Classification of essential amino acids for the weanling pig

Mertz, Edwin T.; Beeson, W. M.; Jackson, Henry

doi:10.1016/0003-9861(52)90015-5

Cited by 69 publications

(23 citation statements)

References 15 publications

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“…In pigs, His has been considered an essential AA for growth by Mertz et al (1952). However, there are indications that histidinol dehydrogenase, the enzyme that catalyzes the terminal step in the biosynthesis of His, is expressed in the liver and kidney but not in the muscle of pigs (Onodera, 2003).…”

Section: Gloaguen Le Floc'h Primot Corrent and Van Milgenmentioning

confidence: 99%

Response of piglets to the standardized ileal digestible isoleucine, histidine and leucine supply in cereal–soybean meal-based diets

Gloaguen

Floc'H

Primot³

et al. 2013

Animal

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Improving the amino acid (AA) profile of the diet by using L-Lys, L-Thr, DL-Met, L-Trp and L-Val helps to reduce the dietary CP content, thereby reducing nitrogen excretion while maintaining the performance of pigs. Valine is the fifth limiting AA in cereal-soybean meal-based diets. The extent to which the CP content in the diet can be reduced further without compromising performance depends on the requirement of the next limiting AA. In cereal-soybean meal-based diets, Ile, His and Leu may be the limiting AAs after Val, although information on the requirements for these AAs is scarce. Six experiments were conducted to determine the effect of supplementing a low-CP diet with L-Ile, L-His and L-Leu on the performance of pigs weighing 10 to 20 kg. Experiment 1 was designed to determine the most limiting AA with respect to performance among Ile, His and Leu. A diet 10% deficient in Ile, Leu and His relative to the National Research Council (NRC, 1998) requirement estimates tended to decrease daily feed intake and daily gain by 6% and 8%, respectively. A 10% deficiency in His alone had no effect, whereas a 10% deficiency in Ile or Leu slightly reduced daily feed intake and gain. In the remaining experiments, the standardized ileal digestible (SID) Ile : Lys, His : Lys and Leu : Lys requirements were estimated. In Experiments 2, 3, 4, 5 and 6, 14 blocks of six pigs each were assigned to six levels of SID Ile : Lys (40%, 43%, 46%, 49%, 52% and 55%), His : Lys (20%, 24%, 28%, 32%, 36% and 40%), His : Lys (21%, 24%, 27%, 30%, 33% and 36%), Leu : Lys (70%, 78%, 86%, 94%, 102% and 110%) and Leu : Lys (80%, 90%, 100%, 110%, 120% and 130%), respectively. Across experiments, the estimated SID Ile : Lys, His : Lys and Leu : Lys requirements for maximizing daily gain were 49%, 32% and 102%, respectively, using a curvilinear plateau model. When Ile, His and Leu levels were 10% below the requirement estimate, daily gain was reduced by 9%, 3% and 3%, respectively. The results of this study indicate that the Ile requirement estimate is lower than the current NRC requirement estimate, whereas the Leu and His requirements correspond to those proposed by the NRC.

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Section: Gloaguen Le Floc'h Primot Corrent and Van Milgenmentioning

confidence: 99%

Response of piglets to the standardized ileal digestible isoleucine, histidine and leucine supply in cereal–soybean meal-based diets

Gloaguen

Floc'H

Primot³

et al. 2013

Animal

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“…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. [14], but as an essential amino acid for young, growing mammals [15][16][17] and for carnivores [18,19].…”

Section: Introductionmentioning

confidence: 99%

Arginine metabolism: nitric oxide and beyond

Morris

1998

Biochemical Journal

2,425

2,036

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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

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“…In experimental animals, tryptophan deficiency can lead to a disturbance in growth [Willcock and Hopkins, 1906]. Tryptophan is required for the maintenance of nitrogen equilibrium in mature rats [Nasset and Ely, 1953], mice [Bauer and Berg, 1943], pigs [Mertz et al, 1952], and dogs [Rose and Rice, 1939]. Animals subjected to tryptophan deficiency can cause some maladies such as cataracts [Totter and Day, 1942;Ferraro and Roizin, 1947] and corneal vascularization [Sydenstricker et al, 1947].…”

Section: Introductionmentioning

confidence: 99%

Possible roles of excess tryptophan metabolites in cancer

Chung

Gadupudi

2011

Environ and Mol Mutagen

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Tryptophan is metabolized through serotonin, indole, and kynurenine (KN) pathways. Uptake of an excess amount of tryptophan accompanied with vitamin B6 deficiency may result in the accumulation of higher concentrations of metabolites mainly from the KN pathways in the bladder. These metabolites could interact with nitrite to become mutagenic nitrosamines. They could be a promoter in the initiator-promoter model of carcinogenesis. They produced bladder cancer when implanted in the bladder. They also interact with transition metals copper or iron to form reactive radicals or reactive oxygen species (ROS). Some metabolites, 3-hydroxy-anthranilic acid, were autooxidized to mutagenic cinnabarinic and anthranilyl radical intermediates. These radical intermediates could also be ligands that interact with aryl hydrocarbon receptor (AhR) and induce xenobiotic metabolizing enzymes (XMEs) to metabolize contaminated carcinogens. When tryptophan is exposed to either visible or UV light, a photoproduct of 6-formylindolo[3,2b]-carbazole is formed, which has a very high affinity for the AhR that plays a role in carcinogenesis. This review gives an insight into various mechanisms through which tryptophan metabolites cause carcinogenesis. It could be concluded that tryptophan metabolites play a complementary role in promoting carcinogenesis along with carcinogens like aflatoxin, CCl(4) , 2-acetylaminofluorene, 4-aminobiphenyl, 2-naphthylamine, or N-[4-(5-nitro-2-furyl)-2-thiazolyl] formamide. The underlying mechanisms could be their autoxidation, exposure to either visible or UV light, interaction with nitrite or transition metals to form reactive intermediates, serving as ligands to interact with an AhR that is known to play a role in carcinogenesis through induction of XMEs. Further research is warranted.Environ.

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Classification of essential amino acids for the weanling pig

Cited by 69 publications

References 15 publications

Response of piglets to the standardized ileal digestible isoleucine, histidine and leucine supply in cereal–soybean meal-based diets

Response of piglets to the standardized ileal digestible isoleucine, histidine and leucine supply in cereal–soybean meal-based diets

Arginine metabolism: nitric oxide and beyond

Possible roles of excess tryptophan metabolites in cancer

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