![]() ![]() ![]() Champaign, ILīacklund B, Zoran DL, Nabity MB, Norby B, Bauer JE (2011) Effects of dietary protein content on renal parameters in normal cats. Champaign, ILĪssociation of American Feed Control Officials (AAFCO) (2014) AAFCO methods for substantiating nutritional adequacy of dog and cat foods. Diabetes 51:928–936Īssociation of American Feed Control Officials (AAFCO) (2007) Official publication of AAFCO. Nutr Rev 33:180–182Īnthony JC, Reiter AK, Anthony TG, Crozier SJ, Lang CH, MacLean DA, Kimball SR, Jefferson LS (2002) Orally administered leucine enhances protein synthesis in skeletal muscle of diabetic rats in the absence of increases in 4E-BP1 or S6K1 phosphorylation. J Nutr 132:2037–2042Īnonymous (1975) Adaptation to low protein intakes. Chem Rev 118:1216–1252Īnderson PJ, Rogers QR, Morris JG (2002) Cats require more dietary phenylalanine or tyrosine for melanin deposition in hair than for maximal growth. J Feline Med Surg 16:749–756Īli I, Conrad RJ, Verdin E, Ott M (2018) Lysine acetylation goes global: from epigenetics to metabolism and therapeutics. KeywordsĪgnew W, Korman R (2014) Pharmacological appetite stimulation: rational choices in the inappetent cat. Meeting dietary requirements for both EAAs and NEAAs in proper amounts and balances is crucial for improving the health, wellbeing, longevity, and reproduction of cats. Besides meat, animal-source foodstuffs (including ruminant meat & bone meal, poultry by-product meal, porcine mucosal protein, and chicken visceral digest) are good sources of proteinogenic AAs and taurine for cats. Plant-source foodstuffs lack taurine and generally contain inadequate Met and Cys and, therefore, should not be fed to cats in any age group. Except for Gln, AAs in the arterial blood of cats may not be available to the mucosa of the small intestine. Some of these AAs (e.g., Gln, Glu, Pro, and Gly) are crucial for intestinal integrity and health. Cats can synthesize de novo eight proteinogenic AAs: Ala, Asn, Asp, Gln, Glu, Gly, Pro, and Ser, as well as some nonproteinogenic AAs, such as γ-aminobutyrate, ornithine, and β-alanine with important physiological functions. ![]() National Academies Press, Washington, DC, 2006) does not recommend dietary requirements of cats for NEAAs, much attention should be directed to this critical issue of nutrition. Although the National Research Council (NCR, Nutrient requirements of dogs and cats. These animals are sensitive to dietary deficiencies of Arg and taurine, which rapidly result in life-threatening hyperammonemia and retinal damage, respectively. All the EAAs (including taurine) must be provided in diets for cats. Except for Leu and Lys that are strictly ketogenic AAs, most EAAs are both glucogenic and ketogenic AAs. Like other feline carnivores but unlike many mammals, cats do not synthesize citrulline and have a very limited ability to produce taurine from Cys. Like other mammals, cats do not synthesize the carbon skeletons of twelve proteinogenic AAs: Arg, Cys, His, Ile, Leu, Lys, Met, Phe, Thr, Trp, Tyr, and Val. This review will focus on AA nutrition and metabolism in cats. Amino acids had been traditionally categorised as nutritionally essential (EAAs) or nonessential (NEAAs), depending on whether they are synthesized de novo in the body. Domestic cats (carnivores) require high amounts of dietary amino acids (AAs) for normal growth, development, and reproduction. ![]()
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