The biological functions and metabolic pathways of valine in swine.
Additional dosage
Biological function
Metabolic pathway
Pig
Valine
Journal
Journal of animal science and biotechnology
ISSN: 1674-9782
Titre abrégé: J Anim Sci Biotechnol
Pays: England
ID NLM: 101581293
Informations de publication
Date de publication:
07 Oct 2023
07 Oct 2023
Historique:
received:
05
05
2023
accepted:
03
08
2023
medline:
8
10
2023
pubmed:
8
10
2023
entrez:
7
10
2023
Statut:
epublish
Résumé
Valine is an essential amino acid and a type of branched-chain amino acid. Due to the involvement of branched-chain amino acids in various metabolic pathways, there has been a surge of interests in valine nutrition and its role in animal physiology. In pigs, the interactions between valine and other branched-chain amino acids or aromatic amino acids are complex. In this review, we delve into the interaction mechanism, metabolic pathways, and biological functions of valine. Appropriate valine supplementation not only enhances growth and reproductive performances, but also modulates gut microbiota and immune functions. Based on past observations and interpretations, we provide recommended feed levels of valine for weaned piglets, growing pigs, gilts, lactating sows, barrows and entire males. The summarized valine nutrient requirements for pigs at different stages offer valuable insights for future research and practical applications in animal husbandry.
Identifiants
pubmed: 37805513
doi: 10.1186/s40104-023-00927-z
pii: 10.1186/s40104-023-00927-z
pmc: PMC10559503
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
135Subventions
Organisme : National Natural Science Foundation of China
ID : 32130099
Organisme : Tianjin Synthetic Biotechnology Innovation Capacity Improvement Project
ID : TSBICIP-CXRC-038
Organisme : Laboratory of Lingnan Modern Agriculture Project
ID : NT2021005
Informations de copyright
© 2023. Chinese Association of Animal Science and Veterinary Medicine.
Références
Nie C, He T, Zhang W, Zhang G, Ma X. Branched chain amino acids: beyond nutrition metabolism. Int J Mol Sci. 2018;19(4):954. https://doi.org/10.3390/ijms19040954 .
doi: 10.3390/ijms19040954
pubmed: 29570613
pmcid: 5979320
Massey KA, Blakeslee CH, Pitkow HS. A review of physiological and metabolic effects of essential amino acids. Amino Acids. 1998;14(4):271–300. https://doi.org/10.1007/bf01318848 .
doi: 10.1007/bf01318848
pubmed: 9871473
Wu G. Amino acids: metabolism, functions, and nutrition. Amino Acids. 2009;37:1–17. https://doi.org/10.1007/s00726-009-0269-0 .
doi: 10.1007/s00726-009-0269-0
pubmed: 19301095
Wu G, Bazer FW, Davis TA, Jaeger LA, Johnson GA, Kim SW, et al. Important roles for the arginine family of amino acids in swine nutrition and production. Livestock Sci. 2007;112(1):8–22. https://doi.org/10.1016/j.livsci.2007.07.003 .
doi: 10.1016/j.livsci.2007.07.003
Neinast M, Murashige D, Arany Z. Branched chain amino acids. Annu Rev Physiol. 2019;81:139–64. https://doi.org/10.1146/annurev-physiol-020518-114455 .
doi: 10.1146/annurev-physiol-020518-114455
pubmed: 30485760
Zheng L, Wei H, He P, Zhao S, Xiang Q, Pang J, et al. Effects of supplementation of branched-chain amino acids to reduced-protein diet on skeletal muscle protein synthesis and degradation in the fed and fasted states in a piglet model. Nutrients. 2016;9(1):17. https://doi.org/10.3390/nu9010017 .
doi: 10.3390/nu9010017
pubmed: 28036018
pmcid: 5295061
Karau A, Grayson I. Amino acids in human and animal nutrition. Adv Biochem Eng Biotechnol. 2014;143:189–228. https://doi.org/10.1007/10_2014_269 .
doi: 10.1007/10_2014_269
pubmed: 24676880
Greiner L, Graham A, Goncalves M, Orlando U, Touchette KJ. Evaluation of the optimal standardized ileal digestible valine:lysine ratio in lactating sow diets1. J Anim Sci. 2019;97(7):2965–71. https://doi.org/10.1093/jas/skz177 .
doi: 10.1093/jas/skz177
pubmed: 31119289
pmcid: 6606485
Soumeh EA, van Milgen J, Sloth NM, Corrent E, Poulsen HD, Norgaard JV. Requirement of standardized ileal digestible valine to lysine ratio for 8- to 14-kg pigs. Animal. 2015;9(8):1312–8. https://doi.org/10.1017/S1751731115000695 .
doi: 10.1017/S1751731115000695
pubmed: 25951981
Yamamoto K, Tsuchisaka A, Yukawa H. Branched-chain amino acids. Adv Biochem Eng Biotechnol. 2017;159:103–28. https://doi.org/10.1007/10_2016_28 .
doi: 10.1007/10_2016_28
pubmed: 27872960
Chen M, Shi C, Zhao J, Gao Z, Zhang C. Application and microbial preparation of D-valine. World J Microbiol Biotechnol. 2016;32(10):171. https://doi.org/10.1007/s11274-016-2119-z .
doi: 10.1007/s11274-016-2119-z
pubmed: 27565781
Pundir CS, Lata S, Narwal V. Biosensors for determination of d and l- amino acids: a review. Biosens Bioelectron. 2018;117:373–84. https://doi.org/10.1016/j.bios.2018.06.033 .
doi: 10.1016/j.bios.2018.06.033
pubmed: 29960269
National Center for Biotechnology Information. PubChem compound summary for CID 6287, valine. 2022. https://pubchem.Ncbi.Nlm.Nih.Gov/compound/valine . Accessed 12 Sep 2022.
Cemin HS, Tokach MD, Woodworth JC, Dritz SS, DeRouchey JM, Goodband RD. Branched-chain amino acid interactions in growing pig diets. Transl Anim Sci. 2019;3(4):1246–53. https://doi.org/10.1093/tas/txz087 .
doi: 10.1093/tas/txz087
pubmed: 32704888
pmcid: 7200481
Yao CK, Muir JG, Gibson PR. Review article: insights into colonic protein fermentation, its modulation and potential health implications. Aliment Pharmacol Ther. 2016;43(2):181–96. https://doi.org/10.1111/apt.13456 .
doi: 10.1111/apt.13456
pubmed: 26527169
Liu S, Xie J, Fan Z, Ma X, Yin Y. Effects of low protein diet with a balanced amino acid pattern on growth performance, meat quality and cecal microflora of finishing pigs. J Sci Food Agric. 2023;103(2):957–67. https://doi.org/10.1002/jsfa.12245 .
doi: 10.1002/jsfa.12245
pubmed: 36178065
Wang L, Wang C, Peng Y, Zhang Y, Liu Y, Liu Y, et al. Research progress on anti-stress nutrition strategies in swine. Anim Nutr. 2023;13:342–60. https://doi.org/10.1016/j.aninu.2023.03.006 .
doi: 10.1016/j.aninu.2023.03.006
pubmed: 37214213
pmcid: 10192683
Rist VT, Weiss E, Eklund M, Mosenthin R. Impact of dietary protein on microbiota composition and activity in the gastrointestinal tract of piglets in relation to gut health: a review. Animal. 2013;7(7):1067–78. https://doi.org/10.1017/s1751731113000062 .
doi: 10.1017/s1751731113000062
pubmed: 23410993
Zhang GJ, Yi XW, Lu N, Qiao SY. Effects of low protein diet formulated by net energy system for growth performance and carcass characteristic of growing and finishing pigs. Chinese Journal of Animal Nutrition. 2010;22:557–63.
Nyachoti CM, Omogbenigun FO, Rademacher M, Blank G. Performance responses and indicators of gastrointestinal health in early-weaned pigs fed low-protein amino acid-supplemented diets. J Anim Sci. 2006;84(1):125–34. https://doi.org/10.2527/2006.841125x .
doi: 10.2527/2006.841125x
pubmed: 16361499
Wang Y, Zhou J, Wang G, Cai S, Zeng X, Qiao S. Advances in low-protein diets for swine. J Anim Sci Biotechnol. 2018;9:60. https://doi.org/10.1186/s40104-018-0276-7 .
Kim SW, Baker DH, Easter RA. Dynamic ideal protein and limiting amino acids for lactating sows: the impact of amino acid mobilization. J Anim Sci. 2001;79(9):2356–66. https://doi.org/10.2527/2001.7992356x .
doi: 10.2527/2001.7992356x
pubmed: 11583422
Kim WK, Singh AK, Wang J, Applegate T. Functional role of branched chain amino acids in poultry: a review. Poult Sci. 2022;101(5):101715. https://doi.org/10.1016/j.psj.2022.101715 .
doi: 10.1016/j.psj.2022.101715
pubmed: 35299066
pmcid: 8927823
Jansman AJM, Cirot O, Corrent E, Lambert W, Ensink J, van Diepen JTM. Interaction and imbalance between indispensable amino acids in young piglets. Animal. 2019;13(5):941–9. https://doi.org/10.1017/S175173111800263X .
doi: 10.1017/S175173111800263X
pubmed: 30333071
NRC. Nutrient requirements of swine. 11th ed. Washington: National Academy Press; 2012.
Whittemore CT, Hazzledine MJ, Close WH. Nutrient requirement standards for pigs. British Society of Animal Science (BSAS); 2003.
Mavromichalis I, Kerr BJ, Parr TM, Albin DM, Gabert VM, Baker DH. Valine requirement of nursery pigs. J Anim Sci. 2001;79(5):1223–9. https://doi.org/10.2527/2001.7951223x .
doi: 10.2527/2001.7951223x
pubmed: 11374542
Leyval D, Uy D, Delaunay S, Goergen JL, Engasser JM. Characterisation of the enzyme activities involved in the valine biosynthetic pathway in a valine-producing strain of Corynebacterium glutamicum. J Biotechnol. 2003;104(1–3):241–52. https://doi.org/10.1016/s0168-1656(03)00162-7 .
Park JH, Lee SY. Fermentative production of branched chain amino acids: a focus on metabolic engineering. Appl Microbiol Biotechnol. 2010;85(3):491–506. https://doi.org/10.1007/s00253-009-2307-y .
doi: 10.1007/s00253-009-2307-y
pubmed: 19844702
Nørgaard JV, Canibe N, Soumeh EA, Jensen BB, Nielsen B, Derkx P, et al. Evaluation of in situ valine production by Bacillus subtilis in young pigs. Animal. 2016;10(11):1796–802. https://doi.org/10.1017/s1751731116000781 .
Blombach B, Schreiner ME, Holátko J, Bartek T, Oldiges M, Eikmanns BJ. L-valine production with pyruvate dehydrogenase complex-deficient Corynebacterium glutamicum. Appl Environ Microb. 2007;73:7. https://doi.org/10.1128/AEM.02826-06 .
Han G, Xu N, Sun X, Chen J, Chen C, Wang Q. Improvement of L-valine production by atmospheric and room temperature plasma mutagenesis and high-throughput screening in Corynebacterium glutamicum. ACS Omega. 2020;5:4751−8. https://doi.org/10.1021/acsomega.9b02747 .
Hao Y, Pan X, Xing R, You J, Hu M, Liu Z, et al. High-level production of L-valine in Escherichia coli using multi-modular engineering. Bioresour Technol. 2022;359:127461. https://doi.org/10.1016/j.biortech.2022.127461 .
Zhang S, Zeng X, Ren M, Mao X, Qiao S. Novel metabolic and physiological functions of branched chain amino acids: a review. J Anim Sci Biotechnol. 2017;8:10. https://doi.org/10.1186/s40104-016-0139-z .
doi: 10.1186/s40104-016-0139-z
pubmed: 28127425
pmcid: 5260006
Kaiser JC, Sen S, Sinha A, Wilkinson BJ, Heinrichs DE. The role of two branched-chain amino acid transporters in staphylococcus aureus growth, membrane fatty acid composition and virulence. Mol Microbiol. 2016;102(5):850–64. https://doi.org/10.1111/mmi.13495 .
doi: 10.1111/mmi.13495
pubmed: 27589208
pmcid: 6225994
Taormina VM, Unger AL, Schiksnis MR, Torres-Gonzalez M, Kraft J. Branched-chain fatty acids-an underexplored class of dairy-derived fatty acids. Nutrients. 2020;12(9):2875. https://doi.org/10.3390/nu12092875 .
doi: 10.3390/nu12092875
pubmed: 32962219
pmcid: 7551613
Broer S. Amino acid transport across mammalian intestinal and renal epithelia. Physiol Rev. 2008;88(1):249–86. https://doi.org/10.1152/physrev.00018.2006 .
doi: 10.1152/physrev.00018.2006
pubmed: 18195088
Cole JT. Metabolism of BCAAs. In: Rajendram R, Preedy V, Patel V, editors. Branched chain amino acids in clinical nutrition. Nutrition and Health. New York: Humana Press; 2015. https://doi.org/10.1007/978-1-4939-1923-9_2 .
Kwon WB, Touchette KJ, Simongiovanni A, Syriopoulos K, Wessels A, Stein HH. Excess dietary leucine in diets for growing pigs reduces growth performance, biological value of protein, protein retention, and serotonin synthesis1. J Anim Sci. 2019;97(10):4282–92. https://doi.org/10.1093/jas/skz259 .
doi: 10.1093/jas/skz259
pubmed: 31410464
pmcid: 6776264
Cemin HS, Tokach MD, Dritz SS, Woodworth JC, DeRouchey JM, Goodband RD. Meta-regression analysis to predict the influence of branched-chain and large neutral amino acids on growth performance of pigs. J Anim Sci. 2019;97(6):2505–14. https://doi.org/10.1093/jas/skz118 .
Morales A, Arce N, Cota M, Buenabad L, Avelar E, Htoo JK, et al. Effect of dietary excess of branched-chain amino acids on performance and serum concentrations of amino acids in growing pigs. J Anim Physiol Anim Nutr. 2016;100(1):39–45. https://doi.org/10.1111/jpn.12327 .
Holen JP, Tokach MD, Woodworth JC, DeRouchey JM, Gebhardt JT, Titgemeyer EC, et al. A review of branched-chain amino acids in lactation diets on sow and litter growth performance. Transl Anim Sci. 2022;6(1):txac017. https://doi.org/10.1093/tas/txac017 .
Wiltafsky MK, Pfaffl MW, Roth FX. The effects of branched-chain amino acid interactions on growth performance, blood metabolites, enzyme kinetics and transcriptomics in weaned pigs. Br J Nutr. 2010;103(7):964–76. https://doi.org/10.1017/S0007114509992212 .
doi: 10.1017/S0007114509992212
pubmed: 20196890
Bröer S. Amino acid transport across mammalian intestinal and renal epithelia. Physiolog Rev. 2008;88:1249–86.
Harper AE, Miller RH, Block KP. Branched-chain amino acid metabolism. Annu Rev Nutr. 1984;4:409–54. https://doi.org/10.1146/annurev.nu.04.070184.002205 .
doi: 10.1146/annurev.nu.04.070184.002205
pubmed: 6380539
Hagenfeldt L, Eriksson S, Wahren J. Influence of leucine on arterial concentrations and regional exchange of amino acids in healthy subjects. Clin Sci. 1980;59(3):173–81. https://doi.org/10.1042/cs0590173 .
Harper AE, Block KP, Cree TC. Branched-chain amino acids: Nutritional and metabolic interrelationship. In: Pion R, Arnal M, Bonin D, editors. Proceedings of the Fourth Symposium on Protein Metabolism and Nutrition. Paris: INRA; 1983.
Swendseid ME, Villalobos J, Figueroa WS, Drenick EJ. The effects of test doses of leucine, isoleucine or valine on plasma amino acid levels. The unique effect of leucine. Am J Clin Nutr. 1965;17(5):317–21. https://doi.org/10.1093/ajcn/17.5.317 .
doi: 10.1093/ajcn/17.5.317
pubmed: 5846904
NRC. Nutrient requirements of swine. 10th ed. Washington: National Academy Press; 1998.
Gloaguen M, Le Floc’h N, Corrent E, Primot Y, van Milgen J. Providing a diet deficient in valine but with excess leucine results in a rapid decrease in feed intake and modifies the postprandial plasma amino acid and alpha-keto acid concentrations in pigs. J Anim Sci. 2012;90(9):3135–42. https://doi.org/10.2527/jas.2011-4956 .
Elango R, Pencharz PB, Ball RO. The branched-chain amino acid requirement of parenterally fed neonatal piglets is less than the enteral requirement. J Nutr. 2002;132(10):3123–9. https://doi.org/10.1093/jn/131.10.3123 .
doi: 10.1093/jn/131.10.3123
pubmed: 12368405
Millet S, Aluwé M, Ampe B, De Campeneere S. Interaction between amino acids on the performances of individually housed piglets. J Anim Physiol Anim Nutr. 2015;99(2):230–6. https://doi.org/10.1111/jpn.12227 .
Hjelle JT, Baird-Lambert J, Cardinale G, Specor S, Udenfriend S. Isolated microvessels: the blood-brain barrier in vitro. Proc Natl Acad Sci U S A. 1978;75(9):4544–8. https://doi.org/10.1073/pnas.75.9.4544 .
doi: 10.1073/pnas.75.9.4544
pubmed: 279933
pmcid: 336153
Hargreaves KM, Pardridge WM. Neutral amino acid transport at the human blood-brain barrier. J Biol Chem. 1988;263(36):19392–7. https://doi.org/10.1016/S0021-9258(19)77645-5 .
doi: 10.1016/S0021-9258(19)77645-5
pubmed: 2848825
Morales A, García H, Araiza A, Htoo JK, Cota M, Arce N, et al. Effect of L-valine supplementation to a wheat-based diet with leucine excess on performance, gene expression, and serum concentration of amino acids. J Anim Sci. 2012;90(Suppl):489–91. https://doi.org/10.2527/jas.51189 .
doi: 10.2527/jas.51189
Xu D, Wang Y, Jiao N, Qiu K, Zhang X, Wang L, et al. The coordination of dietary valine and isoleucine on water holding capacity, pH value and protein solubility of fresh meat in finishing pigs. Meat Sci. 2020;163:108074. https://doi.org/10.1016/j.meatsci.2020.108074 .
doi: 10.1016/j.meatsci.2020.108074
pubmed: 32036285
Richert BT, Goodband RD, Tokach MD, Nelssen JL. Increasing valine, isoleucine, and total branched-chain amino acids for lactating sows. J Anim Sci. 1997;75(8):2117–28. https://doi.org/10.2527/1997.7582117x .
doi: 10.2527/1997.7582117x
pubmed: 9263059
D’Mello JP, Lewis D. Amino acid interactions in chick nutrition. 2. Interrelationships between leucine, isoleucine and valine. Br Poult Sci. 1970;11(3):313–23. https://doi.org/10.1080/00071667008415821 .
Burnham D, Emmans GC, Gous RM. Isoleucine requirements of the chicken: the effect of excess leucine and valine on the response to isoleucine. Br Poult Sci. 1992;33(1):71–87. https://doi.org/10.1080/00071669208417445 .
doi: 10.1080/00071669208417445
pubmed: 1571809
Skvorak KJ, Dorko K, Marongiu F, Tahan V, Hansel MC, Gramignoli R, et al. Placental stem cell correction of murine intermediate maple syrup urine disease. Hepatology. 2013;57:1017–23.
doi: 10.1002/hep.26150
pubmed: 23175463
Verrey F. System l: Heteromeric exchangers of large, neutral amino acids involved in directional transport. Pflugers Arch. 2003;445(5):529–33. https://doi.org/10.1007/s00424-002-0973-z .
doi: 10.1007/s00424-002-0973-z
pubmed: 12634921
Parthasarathy A, Cross PJ, Dobson R, Adams LE, Hudson AO. A three-ring circus: Metabolism of the three proteogenic aromatic amino acids and their role in the health of plants and animals. Front Mol Biosci. 2018;5:29. https://doi.org/10.3389/fmolb.2018.00029 .
Pytka K, Głuch-Lutwin M, Żmudzka E, Sałaciak K, Siwek A, Niemczyk K, et al. HBK-17, a 5-HT
Okamura K, Matsubara F, Yoshioka Y, Kikuchi N, Kikuchi Y, Kohri H. Exercise-induced changes in branched chain amino acid/aromatic amino acid ratio in the rat brain and plasma. Jpn J Pharmacol. 1987;45(2):243–8. https://doi.org/10.1254/jjp.45.243 .
doi: 10.1254/jjp.45.243
pubmed: 3437593
Arfuso F, Assenza A, Fazio F, Rizzo M, Giannetto C, Piccione G. Dynamic change of serum levels of some branched-chain amino acids and tryptophan in athletic horses after different physical exercises. J Equine Vet Sci. 2019;77:12–6. https://doi.org/10.1016/j.jevs.2019.02.006 .
doi: 10.1016/j.jevs.2019.02.006
pubmed: 31133304
Jin G, Kataoka Y, Tanaka M, Mizuma H, Nozaki S, Tahara T, et al. Changes in plasma and tissue amino acid levels in an animal model of complex fatigue. Nutrition. 2009;25(5):597–607. https://doi.org/10.1016/j.nut.2008.11.021 .
doi: 10.1016/j.nut.2008.11.021
pubmed: 19216057
Seve B. Physiological roles of tryptophan in pig nutrition. Adv Exp Med Biol. 1999;467:729–41. https://doi.org/10.1007/978-1-4615-4709-9_95 .
doi: 10.1007/978-1-4615-4709-9_95
pubmed: 10721126
Shimomura Y, Harris RA. Metabolism and physiological function of branched-chain amino acids: discussion of session 1. J Nutr. 2006;136(1):232S–3S. https://doi.org/10.1093/jn/136.1.232S .
Li P, Knabe DA, Kim SW, Lynch CJ, Hutson SM, Wu G. Lactating porcine mammary tissue catabolizes branched-chain amino acids for glutamine and aspartate synthesis. J Nutr. 2009;139(8):1502–9. https://doi.org/10.3945/jn.109.105957 .
doi: 10.3945/jn.109.105957
pubmed: 19549750
pmcid: 3151199
Aftring RP, Miller WJ, Buse MG. Effects of diabetes and starvation on skeletal muscle branched-chain alpha-keto acid dehydrogenase activity. Am J Physiol. 1988;254(3):E292.
pubmed: 2964788
Aftring RP, Manos PN, Buse MG. Catabolism of branched-chain amino acids by diaphragm muscles of fasted and diabetic rats. Metabolism. 1985;34(8):702–11. https://doi.org/10.1016/0026-0495(85)90018-6 .
doi: 10.1016/0026-0495(85)90018-6
pubmed: 4021802
Nakahara K, Takata S, Ishii A, Nagao K, Bannai M, Takahashi M, et al. Somatostatin is involved in anorexia in mice fed a valine-deficient diet. Amino Acids. 2012;42(4):1397–404. https://doi.org/10.1007/s00726-011-0836-z .
doi: 10.1007/s00726-011-0836-z
pubmed: 21293891
Comesaña S, Chivite M, Blanco AM, Alborja-Valado M, Calo J, Conde-Sieira M, et al. Involvement of mechanistic target of rapamycin (mtor) in valine orexigenic effects in rainbow trout. Aquacul Nutr. 2022;2022:7509382. https://doi.org/10.1155/2022/7509382 .
doi: 10.1155/2022/7509382
Gloaguen M, Le Floc’h N, Brossard L, Barea R, Primot Y, Corrent E, et al. Response of piglets to the valine content in diet in combination with the supply of other branched-chain amino acids. Animal. 2011;5(11):1734–42. https://doi.org/10.1017/S1751731111000760 .
Furuse M. Release and endogenous actions of the gastrin/cholecystokinin (CCK) family in the chicken. J Exp Zool. 1999;283(4–5):448–54.
Otsuki M. Pathophysiological role of cholecystokinin in humans. J Gastroenterol Hepatol. 2000;15(S1):71–83. https://doi.org/10.1046/j.1440-1746.2000.02178.x .
Ebenezer IS, de la Riva C, Baldwin BA. Effects of the cck receptor antagonist mk-329 on food intake in pigs. Physiol Behav. 1990;47(1):145–8. https://doi.org/10.1016/0031-9384(90)90053-7 .
doi: 10.1016/0031-9384(90)90053-7
pubmed: 2326329
Fan W, Ellacott KL, Halatchev IG, Takahashi K, Yu P, Cone RD. Cholecystokinin-mediated suppression of feeding involves the brainstem melanocortin system. Nat Neurosci. 2004;7(4):335–6. https://doi.org/10.1038/nn1214 .
doi: 10.1038/nn1214
pubmed: 15034587
Zhang X, Liu X, Jia H, He P, Mao X, Qiao S, et al. Valine supplementation in a reduced protein diet regulates growth performance partially through modulation of plasma amino acids profile, metabolic responses, endocrine, and neural factors in piglets. J Agric Food Chem. 2018;66(12):3161–8. https://doi.org/10.1021/acs.jafc.8b01113 .
doi: 10.1021/acs.jafc.8b01113
pubmed: 29526104
Habibi MA-O, Goodarzi PA-OX, Shili CN, Sutton J, Wileman CM, Kim DM, et al. A mixture of valine and isoleucine restores the growth of protein-restricted pigs likely through improved gut development, hepatic IGF-1 pathway, and plasma metabolomic profile. Int J Mol Sci. 2022;23(6):3300. https://doi.org/10.3390/ijms23063300 .
Yin J, Ma J, Li Y, Ma X, Chen J, Zhang H, et al. Branched-chain amino acids, especially of leucine and valine, mediate the protein restricted response in a piglet model. Food Funct. 2020;11(2):1304–11. https://doi.org/10.1039/c9fo01757g .
doi: 10.1039/c9fo01757g
pubmed: 32016208
Goodarzi PA-OX, Wileman CM, Habibi MA-O, Walsh K, Sutton J, Shili CN, et al. Effect of isoleucine and added valine on performance, nutrients digestibility and gut microbiota composition of pigs fed with very low protein diets. Int J Mol Sci. 2022;23(23):14886. https://doi.org/10.3390/ijms232314886 .
Duan Y, Li F, Guo Q, Wang W, Zhang L, Wen C, et al. Branched-chain amino acid ratios modulate lipid metabolism in adipose tissues of growing pigs. J Funct Foods. 2018;40:614–24. https://doi.org/10.1016/j.jff.2017.12.004
Xu M, Che L, Niu L, Wang L, Li M, Jiang D, et al. Molecular mechanism of valine and its metabolite in improving triglyceride synthesis of porcine intestinal epithelial cells. Sci Rep. 2023;13(1):2933. https://doi.org/10.1038/s41598-023-30036-w .
doi: 10.1038/s41598-023-30036-w
pubmed: 36806358
pmcid: 9941501
Lo EKK, Felicianna, Xu JH, Zhan Q, Zeng Z, El-Nezami H. The emerging role of branched-chain amino acids in liver diseases. Biomedicines. 2022;10(6):1444. https://doi.org/10.3390/biomedicines10061444 .
Jian H, Miao S, Liu Y, Wang X, Xu Q, Zhou W, et al. Dietary valine ameliorated gut health and accelerated the development of nonalcoholic fatty liver disease of laying hens. Oxid Med Cell Longev. 2021;2021:4704771. https://doi.org/10.1155/2021/4704771 .
doi: 10.1155/2021/4704771
pubmed: 34484560
pmcid: 8410442
Wu J, Ma N, Johnston LJ, Ma X. Dietary nutrients mediate intestinal host defense peptide expression. Adv Nutr. 2020;11(1):92–102. https://doi.org/10.1093/advances/nmz057 .
doi: 10.1093/advances/nmz057
pubmed: 31204774
Yeung AT, Gellatly SL, Hancock RE. Multifunctional cationic host defence peptides and their clinical applications. Cell Mol Life Sci. 2011;68(13):2161–76. https://doi.org/10.1007/s00018-011-0710-x .
doi: 10.1007/s00018-011-0710-x
pubmed: 21573784
Ren M, Zhang S, Liu X, Li S, Mao X, Zeng X, et al. Different lipopolysaccharide branched-chain amino acids modulate porcine intestinal endogenous beta-defensin expression through the sirt1/erk/90rsk pathway. J Agric Food Chem. 2016;64(17):3371–9. https://doi.org/10.1021/acs.jafc.6b00968 .
doi: 10.1021/acs.jafc.6b00968
pubmed: 27083206
Veldhuizen EJ, Rijnders M, Claassen EA, van Dijk A, Haagsman HP. Porcine beta-defensin 2 displays broad antimicrobial activity against pathogenic intestinal bacteria. Mol Immunol. 2008;45(2):386–94. https://doi.org/10.1016/j.molimm.2007.06.001 .
doi: 10.1016/j.molimm.2007.06.001
pubmed: 17658606
Dai ZL, Zhang J, Wu G, Zhu WY. Utilization of amino acids by bacteria from the pig small intestine. Amino Acids. 2010;39(5):1201–15. https://doi.org/10.1007/s00726-010-0556-9 .
doi: 10.1007/s00726-010-0556-9
pubmed: 20300787
Heo JM, Kim JC, Hansen CF, Mullan BP, Hampson DJ, Pluske JR. Effects of feeding low protein diets to piglets on plasma urea nitrogen, faecal ammonia nitrogen, the incidence of diarrhoea and performance after weaning. Arch Anim Nutr. 2008;62(5):343–58. https://doi.org/10.1080/17450390802327811 .
doi: 10.1080/17450390802327811
pubmed: 18942582
Aumaitre A, Peiniau J, Madec F. Digestive adaptation after weaning and nutritional consequences in the piglet. Pig News and Information. 1995;16:73N–9N.
Houdijk J, Campbell FM, Fortomaris PD, Eckersall PD, Kyriazakis I. Effects of sub-clinical post-weaning colibacillosis and dietary protein on acute phase proteins in weaner pigs. Livest Sci. 2007;108(1–3):182–5.
doi: 10.1016/j.livsci.2007.01.048
Gao J, Liu Z, Wang C, Ma L, Chen Y, Li T. Effects of dietary protein level on the microbial composition and metabolomic profile in postweaning piglets. Oxid Med Cell Longev. 2022;2022:3355687. https://doi.org/10.1155/2022/3355687 .
doi: 10.1155/2022/3355687
pubmed: 35401925
pmcid: 8986435
Pluske JR, Pethick DW, Hopwood DE, Hampson DJ. Nutritional influences on some major enteric bacterial diseases of pig. Nutr Res Rev. 2002;15(2):333–71. https://doi.org/10.1079/NRR200242 .
doi: 10.1079/NRR200242
pubmed: 19087411
Spring S, Premathilake H, Bradway C, Shili C, Pezeshki A. Effect of very low-protein diets supplemented with branched-chain amino acids on energy balance, plasma metabolomics and fecal microbiome of pigs. Sci Rep. 2020;10:15859. https://doi.org/10.1038/s41598-020-72816-8 .
Chen XH, Liu SR, Peng B, Li D, Cheng ZX, Zhu JX, et al. Exogenous L-valine promotes phagocytosis to kill multidrug-resistant bacterial pathogens. Front Immunol. 2017;8:207. https://doi.org/10.3389/fimmu.2017.00207 .
doi: 10.3389/fimmu.2017.00207
pubmed: 28321214
pmcid: 5337526
Ma QQ, Dong N, Shan AS, Wang L, Hu WN, Sun WY. Biochemical property and in vivo efficacies of novel Val/Arg-rich antimicrobial peptide. Protein Pept Lett. 2012;19(11):1144–8. https://doi.org/10.2174/092986612803217132 .
doi: 10.2174/092986612803217132
pubmed: 22587781
Ma QQ, Shan AS, Dong N, Gu Y, Sun WY, Hu WN, et al. Cell selectivity and interaction with model membranes of val/arg-rich peptides. J Pept Sci. 2011;17(7):520–6. https://doi.org/10.1002/psc.1360 .
doi: 10.1002/psc.1360
pubmed: 21425418
Zhou H, Yu B, Gao J, Htoo JK, Chen D. Regulation of intestinal health by branched-chain amino acids. Anim Sci J. 2018;89(1):3–11. https://doi.org/10.1111/asj.12937 .
doi: 10.1111/asj.12937
pubmed: 29164733
Negro M, Giardina S, Marzani B, Marzatico F. Branched-chain amino acid supplementation does not enhance athletic performance but affects muscle recovery and the immune system. J Sports Med Phys Fitness. 2008;48(3):347–51.
pubmed: 18974721
Ma N, Guo P, Zhang J, He T, Kim SW, Zhang G, et al. Nutrients mediate intestinal bacteria-mucosal immune crosstalk. Front Immunol. 2018;9:5. https://doi.org/10.3389/fimmu.2018.00005 .
doi: 10.3389/fimmu.2018.00005
pubmed: 29416535
pmcid: 5787545
Kinnebrew MA, Pamer EG. Innate immune signaling in defense against intestinal microbes. Immunol Rev. 2012;245(1):113–31. https://doi.org/10.1111/j.1600-065X.2011.01081.x .
doi: 10.1111/j.1600-065X.2011.01081.x
pubmed: 22168416
pmcid: 4624287
Jose DG. Quantitative effects of nutritional essential amino acid deficiency upon immune responses to tumors in mice. J Exper Med. 1973;137(1):1–9. https://doi.org/10.1084/jem.137.1.1 .
doi: 10.1084/jem.137.1.1
Tsukishiro T, Shimizu Y, Higuchi K, Watanabe A. Effect of branched-chain amino acids on the composition and cytolytic activity of liver-associated lymphocytes in rats. J Gastroenterol Hepatol. 2010;15(8):849–59.
doi: 10.1046/j.1440-1746.2000.02220.x
Go M, Shin E, Jang SY, Nam M, Hwang GS, Lee SY. Bcat1 promotes osteoclast maturation by regulating branched-chain amino acid metabolism. Exp Mol Med. 2022;54(6):825–33. https://doi.org/10.1038/s12276-022-00775-3 .
doi: 10.1038/s12276-022-00775-3
pubmed: 35760874
pmcid: 9256685
Chuang JC, Yu CL, Wang SR. Modulation of human lymphocyte proliferation by amino acids. Clin Exp Immunol. 1990;81(1):173–6. https://doi.org/10.1111/j.1365-2249.1990.tb05310.x .
doi: 10.1111/j.1365-2249.1990.tb05310.x
pubmed: 2379319
pmcid: 1535017
Waithe WI, Dauphinais C, Hathaway P, Hirschhorn K. Protein synthesis in stimulated lymphocytes: II amino acid requirements. Cell Immunol. 1975;17(2):323–34.
doi: 10.1016/S0008-8749(75)80036-0
pubmed: 805000
Dauphinais C, Waithe WI. PHA stimulation of human lymphocytes during amino acid deprivation. Protein, RNA and DNA synthesis. J Cell Physiol. 1977. https://doi.org/10.1002/jcp.1040910305 .
Ren M, Zhang SH, Zeng XF, Liu H, Qiao SY. Branched-chain amino acids are beneficial to maintain growth performance and intestinal immune-related function in weaned piglets fed protein restricted diet. Asian-Australas J Anim Sci. 2015;28(12):1742–50. https://doi.org/10.5713/ajas.14.0131 .
doi: 10.5713/ajas.14.0131
pubmed: 26580442
pmcid: 4647083
Zhao L, Li Y, Li Z, Wu S, Huang K, Chen J, et al. Effect of the valine-to-lysine ratio on the performance of sows and piglets in a hot, humid environment. J Therm Biol. 2019;81:89–97. https://doi.org/10.1016/j.jtherbio.2019.02.021 .
doi: 10.1016/j.jtherbio.2019.02.021
pubmed: 30975428
Kakazu E, Kanno N, Ueno Y, Shimosegawa T. Extracellular branched-chain amino acids, especially valine, regulate maturation and function of monocyte-derived dendritic cells. J Immunol. 2007;179(10):7137–46. https://doi.org/10.4049/jimmunol.179.10.7137 .
doi: 10.4049/jimmunol.179.10.7137
pubmed: 17982106
Devillers N, Le Dividich J, Prunier A. Influence of colostrum intake on piglet survival and immunity. Animal. 2011;5(10):1605–12. https://doi.org/10.1017/S175173111100067x .
doi: 10.1017/S175173111100067x
pubmed: 22440352
Inoue R, Tsukahara T. Composition and physiological functions of the porcine colostrum. Anim Sci J. 2021;92(1):e13618. https://doi.org/10.1111/asj.13618 .
doi: 10.1111/asj.13618
pubmed: 34409709
pmcid: 9286568
Ogawa S, Tsukahara T, Imaoka T, Nakanishi N, Ushida K, Inoue R. The effect of colostrum ingestion during the first 24 hours of life on early postnatal development of piglet immune systems. Anim Sci J. 2016;87(12):1511–5. https://doi.org/10.1111/asj.12573 .
doi: 10.1111/asj.12573
pubmed: 26990379
Dividich JL, Herpin P. Nutritional and immunological importance of colostrum for the new-born pig. J Agri Sci. 2005;143:469–85. https://doi.org/10.1017/S0021859605005642 .
doi: 10.1017/S0021859605005642
Hales J, Moustsen VA, Nielsen MB, Hansen CF. Higher preweaning mortality in free farrowing pens compared with farrowing crates in three commercial pig farms. Animal. 2014;8(1):113–20. https://doi.org/10.1017/s1751731113001869 .
doi: 10.1017/s1751731113001869
pubmed: 24152336
Schnier S, Middendorf L, Janssen H, Bruning C, Rohn K, Visscher C. Immunocrit, serum amino acid concentrations and growth performance in light and heavy piglets depending on sow’s farrowing system. Porcine Health Manag. 2019;5:14. https://doi.org/10.1186/s40813-019-0121-1 .
Meek JY, Noble L. Breastfeeding and the use of human milk. J Obstet Gynecol Neonatal Nurs. 2021;50(5):e1–5. https://doi.org/10.1016/j.jogn.2021.06.006 .
doi: 10.1016/j.jogn.2021.06.006
Zheng W, Zhao W, Wu M, Song X, Caro F, Sun X, et al. Microbiota-targeted maternal antibodies protect neonates from enteric infection. Nature. 2020;577(7791):543–8. https://doi.org/10.1038/s41586-019-1898-4 .
doi: 10.1038/s41586-019-1898-4
pubmed: 31915378
pmcid: 7362890
Difilippo E, Pan F, Logtenberg M, Willems RH, Braber S, Fink-Gremmels J, et al. In vitro fermentation of porcine milk oligosaccharides and galacto-oligosaccharides using piglet fecal inoculum. J Agric Food Chem. 2016;64(10):2127–33. https://doi.org/10.1021/acs.jafc.5b05384 .
doi: 10.1021/acs.jafc.5b05384
pubmed: 26898103
Wang L, Liu Q, Chen Y, Zheng X, Wang C, Qi Y, et al. Antioxidant potential of pediococcus pentosaceus strains from the sow milk bacterial collection in weaned piglets. Microbiome. 2022;10(1):83. https://doi.org/10.1186/s40168-022-01278-z .
doi: 10.1186/s40168-022-01278-z
pubmed: 35650642
pmcid: 9158380
Mosnier E, Etienne M, Ramaekers P, Père MC. The metabolic status during the peri partum period affects the voluntary feed intake and the metabolism of the lactating multiparous sow. Livest Sci. 2010;127(2–3):127–36. https://doi.org/10.1016/j.livsci.2009.06.023 .
doi: 10.1016/j.livsci.2009.06.023
Theil PK, Lauridsen C, Quesnel H. Neonatal piglet survival: Impact of sow nutrition around parturition on fetal glycogen deposition and production and composition of colostrum and transient milk. Animal. 2014;8(7):1021–30. https://doi.org/10.1017/s1751731114000950 .
doi: 10.1017/s1751731114000950
pubmed: 24762853
Manjarin R, Bequette BJ, Wu G, Trottier NL. Linking our understanding of mammary gland metabolism to amino acid nutrition. Amino Acids. 2014;46(11):2447–62. https://doi.org/10.1007/s00726-014-1818-8 .
doi: 10.1007/s00726-014-1818-8
pubmed: 25195161
Tokach MD, Menegat MB, Gourley KM, Goodband RD. Review: nutrient requirements of the modern high-producing lactating sow, with an emphasis on amino acid requirements. Animal. 2019;13(12):2967–77. https://doi.org/10.1017/s1751731119001253 .
doi: 10.1017/s1751731119001253
pubmed: 31199216
Feyera T, Theil PK. Energy and lysine requirements and balances of sows during transition and lactation: a factorial approach. Livestock Sci. 2017;201:50–7.
doi: 10.1016/j.livsci.2017.05.001
Jackson SC, Bryson JM, Wang H, Hurley WL. Cellular uptake of valine by lactating porcine mammary tissue. J Anim Sci. 2000;78(11):2927–32. https://doi.org/10.2527/2000.78112927x .
doi: 10.2527/2000.78112927x
pubmed: 11063318
Manjarin R, Zamora V, Wu G, Steibel JP, Kirkwood RN, Taylor NP, et al. Effect of amino acids supply in reduced crude protein diets on performance, efficiency of mammary uptake, and transporter gene expression in lactating sows. J Anim Sci. 2012;90(9):3088–100. https://doi.org/10.2527/jas.2011-4338 .
doi: 10.2527/jas.2011-4338
pubmed: 22585816
Strathe AV, Bruun TS, Zerrahn JE, Tauson AH, Hansen CF. The effect of increasing the dietary valine-to-lysine ratio on sow metabolism, milk production, and litter growth. J Anim Sci. 2016;94(1):155–64. https://doi.org/10.2527/jas.2015-9267 .
doi: 10.2527/jas.2015-9267
pubmed: 26812322
Kim SW, Hurley WL, Wu G, Ji F. Ideal amino acid balance for sows during gestation and lactation. J Anim Sci. 2009;87(14 Suppl):E123–32. https://doi.org/10.2527/jas.2008-1452 .
doi: 10.2527/jas.2008-1452
pubmed: 19098235
Hong J, Lee E. Intrafollicular amino acid concentration and the effect of amino acids in a defined maturation medium on porcine oocyte maturation, fertilization, and preimplantation development. Theriogenology. 2007;68(5):728–35. https://doi.org/10.1016/j.theriogenology.2007.06.002 .
doi: 10.1016/j.theriogenology.2007.06.002
pubmed: 17658593
Che L, Xu M, Gao K, Wang L, Yang X, Wen X, et al. Valine supplementation during late pregnancy in gilts increases colostral protein synthesis through stimulating mtor signaling pathway in mammary cells. Amino Acids. 2019;51(10–12):1547–59. https://doi.org/10.1007/s00726-019-02790-7 .
doi: 10.1007/s00726-019-02790-7
pubmed: 31720834
Boyd RD, Kensinger RS. Metabolic precursors for milk synthesis. In: Verstegen MWA, Verstegen PS, Schrama JW, editors. The Lactating Sow. Wageningen: Wageningen Pers; 1998. p. 69–93.
Che L, Xu M, Gao K, Wang L, Yang X, Wen X, et al. Effects of dietary valine supplementation during late gestation on the reproductive performance and mammary gland development of gilts. J Anim Sci Biotechnol. 2020;11:15. https://doi.org/10.1186/s40104-019-0420-z .
doi: 10.1186/s40104-019-0420-z
pubmed: 32099647
pmcid: 7029528
Moser SA, Tokach MD, Dritz SS, Goodband RD, Nelssen JL, Loughmiller JA. The effects of branched-chain amino acids on sow and litter performance. J Anim Sci. 2000;78(3):658–67. https://doi.org/10.2527/2000.783658x .
doi: 10.2527/2000.783658x
pubmed: 10764073
Paulicks BR, Ott H, Roth-Maier DA. Performance of lactating sows in response to the dietary valine supply. J Anim Physiol Anim Nutr (Berl). 2003;87(11–12):389–96. https://doi.org/10.1046/j.1439-0396.2003.00449.x .
doi: 10.1046/j.1439-0396.2003.00449.x
pubmed: 14633048
Williams AM, Safranski TJ, Spiers DE, Eichen PA, Coate EA, Lucy MC. Effects of a controlled heat stress during late gestation, lactation, and after weaning on thermoregulation, metabolism, and reproduction of primiparous sows. J Anim Sci. 2013;91(6):2700–14. https://doi.org/10.2527/jas.2012-6055 .
doi: 10.2527/jas.2012-6055
pubmed: 23508026
Hao Y, Xing M, Gu X. Research progress on oxidative stress and its nutritional regulation strategies in pigs. Animals (Basel). 2021;11(5):1384. https://doi.org/10.3390/ani11051384 .
doi: 10.3390/ani11051384
pubmed: 34068057
pmcid: 8152462
Montilla SI, Johnson TP, Pearce SC, Gardan-Salmon D, Gabler NK, Ross JW, et al. Heat stress causes oxidative stress but not inflammatory signaling in porcine skeletal muscle. Temperature (Austin). 2014;1(1):42–50. https://doi.org/10.4161/temp.28844 .
doi: 10.4161/temp.28844
pubmed: 27583280
Holmes CW. The energy and protein metabolism of pigs growing at a high ambient temperature. Anim Sci. 2010;16(02):117–33. https://doi.org/10.1017/S0003356100029937 .
doi: 10.1017/S0003356100029937
Bertoldo MJ, Holyoake PK, Evans G, Grupen CG. Seasonal variation in the ovarian function of sows. Reprod Fertil Dev. 2012;24(6):822–34. https://doi.org/10.1071/rd11249 .
doi: 10.1071/rd11249
pubmed: 22781933
Prunier A, Bragana M, Dividich JL. Influence of high ambient temperature on performance of reproductive sows. Livest Prod Sci. 1997;52(2):123–33. https://doi.org/10.1016/S0301-6226(97)00137-1 .
doi: 10.1016/S0301-6226(97)00137-1
Black JL, Mullan BP, Lorschy ML, Giles LR. Lactation in the sow during heat stress. Livest Prod Sci. 1993;35(1–2):153–70. https://doi.org/10.1016/0301-6226(93)90188-N .
doi: 10.1016/0301-6226(93)90188-N
Quiniou N, Noblet J. Influence of high ambient temperatures on performance of multiparous lactating sows. J Anim Sci. 1999;77(8):2124–34. https://doi.org/10.2527/1999.7782124x .
doi: 10.2527/1999.7782124x
pubmed: 10461991
Meyer F, van Rensburg CJ, Gous RM. The response of weaned piglets to dietary valine and leucine. Animal. 2017;11(8):1279–86. https://doi.org/10.1017/S1751731116002834 .
doi: 10.1017/S1751731116002834
pubmed: 28077194
Nowacka-Woszuk J. Nutrigenomics in livestock-recent advances. J Appl Genet. 2020;61(1):93–103. https://doi.org/10.1007/s13353-019-00522-x .
doi: 10.1007/s13353-019-00522-x
pubmed: 31673964
Barea R, Brossard L, Le Floc’h N, Primot Y, Melchior D, van Milgen J. The standardized ileal digestible valine-to-lysine requirement ratio is at least seventy percent in postweaned piglets. J Anim Sci. 2009;87(3):935–47. https://doi.org/10.2527/jas.2008-1006 .
Siebert D, Khan DR, Torrallardona D. The optimal valine to lysine ratio for performance parameters in weaned piglets. Animals (Basel). 2021;11(5):1255. https://doi.org/10.3390/ani11051255 .
doi: 10.3390/ani11051255
pubmed: 33925439
Wiltafsky MK, Schmidtlein B, Roth FX. Estimates of the optimum dietary ratio of standardized ileal digestible valine to lysine for eight to twenty-five kilograms of body weight pigs. J Anim Sci. 2009;87(8):2544–53. https://doi.org/10.2527/jas.2008-1221 .
doi: 10.2527/jas.2008-1221
pubmed: 19359510
van Milgen J, Gloaguen M, Le Floc’h N, Brossard L, Primot Y, Corrent E. Meta-analysis of the response of growing pigs to valine content of the diet. In: Oltjen JW, Kebreab E, Lapierre H, editors. Energy and protein metabolism and nutrition in sustainable animal production, vol 134. Wageningen: Wageningen Academic Publishers; 2013. https://doi.org/10.3920/978-90-8686-781-3_119 .
Lewis AJ, Nishimura N. Valine requirement of the finishing pig. J Anim Sci. 1995;73(8):2315–8. https://doi.org/10.2527/1995.7382315x .
doi: 10.2527/1995.7382315x
pubmed: 8567468
Xu Y, Zeng Z, Xu X, Tian Q, Ma X, Long S, et al. Effects of the standardized ileal digestible valine: lysine ratio on performance, milk composition and plasma indices of lactating sows. Anim Sci J. 2017;88(8):1082–92. https://doi.org/10.1111/asj.12753 .
doi: 10.1111/asj.12753
pubmed: 27921350
Rousselow DL, Speer VC. Valine requirement of the lactating sow. J Anim Sci. 1980;50(3):472–8. https://doi.org/10.2527/jas1980.503472x .
doi: 10.2527/jas1980.503472x
pubmed: 7364683
Roth-Maier DA, Ott H, Roth FX, Paulicks BR. Effects of the level of dietary valine supply on amino acids and urea concentration in milk and blood plasma of lactating sows. J Anim Physiol Anim Nutr. 2004;88(1–2):39–45. https://doi.org/10.1046/j.0931-2439.2003.00458.x .
Richert BT, Tokach MD, Goodband RD, Nelssen JL, Campbell RG, Kershaw S. The effect of dietary lysine and valine fed during lactation on sow and litter performance. J Anim Sci. 1997;75(7):1853–60. https://doi.org/10.2527/1997.7571853x .
doi: 10.2527/1997.7571853x
pubmed: 9222842
Richert BT, Tokach MD, Goodband RD, Nelssen JL, Pettigrew JE, Walker RD, et al. Valine requirement of the high-producing lactating sow. J Anim Sci. 1996;74(6):1307–13. https://doi.org/10.2527/1996.7461307x .
doi: 10.2527/1996.7461307x
pubmed: 8791203
Che L, Xu M, Gao K, Wang L, Yang X, Wen X, et al. Mammary tissue proteomics in a pig model indicates that dietary valine supplementation increases milk fat content via increased de novo synthesis of fatty acid. Food Sci Nutr. 2021;9(11):6213–23. https://doi.org/10.1002/fsn3.2574 .
doi: 10.1002/fsn3.2574
pubmed: 34760251
pmcid: 8565212
Clark AB, Tokach MD, DeRouchey JM, Dritz SS, Goodband RD, Woodworth JC, et al. Modeling the effects of standardized ileal digestible valine to lysine ratio on growth performance of nursery pigs. Transl Anim Sci. 2017;1(4):448–57. https://doi.org/10.2527/tas2017.0049 .
doi: 10.2527/tas2017.0049
pubmed: 32704668
pmcid: 7204984
Lordelo MM, Gaspar AM, Le Bellego L, Freire JP. Isoleucine and valine supplementation of a low-protein corn-wheat-soybean meal-based diet for piglets: growth performance and nitrogen balance. J Anim Sci. 2008;86(11):2936–41. https://doi.org/10.2527/jas.2007-0222 .
doi: 10.2527/jas.2007-0222
pubmed: 18567735
Sperringer JE, Addington A, Hutson SM. Branched-chain amino acids and brain metabolism. Neurochem Res. 2017;42(6):1697–709. https://doi.org/10.1007/s11064-017-2261-5 .
doi: 10.1007/s11064-017-2261-5
pubmed: 28417264
de Lima PP, Funchal C, Loureiro SO, Heimfarth L, Zamoner A, Gottfried C, et al. Branched-chain amino acids accumulating in maple syrup urine disease induce morphological alterations in C6 glioma cells probably through reactive species. Int J Dev Neurosci. 2007;25(3):181–9. https://doi.org/10.1016/j.ijdevneu.2007.01.001 .
doi: 10.1016/j.ijdevneu.2007.01.001
Chi R, Yao C, Chen S, Liu Y, He Y, Zhang J, et al. Elevated BCAA suppresses the development and metastasis of breast cancer. Front Oncol. 2022;12:887257. https://doi.org/10.3389/fonc.2022.887257 .
doi: 10.3389/fonc.2022.887257
pubmed: 35785192
pmcid: 9243538
Takpho N, Watanabe D, Takagi H. High-level production of valine by expression of the feedback inhibition-insensitive acetohydroxyacid synthase in Saccharomyces cerevisiae. Metab Eng. 2018;46:60–7. https://doi.org/10.1016/j.ymben.2018.02.011 .
doi: 10.1016/j.ymben.2018.02.011
pubmed: 29477860
Wang X, Zhang H, Quinn PJ. Production of L-valine from metabolically engineered Corynebacterium glutamicum. Appl Microbiol Biotechnol. 2018;102(10):4319–30. https://doi.org/10.1007/s00253-018-8952-2 .
doi: 10.1007/s00253-018-8952-2
pubmed: 29594358
Park JH, Jang YS, Lee JW, Lee SY. Escherichia coli W as a new platform strain for the enhanced production of L-valine by systems metabolic engineering. Biotechnol Bioeng. 2011;108(5):1140–7. https://doi.org/10.1002/bit.23044 .
Westbrook AW, Ren X, Moo-Young M, Chou CP. Metabolic engineering of Bacillus subtilis for L-valine overproduction. Biotechnol Bioeng. 2018;115(11):2778–92. https://doi.org/10.1002/bit.26789 .
doi: 10.1002/bit.26789
pubmed: 29981237
Liang C, Huo Y, Qi G, Wei X, Wang Q, Chen S. Enhancement of L-valine production in Bacillus licheniformis by blocking three branched pathways. Biotechnol Lett. 2015;37(6):1243–8. https://doi.org/10.1007/s10529-015-1783-7 .
doi: 10.1007/s10529-015-1783-7
pubmed: 25700818
Bampidis V, Azimonti G, de Lourdes Bastos M, Christensen H, Dusemund B, Fašmon Durjava M, et al. Safety and efficacy of a feed additive consisting of L-valine produced by Escherichia coli CCTCC M2020321 for all animal species (Kempex Holland BV). EFSA J. 2022;20(2):e07163. https://doi.org/10.2903/j.efsa.2022.7163 .
Bampidis V, Azimonti G, de Lourdes Bastos M, Christensen H, Dusemund B, Kos Durjava M, et al. Safety and efficacy of L-valine produced by fermentation using Escherichia coli KCCM 80159 for all animal species. EFSA J. 2020;18(4):e06074. https://doi.org/10.2903/j.efsa.2020.6074 .
Gao H, Tuyishime P, Zhang X, Yang T, Xu M, Rao Z. Engineering of microbial cells for L-valine production: challenges and opportunities. Microb Cell Fact. 2021;20(1):172. https://doi.org/10.1186/s12934-021-01665-5 .
doi: 10.1186/s12934-021-01665-5
pubmed: 34461907
pmcid: 8406616