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The Role of Meat Protein in Generation of Oxidative Stress and Pathophysiology of Metabolic Syndromes.

Food science of animal resources

Ahmad MI, Ijaz MU, Haq IU, Li C.
PMID: 31970326
Food Sci Anim Resour. 2020 Jan;40(1):1-10. doi: 10.5851/kosfa.2019.e96. Epub 2020 Jan 01.

Various processing methods have a great impact on the physiochemical and nutritional properties of meat that are of health concern. Hence, the postmortem processing of meat by different methods is likely to intensify the potential effects on protein oxidation....

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Ahmad MI, Ijaz MU, Haq IU, et al. The Role of Meat Protein in Generation of Oxidative Stress and Pathophysiology of Metabolic Syndromes. Food Sci Anim Resour. 2020;40(1):1-10doi: 10.5851/kosfa.2019.e96.
Ahmad, M. I., Ijaz, M. U., Haq, I. U., & Li, C. (2020). The Role of Meat Protein in Generation of Oxidative Stress and Pathophysiology of Metabolic Syndromes. Food science of animal resources, 40(1), 1-10. https://doi.org/10.5851/kosfa.2019.e96
Ahmad, Muhammad Ijaz, et al. "The Role of Meat Protein in Generation of Oxidative Stress and Pathophysiology of Metabolic Syndromes." Food science of animal resources vol. 40,1 (2020): 1-10. doi: https://doi.org/10.5851/kosfa.2019.e96
Ahmad MI, Ijaz MU, Haq IU, Li C. The Role of Meat Protein in Generation of Oxidative Stress and Pathophysiology of Metabolic Syndromes. Food Sci Anim Resour. 2020 Jan;40(1):1-10. doi: 10.5851/kosfa.2019.e96. Epub 2020 Jan 01. PMID: 31970326; PMCID: PMC6957445.
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Correction to: Dietary Proteins Alter Fermentation Characteristics of Human Gut Microbiota In Vitro.

Plant foods for human nutrition (Dordrecht, Netherlands)

Xiao T, Liang T, Geng DH, Wang L, Liu L, Zhou X, Pu H, Huang J, Zhou S, Tong LT.
PMID: 34826021
Plant Foods Hum Nutr. 2021 Nov 26; doi: 10.1007/s11130-021-00940-5. Epub 2021 Nov 26.

No abstract available.

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Xiao T, Liang T, Geng DH, et al. Correction to: Dietary Proteins Alter Fermentation Characteristics of Human Gut Microbiota In Vitro. Plant Foods Hum Nutr. 2021;doi: 10.1007/s11130-021-00940-5.
Xiao, T., Liang, T., Geng, D. H., Wang, L., Liu, L., Zhou, X., Pu, H., Huang, J., Zhou, S., & Tong, L. T. (2021). Correction to: Dietary Proteins Alter Fermentation Characteristics of Human Gut Microbiota In Vitro. Plant foods for human nutrition (Dordrecht, Netherlands), . https://doi.org/10.1007/s11130-021-00940-5
Xiao, Tianzhen, et al. "Correction to: Dietary Proteins Alter Fermentation Characteristics of Human Gut Microbiota In Vitro." Plant foods for human nutrition (Dordrecht, Netherlands) vol. (2021). doi: https://doi.org/10.1007/s11130-021-00940-5
Xiao T, Liang T, Geng DH, Wang L, Liu L, Zhou X, Pu H, Huang J, Zhou S, Tong LT. Correction to: Dietary Proteins Alter Fermentation Characteristics of Human Gut Microbiota In Vitro. Plant Foods Hum Nutr. 2021 Nov 26; doi: 10.1007/s11130-021-00940-5. Epub 2021 Nov 26. PMID: 34826021.
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Detection of IgE, IgG, IgA and IgM antibodies against raw and processed food antigens.

Nutrition & metabolism

Vojdani A.
PMID: 19435515
Nutr Metab (Lond). 2009 May 12;6:22. doi: 10.1186/1743-7075-6-22.

BACKGROUND: Despite the first documented case of food allergy to cooked food in 1921 by Prausnitz and Kustner, all commercial food antigens are prepared from raw food. Furthermore, all IgE and IgG antibodies against dietary proteins offered by many...

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Vojdani A. Detection of IgE, IgG, IgA and IgM antibodies against raw and processed food antigens. Nutr Metab (Lond). 2009;6:22doi: 10.1186/1743-7075-6-22.
Vojdani, A. (2009). Detection of IgE, IgG, IgA and IgM antibodies against raw and processed food antigens. Nutrition & metabolism, 622. https://doi.org/10.1186/1743-7075-6-22
Vojdani, Aristo. "Detection of IgE, IgG, IgA and IgM antibodies against raw and processed food antigens." Nutrition & metabolism vol. 6 (2009): 22. doi: https://doi.org/10.1186/1743-7075-6-22
Vojdani A. Detection of IgE, IgG, IgA and IgM antibodies against raw and processed food antigens. Nutr Metab (Lond). 2009 May 12;6:22. doi: 10.1186/1743-7075-6-22. PMID: 19435515; PMCID: PMC2685801.
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Increased mucin-degrading bacteria by high protein diet leads to thinner mucus layer and aggravates experimental colitis.

Journal of gastroenterology and hepatology

Chen L, Wang J, Yi J, Liu Y, Yu Z, Chen S, Liu X.
PMID: 34050560
J Gastroenterol Hepatol. 2021 Oct;36(10):2864-2874. doi: 10.1111/jgh.15562. Epub 2021 Jun 16.

BACKGROUND AND AIM: Westernized high-fat diet increases the risk for inflammatory bowel diseases (IBDs), yet with insufficient understanding of the role of high-protein diet. We aimed to identify the effect of high-protein diets from different dietary proteins (casein, whey...

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Chen L, Wang J, Yi J, et al. Increased mucin-degrading bacteria by high protein diet leads to thinner mucus layer and aggravates experimental colitis. J Gastroenterol Hepatol. 2021;36(10):2864-2874doi: 10.1111/jgh.15562.
Chen, L., Wang, J., Yi, J., Liu, Y., Yu, Z., Chen, S., & Liu, X. (2021). Increased mucin-degrading bacteria by high protein diet leads to thinner mucus layer and aggravates experimental colitis. Journal of gastroenterology and hepatology, 36(10), 2864-2874. https://doi.org/10.1111/jgh.15562
Chen, Lulu, et al. "Increased mucin-degrading bacteria by high protein diet leads to thinner mucus layer and aggravates experimental colitis." Journal of gastroenterology and hepatology vol. 36,10 (2021): 2864-2874. doi: https://doi.org/10.1111/jgh.15562
Chen L, Wang J, Yi J, Liu Y, Yu Z, Chen S, Liu X. Increased mucin-degrading bacteria by high protein diet leads to thinner mucus layer and aggravates experimental colitis. J Gastroenterol Hepatol. 2021 Oct;36(10):2864-2874. doi: 10.1111/jgh.15562. Epub 2021 Jun 16. PMID: 34050560.
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Microalgae as Sources of High-Quality Protein for Human Food and Protein Supplements.

Foods (Basel, Switzerland)

Wang Y, Tibbetts SM, McGinn PJ.
PMID: 34945551
Foods. 2021 Dec 04;10(12). doi: 10.3390/foods10123002.

As a result of population growth, an emerging middle-class, and a more health-conscious society concerned with overconsumption of fats and carbohydrates, dietary protein intake is on the rise. To address this rapid change in the food market, and the...

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Wang Y, Tibbetts SM, McGinn PJ. Microalgae as Sources of High-Quality Protein for Human Food and Protein Supplements. Foods. 2021;10(12)doi: 10.3390/foods10123002.
Wang, Y., Tibbetts, S. M., & McGinn, P. J. (2021). Microalgae as Sources of High-Quality Protein for Human Food and Protein Supplements. Foods (Basel, Switzerland), 10(12), . https://doi.org/10.3390/foods10123002
Wang, Yanwen, et al. "Microalgae as Sources of High-Quality Protein for Human Food and Protein Supplements." Foods (Basel, Switzerland) vol. 10,12 (2021). doi: https://doi.org/10.3390/foods10123002
Wang Y, Tibbetts SM, McGinn PJ. Microalgae as Sources of High-Quality Protein for Human Food and Protein Supplements. Foods. 2021 Dec 04;10(12). doi: 10.3390/foods10123002. PMID: 34945551.
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Rare food allergens.

Allergologie select

Hoffmann-Sommergruber K.
PMID: 33465170
Allergol Select. 2021 Jan 12;5:29-32. doi: 10.5414/ALX02135E. eCollection 2021.

In food allergy, only a restricted number of protein families have been identified to contain allergenic proteins. These can be further grouped into major allergens, responsible for inducing allergic reactions in the majority of patients allergic to the food...

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Hoffmann-Sommergruber K. Rare food allergens. Allergol Select. 2021;5:29-32doi: 10.5414/ALX02135E.
Hoffmann-Sommergruber, K. (2021). Rare food allergens. Allergologie select, 529-32. https://doi.org/10.5414/ALX02135E
Hoffmann-Sommergruber, Karin. "Rare food allergens." Allergologie select vol. 5 (2021): 29-32. doi: https://doi.org/10.5414/ALX02135E
Hoffmann-Sommergruber K. Rare food allergens. Allergol Select. 2021 Jan 12;5:29-32. doi: 10.5414/ALX02135E. eCollection 2021. PMID: 33465170; PMCID: PMC7807251.
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The Reproduction Rate of Peptide Transporter PEPT-1 Deficient .

Frontiers in molecular biosciences

Spanier B, Wallwitz J, Zapoglou D, Idrissou BMG, Fischer C, Troll M, Petzold K, Daniel H.
PMID: 30560135
Front Mol Biosci. 2018 Nov 30;5:109. doi: 10.3389/fmolb.2018.00109. eCollection 2018.

Intestinal absorption of dietary amino acids is mediated via two routes. Free amino acids released by hydrolysis of dietary proteins are taken up by a multitude of amino acid transporters while di- and tripeptides released are taken up by...

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Spanier B, Wallwitz J, Zapoglou D, et al. The Reproduction Rate of Peptide Transporter PEPT-1 Deficient . Front Mol Biosci. 2018;5:109doi: 10.3389/fmolb.2018.00109.
Spanier, B., Wallwitz, J., Zapoglou, D., Idrissou, B. M. G., Fischer, C., Troll, M., Petzold, K., & Daniel, H. (2018). The Reproduction Rate of Peptide Transporter PEPT-1 Deficient . Frontiers in molecular biosciences, 5109. https://doi.org/10.3389/fmolb.2018.00109
Spanier, Britta, et al. "The Reproduction Rate of Peptide Transporter PEPT-1 Deficient ." Frontiers in molecular biosciences vol. 5 (2018): 109. doi: https://doi.org/10.3389/fmolb.2018.00109
Spanier B, Wallwitz J, Zapoglou D, Idrissou BMG, Fischer C, Troll M, Petzold K, Daniel H. The Reproduction Rate of Peptide Transporter PEPT-1 Deficient . Front Mol Biosci. 2018 Nov 30;5:109. doi: 10.3389/fmolb.2018.00109. eCollection 2018. PMID: 30560135; PMCID: PMC6284198.
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Egg White Protein Promotes Developmental Growth in Rodent Muscle Independent of the Leucine Content.

The Journal of nutrition

Kido K, Koshinaka K, Iizawa H, Honda H, Hirota A, Nakamura T, Arikawa M, Ra SG, Kawanaka K.
PMID: 34610138
J Nutr. 2021 Oct 05; doi: 10.1093/jn/nxab353. Epub 2021 Oct 05.

BACKGROUND: Leucine has unique anabolic properties, serving as a nutrient signal that stimulates muscle protein synthesis.OBJECTIVE: We tested whether the leucine concentration is the only factor determining protein quality for muscle development.METHODS: We selected three dietary proteins: casein (CAS),...

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Kido K, Koshinaka K, Iizawa H, et al. Egg White Protein Promotes Developmental Growth in Rodent Muscle Independent of the Leucine Content. J Nutr. 2021;doi: 10.1093/jn/nxab353.
Kido, K., Koshinaka, K., Iizawa, H., Honda, H., Hirota, A., Nakamura, T., Arikawa, M., Ra, S. G., & Kawanaka, K. (2021). Egg White Protein Promotes Developmental Growth in Rodent Muscle Independent of the Leucine Content. The Journal of nutrition, . https://doi.org/10.1093/jn/nxab353
Kido, Kohei, et al. "Egg White Protein Promotes Developmental Growth in Rodent Muscle Independent of the Leucine Content." The Journal of nutrition vol. (2021). doi: https://doi.org/10.1093/jn/nxab353
Kido K, Koshinaka K, Iizawa H, Honda H, Hirota A, Nakamura T, Arikawa M, Ra SG, Kawanaka K. Egg White Protein Promotes Developmental Growth in Rodent Muscle Independent of the Leucine Content. J Nutr. 2021 Oct 05; doi: 10.1093/jn/nxab353. Epub 2021 Oct 05. PMID: 34610138.
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Poor Dietary Protein Intake in Elderly Population with Sarcopenia and Osteosarcopenia: A Nationwide Population-Based Study.

Journal of bone metabolism

Yoo JI, Lee KH, Choi Y, Lee J, Park YG.
PMID: 33317233
J Bone Metab. 2020 Nov;27(4):301-310. doi: 10.11005/jbm.2020.27.4.301. Epub 2020 Nov 30.

BACKGROUND: Our purpose in this study was to evaluate any deficiency of protein intake for different types of sarcopenia, including osteosarcopenia and sarcopenic obesity and to establish a cut-off value for the relationship between malnutrition, sarcopenia, and osteosarcopenia.METHODS: The...

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Yoo JI, Lee KH, Choi Y, et al. Poor Dietary Protein Intake in Elderly Population with Sarcopenia and Osteosarcopenia: A Nationwide Population-Based Study. J Bone Metab. 2020;27(4):301-310doi: 10.11005/jbm.2020.27.4.301.
Yoo, J. I., Lee, K. H., Choi, Y., Lee, J., & Park, Y. G. (2020). Poor Dietary Protein Intake in Elderly Population with Sarcopenia and Osteosarcopenia: A Nationwide Population-Based Study. Journal of bone metabolism, 27(4), 301-310. https://doi.org/10.11005/jbm.2020.27.4.301
Yoo, Jun-Il, et al. "Poor Dietary Protein Intake in Elderly Population with Sarcopenia and Osteosarcopenia: A Nationwide Population-Based Study." Journal of bone metabolism vol. 27,4 (2020): 301-310. doi: https://doi.org/10.11005/jbm.2020.27.4.301
Yoo JI, Lee KH, Choi Y, Lee J, Park YG. Poor Dietary Protein Intake in Elderly Population with Sarcopenia and Osteosarcopenia: A Nationwide Population-Based Study. J Bone Metab. 2020 Nov;27(4):301-310. doi: 10.11005/jbm.2020.27.4.301. Epub 2020 Nov 30. PMID: 33317233; PMCID: PMC7746483.
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Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas.

The American journal of surgical pathology

Uhlig R, Contreras H, Weidemann S, Gorbokon N, Menz A, Büscheck F, Luebke AM, Kluth M, Hube-Magg C, Hinsch A, Höflmayer D, Fraune C, Möller K, Bernreuther C, Lebok P, Sauter G, Wilczak W, Izbicki J, Perez D, Schrader J, Steurer S, Burandt E, Krech R, Dum D, Krech T, Marx A, Simon R, Minner S, Jacobsen F, Clauditz TS.
PMID: 34889867
Am J Surg Pathol. 2022 Jan 01;46(1):97-104. doi: 10.1097/PAS.0000000000001817.

Carboxypeptidase A1 (CPA1) is a zinc metalloprotease that is produced in pancreatic acinar cells and plays a role in cleaving C-terminal branched-chain and aromatic amino acids from dietary proteins. This study assessed the utility of immunohistochemical CPA1 staining for...

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Uhlig R, Contreras H, Weidemann S, et al. Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas. Am J Surg Pathol. 2022;46(1):97-104doi: 10.1097/PAS.0000000000001817.
Uhlig, R., Contreras, H., Weidemann, S., Gorbokon, N., Menz, A., Büscheck, F., Luebke, A. M., Kluth, M., Hube-Magg, C., Hinsch, A., Höflmayer, D., Fraune, C., Möller, K., Bernreuther, C., Lebok, P., Sauter, G., Wilczak, W., Izbicki, J., Perez, D., Schrader, J., Steurer, S., Burandt, E., Krech, R., Dum, D., Krech, T., Marx, A., Simon, R., Minner, S., Jacobsen, F., & Clauditz, T. S. (2022). Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas. The American journal of surgical pathology, 46(1), 97-104. https://doi.org/10.1097/PAS.0000000000001817
Uhlig, Ria, et al. "Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas." The American journal of surgical pathology vol. 46,1 (2022): 97-104. doi: https://doi.org/10.1097/PAS.0000000000001817
Uhlig R, Contreras H, Weidemann S, Gorbokon N, Menz A, Büscheck F, Luebke AM, Kluth M, Hube-Magg C, Hinsch A, Höflmayer D, Fraune C, Möller K, Bernreuther C, Lebok P, Sauter G, Wilczak W, Izbicki J, Perez D, Schrader J, Steurer S, Burandt E, Krech R, Dum D, Krech T, Marx A, Simon R, Minner S, Jacobsen F, Clauditz TS. Carboxypeptidase A1 (CPA1) Immunohistochemistry Is Highly Sensitive and Specific for Acinar Cell Carcinoma (ACC) of the Pancreas. Am J Surg Pathol. 2022 Jan 01;46(1):97-104. doi: 10.1097/PAS.0000000000001817. PMID: 34889867.
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Leucine content of dietary proteins is a determinant of postprandial skeletal muscle protein synthesis in adult rats.

Nutrition & metabolism

Norton LE, Wilson GJ, Layman DK, Moulton CJ, Garlick PJ.
PMID: 22818257
Nutr Metab (Lond). 2012 Jul 20;9(1):67. doi: 10.1186/1743-7075-9-67.

BACKGROUND: Leucine (Leu) regulates muscle protein synthesis (MPS) producing dose-dependent plasma Leu and MPS responses from free amino acid solutions. This study examined the role of Leu content from dietary proteins in regulation of MPS after complete meals.METHODS: Experiment...

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Norton LE, Wilson GJ, Layman DK, et al. Leucine content of dietary proteins is a determinant of postprandial skeletal muscle protein synthesis in adult rats. Nutr Metab (Lond). 2012;9(1):67doi: 10.1186/1743-7075-9-67.
Norton, L. E., Wilson, G. J., Layman, D. K., Moulton, C. J., & Garlick, P. J. (2012). Leucine content of dietary proteins is a determinant of postprandial skeletal muscle protein synthesis in adult rats. Nutrition & metabolism, 9(1), 67. https://doi.org/10.1186/1743-7075-9-67
Norton, Layne E, et al. "Leucine content of dietary proteins is a determinant of postprandial skeletal muscle protein synthesis in adult rats." Nutrition & metabolism vol. 9,1 (2012): 67. doi: https://doi.org/10.1186/1743-7075-9-67
Norton LE, Wilson GJ, Layman DK, Moulton CJ, Garlick PJ. Leucine content of dietary proteins is a determinant of postprandial skeletal muscle protein synthesis in adult rats. Nutr Metab (Lond). 2012 Jul 20;9(1):67. doi: 10.1186/1743-7075-9-67. PMID: 22818257; PMCID: PMC3488566.
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Impact of Elimination or Reduction of Dietary Animal Proteins on Cancer Progression and Survival: Protocol of an Online Pilot Cohort Study.

JMIR research protocols

Catany Ritter A, Egger AS, Machacek J, Aspalter R.
PMID: 27473726
JMIR Res Protoc. 2016 Jul 29;5(3):e157. doi: 10.2196/resprot.5804.

BACKGROUND: Current evidence suggests that the incidence of cancer is low in vegan populations, and experimental studies have revealed a significant role of dietary proteins in cancer development and progression. However, little data currently exists regarding the effect of...

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Catany Ritter A, Egger AS, Machacek J, et al. Impact of Elimination or Reduction of Dietary Animal Proteins on Cancer Progression and Survival: Protocol of an Online Pilot Cohort Study. JMIR Res Protoc. 2016;5(3):e157doi: 10.2196/resprot.5804.
Catany Ritter, A., Egger, A. S., Machacek, J., & Aspalter, R. (2016). Impact of Elimination or Reduction of Dietary Animal Proteins on Cancer Progression and Survival: Protocol of an Online Pilot Cohort Study. JMIR research protocols, 5(3), e157. https://doi.org/10.2196/resprot.5804
Catany Ritter, Anna, et al. "Impact of Elimination or Reduction of Dietary Animal Proteins on Cancer Progression and Survival: Protocol of an Online Pilot Cohort Study." JMIR research protocols vol. 5,3 (2016): e157. doi: https://doi.org/10.2196/resprot.5804
Catany Ritter A, Egger AS, Machacek J, Aspalter R. Impact of Elimination or Reduction of Dietary Animal Proteins on Cancer Progression and Survival: Protocol of an Online Pilot Cohort Study. JMIR Res Protoc. 2016 Jul 29;5(3):e157. doi: 10.2196/resprot.5804. PMID: 27473726; PMCID: PMC4982911.
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Showing 13 to 24 of 118 entries