Amino acids in nutrition, health, and disease

Wu, Guoyao

doi:10.52586/5032

Cited by 19 publications

(16 citation statements)

References 75 publications

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“…Te most abundant components of nonessential amino acid were glutamate (4.39%), then the second nonessential amino acid was glycine (4.31%). Many previous papers illustrated that the amino acid, such as Arg, Glu, Gly, and Pro, which plays a key role in regulating gene expression, cell signaling, blood fow, nutrient transport, antioxidative, and immune responses [21,22]. In addition, Glu also helps to secrete gastric juice and maintain blood glucose levels [22].…”

Section: Resultsmentioning

confidence: 99%

Ultrasound-Assisted Enzymatic Extraction and Bioactivity Analysis of Polypeptides from Cordyceps militaris

Guo

et al. 2023

Journal of Chemistry

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Cordyceps militaris is rich in protein, polysaccharide, cordycepin, and other active components, with anticancer and antioxidation functions. In order to improve the economic value of C. militaris, the protein was extracted from its fruiting body by alkali-soluble acid precipitation process, and the extraction technology was optimized by orthogonal test. The polypeptide was obtained by digesting those proteins with a complex enzyme. And the antimicrobial and anticancer activities of those polypeptides were evaluated by measuring inhibitory zone and cytotoxicity. The results showed that the optimal extraction conditions of protein were as follows: pH of 8.5, material-to-water ratio of 1 : 28, extraction time of 3.5 h, extraction three times, and the highest protein yield was 45.06%. The optimum enzymatic hydrolysis process of C. militaris polypeptide solution was as follows: the ratio of alkaline protease to papain was 4 : 3, the optimum temperature was 55°C, pH was 7.2, the enzyme dosage was 7000 U/mL, the enzymolysis time was 3.5 h, and the highest yield of peptide was 16.73%. Under those conditions, the polypeptides prepared from C. militaris (<3000 Da) showed good antibacterial activity against Escherichia coli, Bacillus subtilis, and Staphylococcus aureus, with inhibitory zones of (12.08 ± 0.22), (6.67 ± 0.12), and (10.32 ± 0.23) mm, respectively. The results showed that the SAO-S (IC50 = 0.49 mg/L) and T24 (IC50 = 0.23 mg/L) were significantly inhibited by C. militaris polypeptide. Results from this study suggest that polypeptides can be utilized as a new approach for bioactive compounds production from C. militaris.

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Section: Resultsmentioning

confidence: 99%

Ultrasound-Assisted Enzymatic Extraction and Bioactivity Analysis of Polypeptides from Cordyceps militaris

Guo

et al. 2023

Journal of Chemistry

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“…mTORC1 activation can be induced by amino acids, such as arginine, glutamine, and leucine, accompanied by the dynamic lysosomal localization of the mTOR and TSC complexes. Amino acids regulate mRNA translation via an mTOR-dependent pathway [ 76 , 77 ]. Here, we investigated the mechanism by which amino acids activated downstream signaling pathways to promote FMDV replication.…”

Section: Discussionmentioning

confidence: 99%

Picornavirus infection enhances aspartate by the SLC38A8 transporter to promote viral replication

et al. 2023

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Foot-and-mouth disease, a class of animal diseases, is caused by foot-and-mouth disease virus (FMDV). The metabolic changes during FMDV infection remain unclear. Here, PK-15 cells, serum, and tonsils infected with FMDV were analyzed by metabolomics. A total of 284 metabolites in cells were significantly changed after FMDV infection, and most of them belong to amino acids and nucleotides. Further studies showed that FMDV infection significantly enhanced aspartate in vitro and in vivo. The amino acid transporter solute carrier family 38 member 8 (SLC38A8) was responsible for FMDV-upregulated aspartate. Enterovirus 71 (EV71) and Seneca Valley virus (SVV) infection also enhanced aspartate by SLC38A8. Aspartate aminotransferase activity was also elevated in FMDV-, EV71-, and SVV-infected cells, which may lead to reversible transition between the TCA cycle and amino acids synthesis. Aspartate and SLC38A8 were essential for FMDV, EV71, and SVV replication in cells. In addition, aspartate and SLC38A8 also promoted FMDV and EV71 replication in mice. Detailed analysis indicated that FMDV infection promoted the transfer of mTOR to lysosome to enhance interaction between mTOR and Rheb, and activated PI3K/AKT/TSC2/Rheb/mTOR/p70S6K1 pathway to promote viral replication. The mTORC1 signaling pathway was responsible for FMDV-induced SLC38A8 protein expression. For the first time, our data identified metabolic changes during FMDV infection. These data identified a novel mechanism used by FMDV to upregulate aspartate to promote viral replication and will provide new perspectives for developing new preventive strategies.

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“…Adequate knowledge of AA metabolism and nutrition is necessary to meet the needs of animals for dietary AAs. 81…”

Section: Optimal Ratios and Amounts Of All Proteinogenic Aas In Diets...mentioning

confidence: 99%

“…Adequate knowledge of AA metabolism and nutrition is necessary to meet the needs of animals for dietary AAs. 81 Our guiding principles for the development of new optimal patterns of all AAs in diets for swine and chickens at a production stage are (1) endogenous syntheses of AASAs from EAAs are inadequate in highly productive animals, (2) EAAs and AASAs are needed in optimal proportions and amounts for maximum productivity and optimum health, (3) dietary AAs are metabolized at different rates in the small intestine of animals, and (4) dietary requirements of animals for AAs depend on tissue-specific protein turnover and AA metabolism. Since 1992, extensive research has been conducted to improve AA patterns in diets for gestating, lactating, suckling, weanling, and finishing swine through both basic research on AA metabolism and dietary supplementation with functional AAs (including arginine, glutamine, glutamate, proline, or glycine).…”

Section: Optimal Ratios and Amounts Of All Proteinogenic Aas In Diets...mentioning

confidence: 99%

The “ideal protein” concept is not ideal in animal nutrition

2022

Exp Biol Med (Maywood)

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Amino acids (AAs) are required for syntheses of proteins and low-molecular-weight substances with enormous physiological importance. Since 1912, AAs have been classified as nutritionally essential amino acids (EAAs) or nonessential amino acids (NEAAs) for animals. EAAs are those AAs that are either not synthesized or insufficiently synthesized de novo in the organisms. It was assumed that all NEAAs (now known as AAs that are synthesizable in animal cells de novo [AASAs]) were formed sufficiently in animals and were not needed in diets. However, studies over the past three decades have shown that sufficient dietary AASAs (e.g. glutamine, glutamate, glycine, and proline) are necessary for the maximum growth and optimum health of pigs, chickens, and fish. Thus, the concept of “ideal protein” (protein with an optimal EAA pattern that precisely meets the physiological needs of animals), which was originally proposed in the 1950s but ignored AASAs, is not ideal in animal nutrition. Ideal diets must provide all physiologically and nutritionally essential AAs. Improved patterns of AAs in diets for swine and chickens as well as zoo and companion animals have been proposed in recent years. Animal-sourced feedstuffs supply abundant EAAs and AASAs (including glutamate, glutamine, glycine, proline, 4-hydroxyproline, and taurine) for diets of swine, poultry, fish, and crustaceans to improve their growth, development, reproduction, and health, while sustaining global animal production. Nutritionists should move beyond the “ideal protein” concept to consider optimum ratios and amounts of all proteinogenic AAs in diets for mammals, birds, and aquatic animals, and, in the case of carnivores, also taurine.

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Amino acids in nutrition, health, and disease

Cited by 19 publications

References 75 publications

Ultrasound-Assisted Enzymatic Extraction and Bioactivity Analysis of Polypeptides from Cordyceps militaris

Ultrasound-Assisted Enzymatic Extraction and Bioactivity Analysis of Polypeptides from Cordyceps militaris

Picornavirus infection enhances aspartate by the SLC38A8 transporter to promote viral replication

The “ideal protein” concept is not ideal in animal nutrition

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