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Journal articles on the topic 'Protein metabolism'

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Author: Grafiati

Published: 4 June 2021

Last updated: 6 September 2023

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1

Bakhtiyorovich, Eshburiev Sobir, and Kasimov SaifiddinJakhongir Ugli. "DIAGNOSIS OF PROTEIN METABOLISM DISORDERS IN FISH." American Journal Of Agriculture And Horticulture Innovations 03, no. 05 (May 1, 2023): 04–12. http://dx.doi.org/10.37547/ajahi/volume03issue05-02.

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This article describes the most important diagnostic tests in determining protein metabolism disorders of Fish and their importance. When diagnosing disorders of protein metabolism in fish, it is necessary to carry out an analysis of feeding them according to age (nutritional norms), characteristic clinical signs (loss of appetite, development of coxexia, lag behind growth and development), pathologoanatomic changes (accumulation of fat around internal azos, darkening of body color, coxexia, blood clots in the intestines), morphobiochemical changes in the blood (hemoglobin, erythrocyte count, average of hematocrit, leukocyte count, neutrophil with Rod nucleus, basophils, monocytes, lymphocytes, analysis of the average total protein, total calcium, inorganic phosphorus and retinol) is considered important.

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2

TAKAHASHI, Shin-Ichirou. "Hormone and protein metabolism. Insulin and protein metabolism." Journal of the agricultural chemical society of Japan 61, no. 10 (1987): 1300–1304. http://dx.doi.org/10.1271/nogeikagaku1924.61.1300.

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3

KATO, Shigeaki. "Hormone and protein metabolism. Glucocorticoid and protein metabolism." Journal of the agricultural chemical society of Japan 61, no. 10 (1987): 1309–11. http://dx.doi.org/10.1271/nogeikagaku1924.61.1309.

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4

TAKENAKA, Akio. "Hormone and protein metabolism. Glucagon and protein metabolism." Journal of the agricultural chemical society of Japan 61, no. 10 (1987): 1312–14. http://dx.doi.org/10.1271/nogeikagaku1924.61.1312.

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5

YAGASAKI, Kazumi. "Hormone and protein metabolism. Prostaglandin and protein metabolism." Journal of the agricultural chemical society of Japan 61, no. 10 (1987): 1315–18. http://dx.doi.org/10.1271/nogeikagaku1924.61.1315.

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6

Anderson, Kristin A., and Matthew D. Hirschey. "Mitochondrial protein acetylation regulates metabolism." Essays in Biochemistry 52 (May 25, 2012): 23–35. http://dx.doi.org/10.1042/bse0520023.

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Changes in cellular nutrient availability or energy status induce global changes in mitochondrial protein acetylation. Over one-third of all proteins in the mitochondria are acetylated, of which the majority are involved in some aspect of energy metabolism. Mitochondrial protein acetylation is regulated by SIRT3 (sirtuin 3), a member of the sirtuin family of NAD+-dependent protein deacetylases that has recently been identified as a key modulator of energy homoeostasis. In the absence of SIRT3, mitochondrial proteins become hyperacetylated, have altered function, and contribute to mitochondrial dysfunction. This chapter presents a review of the functional impact of mitochondrial protein acetylation, and its regulation by SIRT3.

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7

Emery, Peter. "Basic metabolism: protein." Surgery (Oxford) 27, no. 5 (May 2009): 185–89. http://dx.doi.org/10.1016/j.mpsur.2009.04.005.

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8

Emery, Peter W. "Basic metabolism: protein." Surgery (Oxford) 30, no. 5 (May 2012): 209–13. http://dx.doi.org/10.1016/j.mpsur.2012.02.008.

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9

Emery, Peter W. "Basic metabolism: protein." Surgery (Oxford) 33, no. 4 (April 2015): 143–47. http://dx.doi.org/10.1016/j.mpsur.2015.01.008.

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10

KATO, Hisanori. "Hormone and protein metabolism. Insulin-like growth factor and protein metabolism." Journal of the agricultural chemical society of Japan 61, no. 10 (1987): 1305–8. http://dx.doi.org/10.1271/nogeikagaku1924.61.1305.

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11

De Feo, Pierpaolo. "Hormonal regulation of human protein metabolism." European Journal of Endocrinology 135, no. 1 (July 1996): 7–18. http://dx.doi.org/10.1530/eje.0.1350007.

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De Feo P. Hormonal regulation of human protein metabolism. Eur J Endocrinol 1996:135:7–18. ISSN 0804–4643 This review focuses on the effects of hormones on protein kinetics in humans. Most of the recent knowledge on the regulation of protein metabolism in humans has been obtained by tracing protein kinetics in vivo, using labelled isotopes of essential or non-essential amino acids. This technique allows the rates of the whole-body protein synthesis and breakdown to be estimated together with amino acid oxidation and the fractional synthetic rates of mixed muscle proteins or of single plasma proteins. Changes induced within these parameters by hormonal administration or endocrine diseases are also discussed. Hormones, on the basis of their net effect on protein balance (protein synthesis minus protein breakdown), are divided into two categories: those provided with an anabolic action and those with a prevalent catabolic action. The effects on protein metabolism of the following hormones are reviewed: insulin, growth hormone, IGF-I, adrenaline, androgens, estrogens, progesterone, glucagon, glucocorticosteroids, thyroid hormones. The review concludes with a report on the effects of multiple hormonal infusions on whole-body protein kinetics and a discussion on the potential role played by the concomitant increase of several hormones in the pathogenesis of protein wasting that complicates stress diseases. Pierpaolo De Feo, DIMISEM, Via E. Dal Pozzo, 06126 Perugia, Italy

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12

OKUDA, Toyoko, Hiroko MIYOSHI-NISHIMURA, Tomoe MAKITA, Yohko SUGAWA-KATAYAMA, Toshio HAZAMA, Tuyoshi SIMIZU, and Yuzo YAMAGUCHI. "Protein Metabolism in Vegans." Annals of physiological anthropology 13, no. 6 (1994): 393–401. http://dx.doi.org/10.2114/ahs1983.13.393.

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13

Moller, N., and K. S. Nair. "Diabetes and Protein Metabolism." Diabetes 57, no. 1 (December 28, 2007): 3–4. http://dx.doi.org/10.2337/db07-1581.

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14

Evans, W. J., W. W. Campbell, R. Wolfe, K. Yarasheski, and F. W. Booth. "PROTEIN METABOLISM AND EXERCISE." Medicine & Science in Sports & Exercise 27, Supplement (May 1995): S164. http://dx.doi.org/10.1249/00005768-199505001-00923.

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15

Schoenheimer, Rudolf, S. Ratner, and D. Rittenberg. "Studies in Protein Metabolism." Nutrition Reviews 40, no. 1 (April 27, 2009): 23–26. http://dx.doi.org/10.1111/j.1753-4887.1982.tb06822.x.

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16

Becker, Giles W., and Kenneth Smith. "Basic metabolism III: protein." Surgery (Oxford) 24, no. 4 (April 2006): 115–20. http://dx.doi.org/10.1383/surg.2006.24.4.115.

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17

Sunshine, Philip. "Protein Metabolism During Infancy." American Journal of Clinical Nutrition 61, no. 5 (May 1, 1995): 1177–78. http://dx.doi.org/10.1093/ajcn/61.5.1177-a.

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18

Kalhan, Satish C. "Protein metabolism in pregnancy." American Journal of Clinical Nutrition 71, no. 5 (May 1, 2000): 1249S—1255S. http://dx.doi.org/10.1093/ajcn/71.5.1249s.

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19

Grizard, Dr J., and Dr K. Grzelkowska. "Session 4: Protein metabolism." Reproduction Nutrition Development 39, no. 1 (1999): 104. http://dx.doi.org/10.1051/rnd:19990142.

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20

Cunningham, Carol C., Victor R. Preedy, Alistair G. Paice, John E. Hesketh, Timothy J. Peters, Vinood B. Patel, Elena Volpi, et al. "Ethanol and Protein Metabolism." Alcoholism: Clinical and Experimental Research 25, Supplement (May 2001): 262S—268S. http://dx.doi.org/10.1097/00000374-200105051-00042.

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21

Beaufrere, Bernard, and Yves Boirie. "Aging and protein metabolism." Current Opinion in Clinical Nutrition and Metabolic Care 1, no. 1 (January 1998): 85–89. http://dx.doi.org/10.1097/00075197-199801000-00014.

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22

Jackson, A. A. "Chronic malnutrition: protein metabolism." Proceedings of the Nutrition Society 52, no. 1 (February 1993): 1–10. http://dx.doi.org/10.1079/pns19930031.

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23

Jessop, Neil S. "Protein metabolism during lactation." Proceedings of the Nutrition Society 56, no. 1A (March 1997): 169–75. http://dx.doi.org/10.1079/pns19970019.

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24

Kurzer, Martin, and Michael M. Meguid. "Cancer and Protein Metabolism." Surgical Clinics of North America 66, no. 5 (October 1986): 969–1001. http://dx.doi.org/10.1016/s0039-6109(16)44036-3.

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25

Cunningham, Carol C., Victor R. Preedy, Alistair G. Paice, John E. Hesketh, Timothy J. Peters, Vinood B. Patel, Elena Volpi, et al. "Ethanol and Protein Metabolism." Alcoholism: Clinical and Experimental Research 25, s1 (May 2001): 262S—268S. http://dx.doi.org/10.1111/j.1530-0277.2001.tb02406.x.

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26

Millward, D. Joe, Amelia Fereday, Neil R. Gibson, and Paul J. Pacy. "Post-prandial protein metabolism." Baillière's Clinical Endocrinology and Metabolism 10, no. 4 (October 1996): 533–49. http://dx.doi.org/10.1016/s0950-351x(96)80696-3.

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27

Robinson, Stephen, and Colin H. Prendergast. "Protein metabolism in pregnancy." Baillière's Clinical Endocrinology and Metabolism 10, no. 4 (October 1996): 571–87. http://dx.doi.org/10.1016/s0950-351x(96)80726-9.

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28

Hirschey, Matthew. "Protein Acylation Regulates Metabolism." Biophysical Journal 106, no. 2 (January 2014): 4a. http://dx.doi.org/10.1016/j.bpj.2013.11.053.

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29

Barazzoni, R., M. Zanetti, A. Tiengo, and P. Tessari. "Protein metabolism in glucagonoma." Diabetologia 42, no. 3 (February 19, 1999): 326–29. http://dx.doi.org/10.1007/s001250051158.

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30

NOGUCHI, Tadashi. "Hormone and protein metabolism." Journal of the agricultural chemical society of Japan 61, no. 10 (1987): 1297–99. http://dx.doi.org/10.1271/nogeikagaku1924.61.1297.

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31

Rakhmonjonovna, Kapizova Dilafruz Rakhmonjonovna. "COMMON PATHWAYS OF PROTEIN AND AMINO ACID METABOLISM IN THE BODY." International Journal of Medical Sciences And Clinical Research 03, no. 06 (June 1, 2023): 49–52. http://dx.doi.org/10.37547/ijmscr/volume03issue06-09.

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Protein exchange is crucial for the life of the whole organism, each of its tissues and organs, some cells and subcellular components. Biochemical activity of the cell and all metabolic reactions occurring in it are related to the exchange of proteins.

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32

Umbu Henggu, Krisman, and Yopi Nurdiansyah. "Review dari Metabolisme Karbohidrat, Lipid, Protein, dan Asam Nukleat." QUIMICA: Jurnal Kimia Sains dan Terapan 3, no. 2 (August 2, 2022): 9–17. http://dx.doi.org/10.33059/jq.v3i2.5688.

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Artikel review ini mengulas tentang prinsip dan proses metabolisme karbohidrat, lipid, protein dan asam nukeat pada organisme. Telaah pustaka yang disajikan dalam review ini bersumber pada jurnal ilmiah maupun buku terakreditasi yang relevan. Lintasan metabolisme karbohidrat, lipid, protein, asam nukleat terdiri atas tiga bentuk lintasan yakni katabolik, anabolik dan amfibolik. Lintasan tersebut umumnya terjadi pada mitokondria melalui siklus Krebs. Katabolisme protein, karbohidrat dan lemak dapat menjadi derivat asam amino, glukosa, gliserol dan asam lemak yang mampu dikonversi menjadi energi maupun cadangan energi untuk proses pertumbuhan dan perkembangan sel. Demikian sebaliknya proses anabolisme dapat memanfaatkan derivat makro molekul (asam amino, glukosa, fruktosa, asam lemak) menjadi makro molekul (protein, karbohidrat dan lipid). Proses metabolisme karbohidrat secara khusus melalui glikolisis, glikogenesis dan glukoneogenesis. Sedangkan metabolisme lemak melalui proses asetil-KoA terkarboksilase dan menghasilkan malonil-KoA hingga berlanjut pada proses pembentukan asam lemak melalui proses enzimatis (elongase dan desaturase). Demikian pula pada metabolisme protein yang diawali dengan pemecahan makro molekul dalam bentuk peptida menjadi monomer terkecil (asam amino) secara enzimatis (melibatkan enzim protease) dan menjadi salah satu sumber energi dalam pembentukan ATP untuk perkembangan sel. Sebaliknya anabolisme protein tersebut didasari oleh proses transmisi dan aminasi. Metabolisme asam nukleat melibatkan proses sintesis purin dan pirimidin sebagai nukleotida secara de novo. Proses metabolisme asam nukleat melaui proses enzimatik (housekeeping) yang sangat bertanggungjawab terhadap fungsi katabolisme dan anabolisme. Referensi: [1] Wali, J. A., Milner, A. J., Luk, A. W., Pulpitel, T. J., Dodgson, T., Facey, H. J., ... & Simpson, S. J. (2021). Impact of dietary carbohydrate type and protein–carbohydrate interaction on metabolic health. Nature Metabolism, 3(6), 810-828. [2] Staples, J. F. (2016). Metabolic flexibility: hibernation, torpor, and estivation. Compr. Physiol, 6(2), 737-71. [3] O’Neill, L. A. (2015). A broken krebs cycle in macrophages. Immunity, 42(3), 393-394. [4] Rajendran, M., Dane, E., Conley, J., & Tantama, M. (2016). Imaging adenosine triphosphate (ATP). The Biological Bulletin, 231(1), 73-84. [5] Luo, L., & Liu, M. (2016). Adipose tissue in control of metabolism. Journal of endocrinology, 231(3), R77-R99. [6] Poggiogalle, E., Jamshed, H., & Peterson, C. M. (2018). Circadian regulation of glucose, lipid, and energy metabolism in humans. Metabolism, 84, 11-27. [7] Purba, D. H., Marzuki, I., Dailami, M., Saputra, H. A., Mawarti, H., Gurning, K., ... & Purba, A. M. V. (2021). Biokimia. . Bandung (ID): Yayasan Kita Menulis Press [8] Park, S., Jeon, J. H., Min, B. K., Ha, C. M., Thoudam, T., Park, B. Y., & Lee, I. K. (2018). Role of the pyruvate dehydrogenase complex in metabolic remodeling: differential pyruvate dehydrogenase complex functions in metabolism. Diabetes & metabolism journal, 42(4), 270-281. [9] Adeva-Andany, M. M., Pérez-Felpete, N., Fernández-Fernández, C., Donapetry-García, C., & Pazos-García, C. (2016). Liver glucose metabolism in humans. Bioscience reports, 36(6). [10] Murray, Robert K. Daryl K. Granner; Victor W. Rodwell. Biokimia Harper Ed.27. Jakarta. EGC;2009 : 152-94 [11] Jones, J. G. (2016). Hepatic glucose and lipid metabolism. Diabetologia, 59(6), 1098-1103. [12] Chen, L., Zhang, Z., Hoshino, A., Zheng, H. D., Morley, M., Arany, Z., & Rabinowitz, J. D. (2019). NADPH production by the oxidative pentose-phosphate pathway supports folate metabolism. Nature metabolism, 1(3), 404-415. [13] Shi, L., & Tu, B. P. (2015). Acetyl-CoA and the regulation of metabolism: mechanisms and consequences. Current opinion in cell biology, 33, 125-131. [14] Chandel, N. S. (2021). Lipid metabolism. Cold Spring Harbor Perspectives in Biology, 13(9), a040576. [15] Tsikas, D. (2017). Assessment of lipid peroxidation by measuring malondialdehyde (MDA) and relatives in biological samples: Analytical and biological challenges. Analytical biochemistry, 524, 13-30. [16] Merino-Ramos, T., Vázquez-Calvo, Á., Casas, J., Sobrino, F., Saiz, J. C., & Martín-Acebes, M. A. (2016). Modification of the host cell lipid metabolism induced by hypolipidemic drugs targeting the acetyl coenzyme A carboxylase impairs West Nile virus replication. Antimicrobial agents and chemotherapy, 60(1), 307-315. [17] Schmitt, S., Castelvetri, L. C., & Simons, M. (2015). Metabolism and functions of lipids in myelin. Biochimica et Biophysica Acta (BBA)-Molecular and Cell Biology of Lipids, 1851(8), 999-1005. [18] Cerk, I. K., Wechselberger, L., & Oberer, M. (2018). Adipose triglyceride lipase regulation: an overview. Current Protein and Peptide Science, 19(2), 221-233. [19] Whitford, D. (2013). Proteins: Structure And Function. John Wiley & Sons. [20] Gropper, S. S., & Smith, J. L. (2012). Advanced Nutrition And Human Metabolism. Cengage Learning. [21] Bender, D. A. (2012). Amino acid metabolism. John Wiley & Sons. [22] Chargaff, E. (Ed.). (2012). The nucleic acids. Elsevier. [23] Kochetkov, N. (Ed.). (2012). Organic Chemistry of Nucleic Acids: Part B. Springer Science & Business Media. [24] Wang, L. (2016). Mitochondrial purine and pyrimidine metabolism and beyond. Nucleosides, Nucleotides and Nucleic Acids, 35(10-12), 578-594.

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33

Millward, D. Joe, Joanna L. Bowtell, Paul Pacy, and Michael J. Rennie. "Physical activity, protein metabolism and protein requirements." Proceedings of the Nutrition Society 53, no. 1 (March 1994): 223–40. http://dx.doi.org/10.1079/pns19940024.

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34

Kucharzewski, Marek, Ireneusz Ryszkiel, Katarzyna Wilemska-Kucharzewska, Ewa Rojczyk-Gołębiewska, and Artur Pałasz. "Protein metabolism in the patients with thermal injury." Leczenie Ran 11, no. 3 (September 5, 2014): 91–96. http://dx.doi.org/10.15374/lr2014014.

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35

Roberts, Melissa A., and James A. Olzmann. "Protein Quality Control and Lipid Droplet Metabolism." Annual Review of Cell and Developmental Biology 36, no. 1 (October 6, 2020): 115–39. http://dx.doi.org/10.1146/annurev-cellbio-031320-101827.

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Lipid droplets (LDs) are endoplasmic reticulum–derived organelles that consist of a core of neutral lipids encircled by a phospholipid monolayer decorated with proteins. As hubs of cellular lipid and energy metabolism, LDs are inherently involved in the etiology of prevalent metabolic diseases such as obesity and nonalcoholic fatty liver disease. The functions of LDs are regulated by a unique set of associated proteins, the LD proteome, which includes integral membrane and peripheral proteins. These proteins control key activities of LDs such as triacylglycerol synthesis and breakdown, nutrient sensing and signal integration, and interactions with other organelles. Here we review the mechanisms that regulate the composition of the LD proteome, such as pathways that mediate selective and bulk LD protein degradation and potential connections between LDs and cellular protein quality control.

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36

Teerlink, Tom. "ADMA metabolism and clearance." Vascular Medicine 10, no. 2_suppl (May 2005): S73—S81. http://dx.doi.org/10.1191/1358863x05vm597oa.

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The plasma concentration of asymmetric dimethylarginine (ADMA), an endogenous inhibitor of nitric oxide synthase, is the resultant of many processes at cellular and organ levels. Post-translational methylation of arginine residues of proteins plays a crucial role in the regulation of their functions, which include processes such as transcription, translation and RNA splicing. Because protein methylation is irreversible, the methylation signal can be turned off only by proteolysis of the entire protein. Consequently, most methylated proteins have high turnover rates. Free ADMA, which is formed during proteolysis, is actively degraded by the intracellular enzyme dimethylarginine dimethylaminohydrolase (DDAH). Some ADMA escapes degradation and leaves the cell via cationic amino acid transporters. These transporters also mediate uptake of ADMA by neighboring cells or distant organs, thereby facilitating active interorgan transport. Clearance of ADMA from the plasma occurs in small part by urinary excretion, but the bulk of ADMA is degraded by intracellular DDAH, after uptake from the circulation. This review discusses the various processes involved in ADMA metabolism: protein methylation, proteolysis of methylated proteins, metabolism by DDAH, and interorgan transport. In addition, the role of the kidney and the liver in the clearance of ADMA is highlighted.

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37

Samardzic, Kate, and Kenneth J. Rodgers. "Oxidised protein metabolism: recent insights." Biological Chemistry 398, no. 11 (October 26, 2017): 1165–75. http://dx.doi.org/10.1515/hsz-2017-0124.

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Abstract The ‘oxygen paradox’ arises from the fact that oxygen, the molecule that aerobic life depends on, threatens its very existence. An oxygen-rich environment provided life on Earth with more efficient bioenergetics and, with it, the challenge of having to deal with a host of oxygen-derived reactive species capable of damaging proteins and other crucial cellular components. In this minireview, we explore recent insights into the metabolism of proteins that have been reversibly or irreversibly damaged by oxygen-derived species. We discuss recent data on the important roles played by the proteasomal and lysosomal systems in the proteolytic degradation of oxidatively damaged proteins and the effects of oxidative damage on the function of the proteolytic pathways themselves. Mitochondria are central to oxygen utilisation in the cell, and their ability to handle oxygen-derived radicals is an important and still emerging area of research. Current knowledge of the proteolytic machinery in the mitochondria, including the ATP-dependent AAA+ proteases and mitochondrial-derived vesicles, is also highlighted in the review. Significant progress is still being made in regard to understanding the mechanisms underlying the detection and degradation of oxidised proteins and how proteolytic pathways interact with each other. Finally, we highlight a few unanswered questions such as the possibility of oxidised amino acids released from oxidised proteins by proteolysis being re-utilised in protein synthesis thus establishing a vicious cycle of oxidation in cells.

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38

Hogan, Meghan F., Mark Ziemann, Harikrishnan K N, Hanah Rodriguez, Antony Kaspi, Nathalie Esser, Andrew T. Templin, Assam El-Osta, and Steven E. Kahn. "RNA-seq-based identification of Star upregulation by islet amyloid formation." Protein Engineering, Design and Selection 32, no. 2 (February 2019): 67–76. http://dx.doi.org/10.1093/protein/gzz022.

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AbstractAggregation of islet amyloid polypeptide (IAPP) into islet amyloid results in β-cell toxicity in human type 2 diabetes. To determine the effect of islet amyloid formation on gene expression, we performed ribonucleic acid (RNA) sequencing (RNA-seq) analysis using cultured islets from either wild-type mice (mIAPP), which are not amyloid prone, or mice that express human IAPP (hIAPP), which develop amyloid. Comparing mIAPP and hIAPP islets, 5025 genes were differentially regulated (2439 upregulated and 2586 downregulated). When considering gene sets (reactomes), 248 and 52 pathways were up- and downregulated, respectively. Of the top 100 genes upregulated under two conditions of amyloid formation, seven were common. Of these seven genes, only steroidogenic acute regulatory protein (Star) demonstrated no effect of glucose per se to modify its expression. We confirmed this differential gene expression using quantitative reverse transcription polymerase chain reaction (qRT-PCR) and also demonstrated the presence of STAR protein in islets containing amyloid. Furthermore, Star is a part of reactomes representing metabolism, metabolism of lipids, metabolism of steroid hormones, metabolism of steroids and pregnenolone biosynthesis. Thus, examining gene expression that is differentially regulated by islet amyloid has the ability to identify new molecules involved in islet physiology and pathology applicable to type 2 diabetes.

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39

Kurpińska, Anna, Agnieszka Jarosz, and Wiesław Skrzypczak. "Parameters of protein and iron metabolism in dairy cows during periparturient period." Acta Scientiarum Polonorum Zootechnica 18, no. 3 (January 15, 2020): 3–10. http://dx.doi.org/10.21005/asp.2019.18.3.01.

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40

Dianti, Sari, Anggi Suwi Apriansyah, Rapies Honal Hari Sya'ban, and Qomariah Hasanah. "PANDANGAN ISLAM TERHADAP METABOLISME PROTEIN." Borneo : Journal of Islamic Studies 3, no. 1 (December 28, 2022): 15–26. http://dx.doi.org/10.37567/borneo.v3i1.1497.

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Islam obliges its followers to seek knowledge, where in the book of the Qur'an there is all knowledge from the smallest to the largest including knowledge related to living things in which it describes protein metabolism. The purpose of this study was to determine the Islamic view of protein metabolism. The author uses qualitative methods with sources in the form of books, journals, al-Qur'an, al-Hadith and sources from theses and articles from the internet. The results of the study show that metabolism is one of the most important processes in the body of living things, in order to produce the energy needed for survival. One example of metabolism is protein metabolism, which is a chemical and physical process that occurs in two phases, namely anabolism and catabolism where the change (anabolism) of proteins into amino acids and the breakdown (catabolism) of amino acids in proteins. A high source of protein that is needed by the body comes from animal protein as contained in QS. An-Nahl verse 5. In order to maintain protein metabolism, food must be in accordance with the portion. Therefore, Islam regulates food that is halal and good for processing in the body, including the quantity of food that is consumed. This was exemplified by the Prophet by putting food into the mouth in small portions to help digestion go well.

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41

Teerlink, Tom. "ADMA metabolism and clearance." Vascular Medicine 10, no. 1_suppl (July 2005): S73—S81. http://dx.doi.org/10.1177/1358836x0501000111.

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Abstract:

The plasma concentration of asymmetric dimethylarginine (ADMA), an endogenous inhibitor of nitric oxide synthase, is the resultant of many processes at cellular and organ levels. Post-translational methylation of arginine residues of pro teins plays a crucial role in the regulation of their functions, which include processes such as transcription, translation and RNA splicing. Because protein methylation is irreversible, the methylation signal can be turned off only by proteolysis of the entire protein. Consequently, most methylated proteins have high turnover rates. Free ADMA, which is formed during proteolysis, is actively degraded by the intracellular enzyme dimethylarginine dimethylaminohydrolase (DDAH). Some ADMA escapes degradation and leaves the cell via cationic amino acid transporters. These trans porters also mediate uptake of ADMA by neighboring cells or distant organs, thereby facilitating active interorgan transport. Clearance of ADMA from the plasma occurs in small part by urinary excretion, but the bulk of ADMA is degraded by intracellular DDAH, after uptake from the circulation. This review discusses the various processes involved in ADMA metabolism: protein methylation, proteolysis of methylated proteins, metabolism by DDAH, and interorgan transport. In addition, the role of the kidney and the liver in the clearance of ADMA is highlighted.

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Sklan, D., S. Trifon, O. Kedar, N. Vaisman, and Y. Berner. "Retinoid metabolism in human leucocytes." British Journal of Nutrition 73, no. 6 (June 1995): 889–95. http://dx.doi.org/10.1079/bjn19950094.

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Leucocytes from subjects from 0 to 80 years old were separated into mononuclear and granulocyte fractions and the retinoids and retinoid-binding fractions were examined. Both leucocyte ractions were found to contain retinol, retinoic acid and an additional retinoid; retinoic acid Comprised 40% of retinoids in some samples. The protein fractions containing retinoids included a 200 k Da protein and several 14–18 k Da proteins. Plasma concentrations of retinol changed little with increasing age. In contrast, leucocyte concentrations of retinoids and retinoid-binding proteins increased quadratically with age. However, in granulocytes from young children retinoids were almost undetectable.

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Luo, Junqiu, Daiwen Chen, and Bing Yu. "Effects of different dietary protein sources on expression of genes related to protein metabolism in growing rats." British Journal of Nutrition 104, no. 10 (July 8, 2010): 1421–28. http://dx.doi.org/10.1017/s000711451000231x.

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Protein metabolism is known to be affected by dietary proteins, but the fundamental mechanisms that underlie the changes in protein metabolism are unclear. The aim of the present study was to test the effects of feeding growing rats with balanced diets containing soya protein isolate, zein and casein as the sole protein source on the expression of genes related to protein metabolism responses in skeletal muscle. The results showed that feeding a zein protein diet to the growing rats induced changes in protein anabolic and catabolic metabolism in their gastrocnemius muscles when compared with those fed either the reference protein casein diet or the soya protein isolate diet. The zein protein diet increased not only the mRNA levels and phosphorylation of mammalian target of rapamycin (mTOR), but also the mRNA expression of muscle atrophy F-box (MAFbx)/atrogin-1 and muscle ring finger 1 (MuRF1), as well as the forkhead box-O (FoxO) transcription factors involved in the induction of the E3 ligases. The amino acid profile of proteins seems to control signalling pathways leading to changes in protein synthesis and proteolysis.

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NATORI, Yasuo. "Nutritional Regulation of Protein Metabolism." Nippon Eiyo Shokuryo Gakkaishi 48, no. 6 (1995): 429–39. http://dx.doi.org/10.4327/jsnfs.48.429.

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Gibala, Martin J. "Protein Metabolism and Endurance Exercise." Sports Medicine 37, no. 4 (2007): 337–40. http://dx.doi.org/10.2165/00007256-200737040-00016.

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46

Hasselgren, P. O. "Muscle protein metabolism during sepsis." Biochemical Society Transactions 23, no. 4 (November 1, 1995): 1019–25. http://dx.doi.org/10.1042/bst0231019.

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Moore, Daniel R. "Resistance Training and Protein Metabolism." Medicine & Science in Sports & Exercise 39, Supplement (May 2007): 67–68. http://dx.doi.org/10.1249/01.mss.0000272811.42587.ce.

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Hayase, Kazutoshi, and Hidehiko Yokogoshi. "Nutrition and Brain Protein Metabolism." Nippon Nōgeikagaku Kaishi 69, no. 5 (1995): 586–88. http://dx.doi.org/10.1271/nogeikagaku1924.69.586.

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Manstein, Carl H. "Protein metabolism kinetics in neonates." Plastic & Reconstructive Surgery 98, no. 7 (December 1996): 1331. http://dx.doi.org/10.1097/00006534-199612000-00090.

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Bohé, Julien, and Michael J. Rennie. "Muscle Protein Metabolism During Hemodialysis." Journal of Renal Nutrition 16, no. 1 (January 2006): 3–16. http://dx.doi.org/10.1053/j.jrn.2005.07.005.

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