
*
*Corresponding authors: Wutai Guan, email wutaiguan1963@163.com; Shihai Zhang, email zhangshihai@scau.edu.cn
*Corresponding authors: Wutai Guan, email wutaiguan1963@163.com; Shihai Zhang, email zhangshihai@scau.edu.cn

Abstract

The mammary gland, a unique exocrine organ, is responsible for milk synthesis in mammals. Neonatal growth and health are predominantly determined by quality and quantity of milk production. Amino acids are crucial maternal nutrients that are the building blocks for milk protein and are potential energy sources for neonates. Recent advances made regarding the mammary gland further demonstrate that some functional amino acids also regulate milk protein and fat synthesis through distinct intracellular and extracellular pathways. In the present study, we discuss recent advances in the role of amino acids (especially branched-chain amino acids, methionine, arginine and lysine) in the regulation of milk synthesis. The present review also addresses the crucial questions of how amino acids are transported, sensed and transduced in the mammary gland.

Type
Review Article
Copyright
© The Author(s) 2020

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References

Pattison, KL, Kraschnewski, JL, Lehman, E, et al. (2019) Breastfeeding initiation and duration and child health outcomes in the first baby study. Prev Med 118, 16.CrossRefGoogle ScholarPubMed
Theil, PK, Lauridsen, C & Quesnel, H (2014) Neonatal piglet survival: impact of sow nutrition around parturition on fetal glycogen deposition and production and composition of colostrum and transient milk. Animal 8, 10211030.CrossRefGoogle ScholarPubMed
Rauprich, A, Hammon, H & Blum, J (2000) Influence of feeding different amounts of first colostrum on metabolic, endocrine, and health status and on growth performance in neonatal calves. J Anim Sci 78, 896908.CrossRefGoogle ScholarPubMed
Wu, G (2009) Amino acids: metabolism, functions, and nutrition. Amino Acids 37, 117.CrossRefGoogle ScholarPubMed
Zhang, S, Zeng, X, Ren, M, et al. (2017) Novel metabolic and physiological functions of branched chain amino acids: a review. J Anim Sci Biotechnol 8, 10.CrossRefGoogle ScholarPubMed
Omphalius, C, Lapierre, H, Guinard-Flament, J, et al. (2019) Amino acid efficiencies of utilization vary by different mechanisms in response to energy and protein supplies in dairy cows: study at mammary-gland and whole-body levels. J Dairy Sci 102, 98839901.CrossRefGoogle ScholarPubMed
Raggio, G, Lemosquet, S, Lobley, G, et al. (2006) Effect of casein and propionate supply on mammary protein metabolism in lactating dairy cows. J Dairy Sci 89, 43404351.CrossRefGoogle ScholarPubMed
Haque, M, Guinard-Flament, J, Lamberton, P, et al. (2015) Changes in mammary metabolism in response to the provision of an ideal amino acid profile at 2 levels of metabolizable protein supply in dairy cows: consequences on efficiency. J Dairy Sci 98, 39513968.CrossRefGoogle ScholarPubMed
Safayi, S & Nielsen, MO (2013) Intravenous supplementation of acetate, glucose or essential amino acids to an energy and protein deficient diet in lactating dairy goats: effects on milk production and mammary nutrient extraction. Small Ruminant Res 112, 162173.CrossRefGoogle Scholar
Trottier, N, Shipley, C & Easter, R (1997) Plasma amino acid uptake by the mammary gland of the lactating sow. J Anim Sci 75, 12661278.CrossRefGoogle ScholarPubMed
Davis, S, Bickerstaffe, R & Hart, D (1978) Amino acid uptake by the mammary gland of the lactating ewe. Aust J Biol Sci 31, 123132.CrossRefGoogle ScholarPubMed
Mepham, T & Linzell, J (1966) A quantitative assessment of the contribution of individual plasma amino acids to the synthesis of milk proteins by the goat mammary gland. Biochem J 101, 7683.CrossRefGoogle ScholarPubMed
Mepham, T (1982) Amino acid utilization by lactating mammary gland. J Dairy Sci 65, 287298.CrossRefGoogle ScholarPubMed
Hennighausen, L & Robinson, GW (2001) Signaling pathways in mammary gland development. Dev Cell 1, 467475.CrossRefGoogle ScholarPubMed
Jackson, S, Bryson, J, Wang, H, et al. (2000) Cellular uptake of valine by lactating porcine mammary tissue. J Anim Sci 78, 29272932.CrossRefGoogle ScholarPubMed
Luo, X, Coon, JS, Su, E, et al. (2010) LAT1 regulates growth of uterine leiomyoma smooth muscle cells. Reprod Sci 17, 791797.Google Scholar
Fan, X, Ross, DD, Arakawa, H, et al. (2010) Impact of system l amino acid transporter 1 (LAT1) on proliferation of human ovarian cancer cells: a possible target for combination therapy with anti-proliferative aminopeptidase inhibitors. Biochem Pharmacol 80, 811818.CrossRefGoogle ScholarPubMed
Kurayama, R, Ito, N, Nishibori, Y, et al. (2011) Role of amino acid transporter LAT2 in the activation of mTORC1 pathway and the pathogenesis of crescentic glomerulonephritis. Lab Invest 91, 9921006.CrossRefGoogle ScholarPubMed
Matsumoto, T, Nakamura, E, Nakamura, H, et al. (2013) The production of free glutamate in milk requires the leucine transporter LAT1. Am J Physiol Cell Physiol 305, C623C631.CrossRefGoogle ScholarPubMed
Lin, Y, Duan, X, Lv, H, et al. (2018) The effects of l-type amino acid transporter 1 on milk protein synthesis in mammary glands of dairy cows. J Dairy Sci 101, 16871696.CrossRefGoogle ScholarPubMed
Chen, F, Zhang, S, Deng, Z, et al. (2018) Regulation of amino acid transporters in the mammary gland from late pregnancy to peak lactation in the sow. J Anim Sci Biotechnol 9, 35.CrossRefGoogle ScholarPubMed
Duan, X, Lin, Y, Lv, H, et al. (2017) Methionine induces LAT1 expression in dairy cow mammary gland by activating the mTORC1 signaling pathway. DNA Cell Biol 36, 11261133.CrossRefGoogle ScholarPubMed
Li, P, Knabe, DA, Kim, SW, et al. (2006) Lactating porcine mammary tissue catabolizes branched-chain amino acids for glutamine and aspartate synthesis. J Nutr 139, 15021509.CrossRefGoogle Scholar
Wohlt, J, Clark, J, Derrig, R, et al. (1977) Valine, leucine, and isoleucine metabolism by lactating bovine mammary tissue. J Dairy Sci 60, 18751882.CrossRefGoogle ScholarPubMed
Saxton, RA, Knockenhauer, KE, Wolfson, RL, et al. (2016) Structural basis for leucine sensing by the Sestrin2–mTORC1 pathway. Science 351, 5358.CrossRefGoogle ScholarPubMed
Kimball, SR, Gordon, BS, Moyer, JE, et al. (2016) Leucine induced dephosphorylation of Sestrin2 promotes mTORC1 activation. Cell Signal 28, 896906.CrossRefGoogle ScholarPubMed
Wolfson, RL, Chantranupong, L, Saxton, RA, et al. (2016) Sestrin2 is a leucine sensor for the mTORC1 pathway. Science 351, 4348.CrossRefGoogle ScholarPubMed
Luo, C, Zheng, N, Zhao, S, et al. (2019) Sestrin2 negatively regulates casein synthesis through the SH3BP4–mTORC1 pathway in response to AA depletion or supplementation in cow mammary epithelial cells. J Agric Food Chem 67, 48494859.CrossRefGoogle ScholarPubMed
Kim, Y-M, Stone, M, Hwang, TH, et al. (2012) SH3BP4 is a negative regulator of amino acid–Rag GTPase–mTORC1 signaling. Mol Cell 46, 833846.CrossRefGoogle ScholarPubMed
Luo, C, Zhao, S, Zhang, M, et al. (2018) SESN2 negatively regulates cell proliferation and casein synthesis by inhibition the amino acid-mediated mTORC1 pathway in cow mammary epithelial cells. Sci Rep 8, 3912.CrossRefGoogle ScholarPubMed
Luo, C, Zhao, S, Dai, W, et al. (2018) Proteomic analyses reveal GNG12 regulates cell growth and casein synthesis by activating the Leu-mediated mTORC1 signaling pathway. Biochim Biophys Acta Proteins Proteom 1866, 10921101.CrossRefGoogle ScholarPubMed
Sancak, Y, Bar-Peled, L, Zoncu, R, et al. (2010) Ragulator–Rag complex targets mTORC1 to the lysosomal surface and is necessary for its activation by amino acids. Cell 141, 290303.CrossRefGoogle ScholarPubMed
Han, JM, Jeong, SJ, Park, MC, et al. (2012) Leucyl-tRNA synthetase is an intracellular leucine sensor for the mTORC1-signaling pathway. Cell 149, 410424.CrossRefGoogle ScholarPubMed
McGuckin, M, Manjarin, R, Peterson, D (2016) Leucine supplementation increases mouse mammary cell proliferation in vitro. J Anim Sci 94, 9898.CrossRefGoogle Scholar
Richert, B, Goodband, R, Tokach, M, et al. (1997) Increasing valine, isoleucine, and total branched-chain amino acids for lactating sows. J Anim Sci 75, 21172128.CrossRefGoogle ScholarPubMed
Richert, B, Tokach, M, Goodband, R, et al. (1996) Valine requirement of the high-producing lactating sow. J Anim Sci 74, 13071313.CrossRefGoogle ScholarPubMed
Haque, M, Rulquin, H & Lemosquet, S (2013) Milk protein responses in dairy cows to changes in postruminal supplies of arginine, isoleucine, and valine. J Dairy Sci 96, 420430.CrossRefGoogle ScholarPubMed
Appuhamy, JRN, Knoebel, NA, Nayananjalie, WD, et al. (2012) Isoleucine and leucine independently regulate mTOR signaling and protein synthesis in MAC-T cells and bovine mammary tissue slices. J Nutr 142, 484491.CrossRefGoogle ScholarPubMed
Liu, G, Hanigan, M, Lin, X, et al. (2017) Methionine, leucine, isoleucine, or threonine effects on mammary cell signaling and pup growth in lactating mice. J Dairy Sci 100, 40384050.CrossRefGoogle ScholarPubMed
Che, L, Xu, M, Gao, K, et al. (2019) Valine increases milk fat synthesis in mammary gland of gilts through stimulating AKT/MTOR/SREBP1 pathway. Biol Reprod 101, 126137.CrossRefGoogle Scholar
Carcangiu, V, Mura, MC, Daga, C, et al. (2013) Association between SREBP-1 gene expression in mammary gland and milk fat yield in Sarda breed sheep. Meta Gene 1, 4349.CrossRefGoogle ScholarPubMed
Ma, L & Corl, B (2012) Transcriptional regulation of lipid synthesis in bovine mammary epithelial cells by sterol regulatory element binding protein-1. J Dairy Sci 95, 37433755.CrossRefGoogle ScholarPubMed
Rudolph, MC, McManaman, JL, Phang, T, et al. (2007) Metabolic regulation in the lactating mammary gland: a lipid synthesizing machine. Physiol Genomics 28, 323336.CrossRefGoogle ScholarPubMed
Peterson, TR, Sengupta, SS, Harris, TE, et al. (2011) mTOR complex 1 regulates lipin 1 localization to control the SREBP pathway. Cell 146, 408420.CrossRefGoogle ScholarPubMed
Roets, E, Massart-Leën, A-M, Peeters, G, et al. (1983) Metabolism of leucine by the isolated perfused goat udder. J Dairy Res 50, 413424.CrossRefGoogle ScholarPubMed
Nelson, G, Chandrashekar, J, Hoon, MA, et al. (2002) An amino-acid taste receptor. Nature 416, 199202.CrossRefGoogle Scholar
Wang, Y, Liu, J, Wu, H, et al. (2017) Amino acids regulate mTOR pathway and milk protein synthesis in a mouse mammary epithelial cell line is partly mediated by T1R1/T1R3. Eur J Nutr 56, 24672474.CrossRefGoogle Scholar
Liu, J, Wang, Y, Li, D, et al. (2017) Milk protein synthesis is regulated by T1R1/T1R3, a G protein-coupled taste receptor, through the mTOR pathway in the mouse mammary gland. Mol Nutr Food Res 61, 1601017.CrossRefGoogle Scholar
Wauson, EM, Zaganjor, E, Lee, A-Y, et al. (2012) The G protein-coupled taste receptor T1R1/T1R3 regulates mTORC1 and autophagy. Mol Cell 47, 851862.CrossRefGoogle Scholar
Wauson, EM, Zaganjor, E & Cobb, MH (2013) Amino acid regulation of autophagy through the GPCR TAS1R1-TAS1R3. Autophagy 9, 418419.CrossRefGoogle ScholarPubMed
Carriere, A, Romeo, Y, Acosta-Jaquez, HA, et al. (2011) ERK1/2 phosphorylate Raptor to promote Ras-dependent activation of mTOR complex 1 (mTORC1). J Biol Chem 286, 567577.CrossRefGoogle Scholar
Rolfe, M, McLeod, LE, Pratt, PF, et al. (2005) Activation of protein synthesis in cardiomyocytes by the hypertrophic agent phenylephrine requires the activation of ERK and involves phosphorylation of tuberous sclerosis complex 2 (TSC2). Biochem J 388, 973984.CrossRefGoogle Scholar
Zhou, Y, Zhou, Z, Peng, J, et al. (2018) Methionine and valine activate the mammalian target of rapamycin complex 1 pathway through heterodimeric amino acid taste receptor (TAS1R1/TAS1R3) and intracellular Ca2+ in bovine mammary epithelial cells. J Dairy Sci 101, 1135411363.CrossRefGoogle ScholarPubMed
Verma, N & Kansal, VK (1993) Characterisation of the routes of methionine transport in mouse mammary glands. Indian J Med Res 98, 297304.Google ScholarPubMed
Shennan, D & Boyd, C (2014) The functional and molecular entities underlying amino acid and peptide transport by the mammary gland under different physiological and pathological conditions. J Mammary Gland Biol Neoplasia 19, 1933.CrossRefGoogle ScholarPubMed
Chillaron, J, Roca, R, Valencia, A, et al. (2001) Heteromeric amino acid transporters: biochemistry, genetics, and physiology. Am J Physiol Renal Physiol 281, F995F1018.CrossRefGoogle Scholar
Qi, H, Meng, C, Jin, X, et al. (2018) Methionine promotes milk protein and fat synthesis and cell proliferation via the SNAT2–PI3K signaling pathway in bovine mammary epithelial cells. J Agric Food Chem 66, 1102711033.CrossRefGoogle ScholarPubMed
Schwab, CG, Satter, L & Clay, A (1976) Response of lactating dairy cows to abomasal infusion of amino acids. J Dairy Sci 59, 12541270.CrossRefGoogle ScholarPubMed
Rulquin, H, Pisulewski, P, Vérité, R, et al. (1993) Milk production and composition as a function of postruminal lysine and methionine supply: a nutrient-response approach. Livest Prod Sci 37, 6990.CrossRefGoogle Scholar
Dourmad, J-Y, Etienne, M, Valancogne, A, et al. (2008) InraPorc: a model and decision support tool for the nutrition of sows. Anim Feed Sci Technol 143, 372386.CrossRefGoogle Scholar
National Research Council (1998) Nutrient Requirements of Swine, 10th ed. Washington, DC: National Academies Press.Google Scholar
Lapierre, H, Lobley, GE, Doepel, L, et al. (2012) Triennial Lactation Symposium: Mammary metabolism of amino acids in dairy cows. J Anim Sci 90, 17081721.CrossRefGoogle ScholarPubMed
Gu, X, Orozco, JM, Saxton, RA, et al. (2017) SAMTOR is an S-adenosylmethionine sensor for the mTORC1 pathway. Science 358, 813818.CrossRefGoogle ScholarPubMed
Ma, Y, Batistel, F, Xu, T, et al. (2019) Phosphorylation of AKT serine/threonine kinase and abundance of milk protein synthesis gene networks in mammary tissue in response to supply of methionine in periparturient Holstein cows. J Dairy Sci 102, 42644274.CrossRefGoogle ScholarPubMed
Li, P, Yu, M, Zhou, C, et al. (2019) FABP5 is a critical regulator of methionine- and estrogen-induced SREBP-1c gene expression in bovine mammary epithelial cells. J Cell Physiol 234, 537549.CrossRefGoogle Scholar
Lv, Q, Wang, G, Zhang, Y, et al. (2019) FABP5 regulates the proliferation of clear cell renal cell carcinoma cells via the PI3K/AKT signaling pathway. Int J Oncol 54, 12211232.Google ScholarPubMed
Li, X, Li, P, Wang, L, et al. (2019) Lysine enhances the stimulation of fatty acids on milk fat synthesis via the GPRC6A–PI3K–FABP5 signaling in bovine mammary epithelial cells. J Agric Food Chem 67, 70057015.CrossRefGoogle ScholarPubMed
Latres, E, Amini, AR, Amini, AA, et al. (2005) Insulin-like growth factor-1 (IGF-1) inversely regulates atrophy-induced genes via the phosphatidylinositol 3-kinase/Akt/mammalian target of rapamycin (PI3K/Akt/mTOR) pathway. J Biol Chem 280, 27372744.CrossRefGoogle ScholarPubMed
Stitt, TN, Drujan, D, Clarke, BA, et al. (2004) The IGF-1/PI3K/Akt pathway prevents expression of muscle atrophy-induced ubiquitin ligases by inhibiting FOXO transcription factors. Mol Cell 14, 395403.CrossRefGoogle ScholarPubMed
Miller, RA, Buehner, G, Chang, Y, et al. (2005) Methionine-deficient diet extends mouse lifespan, slows immune and lens aging, alters glucose, T4, IGF-I and insulin levels, and increases hepatocyte MIF levels and stress resistance. Aging Cell 4, 119125.CrossRefGoogle ScholarPubMed
Carew, L, McMurtry, J & Alster, F (2003) Effects of methionine deficiencies on plasma levels of thyroid hormones, insulin-like growth factors-I and-II, liver and body weights, and feed intake in growing chickens. Poult Sci 82, 19321938.CrossRefGoogle ScholarPubMed
Stubbs, A, Wheelhouse, N, Lomax, M, et al. (2002) Nutrient–hormone interaction in the ovine liver: methionine supply selectively modulates growth hormone-induced IGF-I gene expression. J Endocrinol 174, 335341.CrossRefGoogle ScholarPubMed
Broer, S (2008) Amino acid transport across mammalian intestinal and renal epithelia. Physiol Rev 88, 249286.CrossRefGoogle ScholarPubMed
Laspiur, JP, Burton, J, Weber, P, et al. (2004) Amino acid transporters in porcine mammary gland during lactation. J Dairy Sci 87, 32353237.CrossRefGoogle ScholarPubMed
Manjarin, R, Steibel, J, Zamora, V, et al. (2011) Transcript abundance of amino acid transporters, β-casein, and α-lactalbumin in mammary tissue of periparturient, lactating, and postweaned sows. J Dairy Sci 94, 34673476.CrossRefGoogle ScholarPubMed
Calvert, D & Shennan, D (1996) Evidence for an interaction between cationic and neutral amino acids at the blood-facing aspect of the lactating rat mammary epithelium. J Dairy Res 63, 2533.CrossRefGoogle ScholarPubMed
Shennan, D, McNeillie, S, Jamieson, E, et al. (1994) Lysine transport in lactating rat mammary tissue: evidence for an interaction between cationic and neutral amino acids. Acta Physiol Scand 151, 461466.CrossRefGoogle ScholarPubMed
Abdelmagid, SA, Rickard, JA, McDonald, WJ, et al. (2011) CAT-1-mediated arginine uptake and regulation of nitric oxide synthases for the survival of human breast cancer cell lines. J Cell Biochem 112, 10841092.CrossRefGoogle ScholarPubMed
Too, CK & Abdelmagid, SA (2017) l-Arginine uptake and its role in the survival of breast cancer cells. In l-Arginine in Clinical Nutrition, pp. 253268 [Patel, VB, Preedy, VR and Rajendram, R, editors]. Cham: Springer.CrossRefGoogle Scholar
Karunakaran, S, Ramachandran, S, Coothankandaswamy, V, et al. (2011) SLC6A14 (ATB0,+) protein, a highly concentrative and broad specific amino acid transporter, is a novel and effective drug target for treatment of estrogen receptor-positive breast cancer. J Biol Chem 286, 3183031838.CrossRefGoogle Scholar
Lin, X, Li, S, Zou, Y, et al. (2018) Lysine stimulates protein synthesis by promoting the expression of ATB0,+ and activating the mTOR pathway in bovine mammary epithelial cells. J Nutr 148, 14261433.CrossRefGoogle ScholarPubMed
Hurley, W, Wang, H, Bryson, J, et al. (2000) Lysine uptake by mammary gland tissue from lactating sows. J Anim Sci 78, 391395.CrossRefGoogle ScholarPubMed
Wu, G, Bazer, FW, Satterfield, MC, et al. (2013) Impacts of arginine nutrition on embryonic and fetal development in mammals. Amino Acids 45, 241256.CrossRefGoogle ScholarPubMed
O’Quinn, P, Knabe, D & Wu, G (2002) Arginine catabolism in lactating porcine mammary tissue. J Anim Sci 80, 467474.CrossRefGoogle ScholarPubMed
Cui, Z, Guo, C-Y, Gao, K-G, et al. (2017) Dietary arginine supplementation in multiparous sows during lactation improves the weight gain of suckling piglets. J Integr Agr 16, 648655.Google Scholar
Ma, Q, Hu, S, Bannai, M, et al. (2018) l-Arginine regulates protein turnover in porcine mammary epithelial cells to enhance milk protein synthesis. Amino Acids 50, 621628.CrossRefGoogle ScholarPubMed
Wang, M, Xu, B, Wang, H, et al. (2014) Effects of arginine concentration on the in vitro expression of casein and mTOR pathway related genes in mammary epithelial cells from dairy cattle. PLOS ONE 9, e95985.CrossRefGoogle ScholarPubMed
Chantranupong, L, Scaria, SM, Saxton, RA, et al. (2016) The CASTOR proteins are arginine sensors for the mTORC1 pathway. Cell 165, 153164.CrossRefGoogle ScholarPubMed
Saxton, RA, Chantranupong, L, Knockenhauer, KE, et al. (2016) Mechanism of arginine sensing by CASTOR1 upstream of mTORC1. Nature 536, 229233.CrossRefGoogle ScholarPubMed
Kim, SW & Wu, G (2009) Regulatory role for amino acids in mammary gland growth and milk synthesis. Amino Acids 37, 8995.CrossRefGoogle ScholarPubMed
Holanda, D, Marcolla, C, Guimarães, S, et al. (2019) Dietary l-arginine supplementation increased mammary gland vascularity of lactating sows. Animal 13, 790798.CrossRefGoogle ScholarPubMed
National Research Council (2001) Nutrient Requirements of Dairy Cattle, 7th revised ed. Washington, DC: The National Academies Press.Google Scholar
Lapierre, H, Doepel, L, Milne, E, et al. (2009) Responses in mammary and splanchnic metabolism to altered lysine supply in dairy cows. Animal 3, 360371.CrossRefGoogle ScholarPubMed
Doelman, J, Kim, JJ, Carson, M, et al. (2015) Branched-chain amino acid and lysine deficiencies exert different effects on mammary translational regulation. J Dairy Sci 98, 78467855.CrossRefGoogle ScholarPubMed
Dong, X, Zhou, Z, Saremi, B, et al. (2018) Varying the ratio of Lys:Met while maintaining the ratios of Thr:Phe, Lys:Thr, Lys:His, and Lys:Val alters mammary cellular metabolites, mammalian target of rapamycin signaling, and gene transcription. J Dairy Sci 101, 17081718.CrossRefGoogle ScholarPubMed
Clemmensen, C, Smajilovic, S, Wellendorph, P, et al. (2014) The GPCR, class C, group 6, subtype A (GPRC6A) receptor: from cloning to physiological function. Br J Pharmacol 171, 11291141.CrossRefGoogle Scholar
Husted, AS, Trauelsen, M, Rudenko, O, et al. (2017) GPCR-mediated signaling of metabolites. Cell Metab 25, 777796.CrossRefGoogle ScholarPubMed
Gao, H-N, Hu, H, Zheng, N, et al. (2015) Leucine and histidine independently regulate milk protein synthesis in bovine mammary epithelial cells via mTOR signaling pathway. J Zhejiang Univ Sci B 16, 560572.CrossRefGoogle ScholarPubMed
Zhao, Y, Yan, S, Chen, L, et al. (2019) Effect of interaction between leucine and acetate on the milk protein synthesis in bovine mammary epithelial cells. Anim Sci J 90, 8189.CrossRefGoogle ScholarPubMed
Tian, W, Wu, T, Zhao, R, et al. (2017) Responses of milk production of dairy cows to jugular infusions of a mixture of essential amino acids with or without exclusion leucine or arginine. Anim Nutr 3, 271275.CrossRefGoogle ScholarPubMed
Zhang, J, He, W, Yi, D, et al. (2019) Regulation of protein synthesis in porcine mammary epithelial cells by l-valine. Amino Acids 51, 717726.CrossRefGoogle ScholarPubMed
Han, L, Batistel, F, Ma, Y, et al. (2018) Methionine supply alters mammary gland antioxidant gene networks via phosphorylation of nuclear factor erythroid 2-like 2 (NFE2L2) protein in dairy cows during the periparturient period. J Dairy Sci 101, 85058512.CrossRefGoogle ScholarPubMed
Lu, L, Gao, X, Li, Q, et al. (2012) Comparative phosphoproteomics analysis of the effects of l-methionine on dairy cow mammary epithelial cells. Can J Anim Sci 92, 433442.CrossRefGoogle Scholar
Zhang, Y, Wang, P, Lin, S, et al. (2018) mTORC1 signaling-associated protein synthesis in porcine mammary glands was regulated by the local available methionine depending on methionine sources. Amino Acids 50, 105115.CrossRefGoogle ScholarPubMed
Rosa, F & Osorio, J (2018) In vitro histone manipulation of bovine mammary epithelial cells through methionine supplementation. Dairy Science Publication Database, 1977. https://openprairie.sdstate.edu/dairy_pubdb/1977 (accessed March 2020).Google Scholar
Salama, A, Duque, M, Wang, L, et al. (2019) Enhanced supply of methionine or arginine alters mechanistic target of rapamycin signaling proteins, messenger RNA, and microRNA abundance in heat-stressed bovine mammary epithelial cells in vitro. J Dairy Sci 102, 24692480.CrossRefGoogle ScholarPubMed
Ding, L, Shen, Y, Wang, Y, et al. (2019) Jugular arginine supplementation increases lactation performance and nitrogen utilization efficiency in lactating dairy cows. J Anim Sci Biotechnol 10, 3.CrossRefGoogle ScholarPubMed
Zhao, F, Wu, T, Wang, H, et al. (2018) Jugular arginine infusion relieves lipopolysaccharide-triggered inflammatory stress and improves immunity status of lactating dairy cows. J Dairy Sci 101, 59615970.CrossRefGoogle ScholarPubMed
Wu, T, Wang, C, Ding, L, et al. (2016) Arginine relieves the inflammatory response and enhances the casein expression in bovine mammary epithelial cells induced by lipopolysaccharide. Mediators Inflamm 2016, 9618795.CrossRefGoogle ScholarPubMed
Xia, X, Che, Y, Gao, Y, et al. (2016) Arginine supplementation recovered the IFN-γ-mediated decrease in milk protein and fat synthesis by inhibiting the GCN2/eIF2α pathway, which induces autophagy in primary bovine mammary epithelial cells. Mol Cells 39, 410417.Google ScholarPubMed
Xia, X, Gao, Y, Zhang, J, et al. (2016) Autophagy mediated by arginine depletion activation of the nutrient sensor GCN2 contributes to interferon-γ-induced malignant transformation of primary bovine mammary epithelial cells. Cell Death Discov 2, 15065.CrossRefGoogle ScholarPubMed
Chen, L, Li, Z, Wang, M, et al. (2013) Preliminary report of arginine on synthesis and gene expression of casein in bovine mammary epithelial cell. Int Res J Agric Sci Soil Sci 3, 1723.Google Scholar