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      Amino acid nutrition and metabolism in domestic cats and dogs

      review-article
      1 , 2 ,
      Journal of Animal Science and Biotechnology
      BioMed Central
      Animal-sourced foodstuffs, Cats, Dogs, Health, Metabolism, Nutrition

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          Abstract

          Domestic cats and dogs are carnivores that have evolved differentially in the nutrition and metabolism of amino acids. This article highlights both proteinogenic and nonproteinogenic amino acids. Dogs inadequately synthesize citrulline (the precursor of arginine) from glutamine, glutamate, and proline in the small intestine. Although most breeds of dogs have potential for adequately converting cysteine into taurine in the liver, a small proportion (1.3%–2.5%) of the Newfoundland dogs fed commercially available balanced diets exhibit a deficiency of taurine possibly due to gene mutations. Certain breeds of dogs (e.g., golden retrievers) are more prone to taurine deficiency possibly due to lower hepatic activities of cysteine dioxygenase and cysteine sulfinate decarboxylase. De novo synthesis of arginine and taurine is very limited in cats. Thus, concentrations of both taurine and arginine in feline milk are the greatest among domestic mammals. Compared with dogs, cats have greater endogenous nitrogen losses and higher dietary requirements for many amino acids (e.g., arginine, taurine, cysteine, and tyrosine), and are less sensitive to amino acid imbalances and antagonisms. Throughout adulthood, cats and dogs may lose 34% and 21% of their lean body mass, respectively. Adequate intakes of high-quality protein (i.e., 32% and 40% animal protein in diets of aging dogs and cats, respectively; dry matter basis) are recommended to alleviate aging-associated reductions in the mass and function of skeletal muscles and bones. Pet-food grade animal-sourced foodstuffs are excellent sources of both proteinogenic amino acids and taurine for cats and dogs, and can help to optimize their growth, development, and health.

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          Most cited references150

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          Canine SARS-CoV-2 infection

          SARS-CoV-2 emerged in Wuhan in December 2019 and caused the pandemic respiratory disease, COVID-19. 1,2 In 2003, the closely related SARS-CoV had been detected in domestic cats and a dog. 3 However, little is known about the susceptibility of domestic pet mammals to SARS-CoV-2. Two of 15 dogs from households with confirmed human cases of COVID-19 in Hong Kong SAR were found to be infected using quantitative RT-PCR, serology, sequencing the viral genome, and in one dog, virus isolation. SARS-CoV-2 RNA was detected in a 17 year-old neutered male Pomeranian from five nasal swabs collected over a 13 day period. A 2.5 yo male German Shepherd dog had SARS CoV-2 RNA on two occasions and virus was isolated from nasal and oral swabs. Both dogs had antibody responses detected using plaque reduction neutralisation assays. Viral genetic sequences of viruses from the two dogs were identical to the virus detected in the respective human cases. The animals remained asymptomatic during quarantine. The evidence suggests that these are instances of human-to-animal transmission of SARS-CoV-2. It is unclear whether infected dogs can transmit the virus to other animals or back to humans.
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            Arginine metabolism: nitric oxide and beyond.

            Arginine is one of the most versatile amino acids in animal cells, serving as a precursor for the synthesis not only of proteins but also of nitric oxide, urea, polyamines, proline, glutamate, creatine and agmatine. Of the enzymes that catalyse rate-controlling steps in arginine synthesis and catabolism, argininosuccinate synthase, the two arginase isoenzymes, the three nitric oxide synthase isoenzymes and arginine decarboxylase have been recognized in recent years as key factors in regulating newly identified aspects of arginine metabolism. In particular, changes in the activities of argininosuccinate synthase, the arginases, the inducible isoenzyme of nitric oxide synthase and also cationic amino acid transporters play major roles in determining the metabolic fates of arginine in health and disease, and recent studies have identified complex patterns of interaction among these enzymes. There is growing interest in the potential roles of the arginase isoenzymes as regulators of the synthesis of nitric oxide, polyamines, proline and glutamate. Physiological roles and relationships between the pathways of arginine synthesis and catabolism in vivo are complex and difficult to analyse, owing to compartmentalized expression of various enzymes at both organ (e.g. liver, small intestine and kidney) and subcellular (cytosol and mitochondria) levels, as well as to changes in expression during development and in response to diet, hormones and cytokines. The ongoing development of new cell lines and animal models using cDNA clones and genes for key arginine metabolic enzymes will provide new approaches more clearly elucidating the physiological roles of these enzymes.
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              Regulation of glutaminase activity and glutamine metabolism.

              Glutamine is synthesized primarily in skeletal muscle, lungs, and adipose tissue. Plasma glutamine plays an important role as a carrier of nitrogen, carbon, and energy between organs and is used for hepatic urea synthesis, for renal ammoniagenesis, for gluconeogenesis in both liver and kidney, and as a major respiratory fuel for many cells. The catabolism of glutamine is initiated by either of two isoforms of the mitochondrial glutaminase. Liver-type glutaminase is expressed only in periportal hepatocytes of the postnatal liver, where it effectively couples ammonia production with urea synthesis. Kidney-type glutaminase is abundant in kidney, brain, intestine, fetal liver, lymphocytes, and transformed cells, where the resulting ammonia is released without further metabolism. The two isoenzymes have different structural and kinetic properties that contribute to their function and short-term regulation. Although there is a high degree of identity in amino acid sequences, the two glutaminases are the products of different but related genes. The two isoenzymes are also subject to long-term regulation. Hepatic glutaminase is increased during starvation, diabetes, and feeding a high-protein diet, whereas kidney-type glutaminase is increased only in kidney in response to metabolic acidosis. The adaptations in hepatic glutaminase are mediated by changes in the rate of transcription, whereas kidney-type glutaminase is regulated at a posttranscriptional level.
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                Author and article information

                Contributors
                hi-peng@hotmail.com
                g-wu@tamu.edu
                Journal
                J Anim Sci Biotechnol
                J Anim Sci Biotechnol
                Journal of Animal Science and Biotechnology
                BioMed Central (London )
                1674-9782
                2049-1891
                21 February 2023
                21 February 2023
                2023
                : 14
                : 19
                Affiliations
                [1 ]GRID grid.508113.e, North American Renderers Association, ; Alexandria, Virginia 22314 USA
                [2 ]GRID grid.264756.4, ISNI 0000 0004 4687 2082, Department of Animal Science, , Texas A&M University, ; College Station, TX 77843 USA
                Author information
                http://orcid.org/0000-0001-8058-6969
                Article
                827
                10.1186/s40104-022-00827-8
                9942351
                36803865
                3cecae11-0a58-4776-bd79-2b707d39817e
                © The Author(s) 2023

                Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/. The Creative Commons Public Domain Dedication waiver ( http://creativecommons.org/publicdomain/zero/1.0/) applies to the data made available in this article, unless otherwise stated in a credit line to the data.

                History
                : 8 October 2022
                : 21 December 2022
                Categories
                Review
                Custom metadata
                © The Author(s) 2023

                Animal science & Zoology
                animal-sourced foodstuffs,cats,dogs,health,metabolism,nutrition
                Animal science & Zoology
                animal-sourced foodstuffs, cats, dogs, health, metabolism, nutrition

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