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Gepubliceerd in:
Biomoleculen hoofdstuk lezen eerste hoofdstuk lezen

2019 | OriginalPaper | Hoofdstuk

9. Aminozuurmetabolisme

Auteur : Prof. dr. F.C. Schuit

Gepubliceerd in: Leerboek metabolisme en voeding

Uitgeverij: Bohn Stafleu van Loghum

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Samenvatting

Hoofdstuk 9 behandelt een netwerk van metabole wegen waarin een aantal voor de mens belangrijke aminozuren met elkaar verbonden worden. We beginnen met de twintig verschillende aminozuurbouwstenen die nodig zijn voor de eiwitsynthese. Een deel hiervan, de niet-essentiële aminozuren, kan door ons eigen metabolisme worden aangemaakt. In tegenstelling hiermee staan de essentiële aminozuren, die alleen via de voeding in het lichaam kunnen worden opgenomen. Aminozuren kunnen ook worden afgebroken, waarbij het stikstofafval in de lever veilig tot ureum wordt verwerkt, dat in de urine wordt uitgescheiden. Zonder deze metabole werking van de lever zou het lichaam door opstapeling van ammoniak worden vergiftigd. We bespreken ook stofwisselingsziekten van het aminozuurmetabolisme, zoals alkaptonurie, albinisme en fenylketonurie. We eindigen het hoofdstuk met belangrijke van aminozuren afgeleide moleculen. Voorbeelden hiervan zijn heem dat we vinden in hemoglobine en in cytochromen, en de hormonen adrenaline en schildklierhormoon.
vorige hoofdstuk Vetzuur- en cholesterolafgeleiden
volgende hoofdstuk Nucleotidenmetabolisme
Literatuur
Albrecht, J., Sidoryk-Węgrzynowicz, M., Zielińska, M. & Aschner, M. (2010). Roles of glutamine in neurotransmission. Neuron Glia Biol. 6, 263–276.
Ahles, A. & Engelhardt, S. (2014) Polymorphic variants of adrenoceptors: pharmacology, physiology, and role in disease. Pharmacol Rev. 66, 598–637.
Akdis, C.A., Jutel, M. & Akdis, M. (2008). Regulatory effects of histamine & histamine receptor expression in human allergic immune responses. Chem. Immunol. Allergy. 94, 67–82.
Autti-Rämö, I., et al. (2005). Expanding screening for rare metabolic disease in the newborn: an analysis of costs, effect and ethical consequences for decision-making in Finland. Acta Paediatr. 94, 1126–1136.CrossRef
Baker, DH. (2005). Comparative nutrition and metabolism: explication of open questions with emphasis on protein and amino acids. Proc. Natl. Acad. Sci. U.S.A. 102, 17897–17902.CrossRef
Baskin, A.S., et al. (2018) Regulation of human adipose tissue activation, gallbladder size, and bile acid metabolism by a β3-adrenergic receptor agonist. Diabetes 67, 2113–2125.CrossRef
Behera, J. et al. (2017) Homocysteine as a Pathological Biomarker for Bone Disease. J Cell Physiol. 232, 2704–2709.CrossRef
Bogdan C. (2015) Nitric oxide synthase in innate and adaptive immunity: an update. Trends Immunol. 36, 161–178.CrossRef
Bosma, P.J. (2003). Inherited disorders of bilirubin metabolism. J. Hepatol. 38, 107–117.CrossRef
Braissant, O. & Henry, H. (2008). AGAT, GAMT and SLC6A8 distribution in the central nervous system, in relation to creatine deficiency syndromes: a review. J Inherit Metab Dis. 31, 230–239.
Brosnan, M.E. & Brosnan, J.T. (2009). Hepatic glutamate metabolism: a tale of 2 hepatocytes. Am. J. Clin. Nutr. 90, 857S–861S.
Camp, K.M., Lloyd-Puryear, M.A. & Huntington, K.L. (2012). Nutritional treatment for inborn errors of metabolism: indications, regulations, and availability of medical foods and dietary supplements using phenylketonuria as an example. Mol Genet Metab. 107, 3–9.
Caruso, J., Charles. J., Unruh, K., Giebel, R., Learmonth, L. & Potter, W. (2012). Ergogenic effects of β-alanine and carnosine: proposed future research to quantify their efficacy. Nutrients. 4, 585–601.
Casero, R.A. & Pegg, A.E. (2009). Polyamine catabolism and disease. Biochem J. 421, 323–338.
COUNCIL ON ENVIRONMENTAL HEALTH (2016) Prevention of Childhood Lead Toxicity. Pediatrics 138, e20161493.
Derave, W., Ozdemir, M.S., Harris, R.C., Pottier, A., Reyngoudt, H., Koppo, K., Wise, J.A. & Achten, E. (2007). Beta-alanine supplementation augments muscle carnosine content and attenuates fatigue during repeated isokinetic contraction bouts in trained sprinters. J Appl Physiol. 103, 1736–1743.
Dever, T.E. & Ivanov, I.P. (2018) Roles of polyamines in translation. J Biol Chem. 293, 18719–18729.
Eckel-Mahan, K. & Sassone-Corsi, P. (2013). Metabolism and the circadian clock converge. Physiol Rev. 93, 107–135.
Endo, F., Matsuura, T., Yanagita, K. & Matsuda, I. (2004). Clinical manifestations of inborn errors of the urea cycle & related metabolic disorders during childhood. J. Nutr. 134, 1605S–1609S.
Flora, G., Gupta, D. & Tiwari A. (2012). Toxicity of lead: A review with recent updates. Interdiscip Toxicol. 5, 47–58.
Galgano, F., Caruso, M., Condelli, N. & Favati, F. (2012). Focused review: agmatine in fermented foods. Front Microbiol. 3, 199.
Girault, J.A. & Greengard, P. (2004). The neurobiology of dopamine signaling. Arch. Neurol. 61, 641–644.
Grady, S.L., Purdy, J.G., Rabinowitz, J.D. & Shenk, T. (2013). Argininosuccinate synthetase 1 depletion produces a metabolic state conducive to herpes simplex virus 1 infection. Proc Natl Acad Sci U.S.A. 110, E5006–5015.
Granadino, B., Beltran-Valero de, B.D., Fernandez-Canon, J.M., Penalva, M.A. & Rodriguez de, C.S. (1997). The human homogentisate 1, 2-dioxygenase (HGO) gene. Genomics. 43, 115–122.
Gropman, A.L. (2012). Patterns of brain injury in inborn errors of metabolism. Semin. Pediatr. Neurol. 19, 203–210CrossRef
Gross, U., Hoffmann, G.F. & Doss, M.O. (2000). Erythropoietic & hepatic porphyrias. J. Inherit. Metab Dis. 23, 641–661.
Gupta, V.K., et al. (2013). Restoring polyamines protects from age-induced memory impairment in an autophagy-dependent manner. Nat. Neurosci. 16: 1453–1460.
Harno, E. et al. (2018) POMC: The Physiological Power of Hormone Processing. Physiol Rev. 98, 2381–2430.CrossRef
Helmich, F. & Lock, G. (2018) Burton’s Line from Chronic Lead Intoxication. N Engl J Med. 379, e35.
Hoeks, M.P., Heijer, M. den & Janssen, M.C. (2009). Adult issues in phenylketonuria. Neth J Med. 67, 2–7.
Hipkiss, A.R. (2009). Carnosine and its possible roles in nutrition and health. Adv Food Nutr Res. 57, 87–154.
Huang, W., Ramsey, K.M., Marcheva, B. & Bass, J. (2011). Circadian rhythms, sleep, and metabolism. J Clin Invest. 121, 2133–2141.
Humphrey, L.L., Fu, R., Rogers, K., Freeman, M. & Helfand, M. (2008). Homocysteine level & coronary heart disease incidence: a systematic review & meta-analysis. Mayo Clin. Proc. 83, 1203–1212.
Jakubowski, H. (2018) Homocysteine modification in protein structure/function and human disease. Physiol Rev. 99,555–604.CrossRef
Kalia, L.V. & Lang, A.E. (2015) Parkinson’s disease. Lancet 386, 896–912.
Kauppinen, R. (2005). Porphyrias. Lancet. 365, 241–252.
Kirk, J.M. (2008). Neonatal jaundice: a critical review of the role & practice of bilirubin analysis. Ann. Clin. Biochem. 45, 452–462.
Kondo, T. & Hearing, V.J. (2011). Update on the regulation of mammalian melanocyte function and skin pigmentation. Expert Rev Dermatol. 6, 97–108.
Lawrence, S.H., Ramirez, U.D., Selwood, T., Stith, L. & Jaffe, E.K. (2009). Allosteric inhibition of human porphobilinogen synthase. J. Biol. Chem. 18, 35807–35817.
Liu, P.T. & Modlin, R.L. (2008). Human macrophage host defense against Mycobacterium tuberculosis. Curr. Opin. Immunol. 20, 371–376.
Mallikethi-Reddy, S. et al. (2017) Novel biomarkers with potential for cardiovascular risk reclassification. Biomarkers 22, 189–199.CrossRef
Mayer, M. (2000). Association of serum bilirubin concentration with risk of coronary artery disease. Clin. Chem. 46, 1723–1727.
McMurdy, J.W., Jay, G.D., Suner, S. & Crawford, G. (2008). Noninvasive optical, electrical, & acoustic methods of total hemoglobin determination. Clin. Chem. 54, 264–272.
Meder, D. et al. (2018) The role of dopamine in the brain – lessons learned from Parkinson’s disease. Neuroimage. Nov 20. pii: S1053-8119(18)32092-5.
Mesa, J.L.M., Ruiz, J.R., Gonzalez-Gross, M.M., Sainz, A.G. & Garzon, M.J.C. (2002). Oral creatine supplementation & skeletal muscle metabolism in physical exercise. Sports Med. 32, 903–944.
Missale, C., Nash, S.R., Robinson, S.W., Jaber, M. & Caron, M.G. (1998). Dopamine receptors: from structure to function. Physiol. Rev. 78, 189–225.
Mitra, D. et al. (2012) An ultraviolet-radiation-independent pathway to melanoma carcinogenesis in the red hair/fair skin background. Nature 491, 449–453.
Moinard, C. & Cynober, L. (2007). Citrulline: a new player in the control of nitrogen homeostasis. J. Nutr. 137, 1621S–1625S.
Moini, M., Mistry, P. & Schilsky, M.L. (2010). Liver transplantation for inherited metabolic disorders of the liver. Curr Opin Organ Transplant. 15, 269–276.
Moutkine, I., Collins, E.L., Béchade, C. & Maroteaux, L. (2018) Evolutionary considerations on 5-HT(2) receptors. Pharmacol Res. S1043–6618.
Nasti, T.H. & Timares, L. (2015) MC1R, eumelanin and pheomelanin: their role in determining the susceptibility to skin cancer. Photochem Photobiol. 91,188–200.
Norenberg, M.D., Rama Rao, K.V. & Jayakumar, A.R. (2009). Signaling factors in the mechanism of ammonia neurotoxicity. Metab. Brain Dis. 24, 103–117.
Olsen, R.R. & Zetter, B.R. (2011). Evidence of a role for antizyme and antizyme inhibitor as regulators of human cancer. Mol Cancer Res. 9, 1285–1293.
Osowska, S., Moinard, C., Neveux, N., Loi, C. & Cynober, L. (2004). Citrulline increases arginine pools & restores nitrogen balance after massive intestinal resection. Gut. 53, 1781–1786.
Plaitakis, A., Zaganas, I. & Spanaki, C. (2013). Deregulation of glutamate dehydrogenase in human neurologic disorders. J Neurosci Res. 91, 1007–1017.
Prasad, C. & Galbraith, P.A. (2005). Sir Archibald Garrod & alkaptonuria -‘story of metabolic genetics’. Clin. Genet. 68, 199–203.
Rodrigo, R., Cauli, O., Boix, J., ElMlili, N., Agusti, A. & Felipo, V. (2009). Role of NMDA receptors in acute liver failure & ammonia toxicity: therapeutical implications. Neurochem. Int. 55, 113–118.
Sanders, K.M. & Ward, S.M. (2019) Nitric oxide and its role as a non-adrenergic,non-cholinergic inhibitory neurotransmitter in the gastrointestinal tract. Br J Pharmacol. 176, 212–227.
Schousboe, A., Bak, L.K. & Waagepetersen, H.S. (2013). Astrocytic Control of Biosynthesis and turnover of the Neurotransmitters Glutamate and GABA. Front Endocrinol. 4, 102.
Schubert, M.L. & Peura, D.A. (2008). Control of gastric acid secretion in health and disease. Gastroenterology 134,1842–1860.
Seifert, R., Strasser, A., Schneider, E.H., Neumann, D., Dove, S. & Buschauer A. (2013). Molecular and cellular analysis of human histamine receptor subtypes. Trends Pharmacol Sci. 34, 33–58.
Shu, X. et al. (2015) Endothelial nitric oxide synthase in the microcirculation. Cell Mol Life Sci. 72, 4561–75.CrossRef
Thurmond, R.L., Gelfand, E.W. & Dunford, P.J. (2008). The role of histamine H1 & H4 receptors in allergic inflammation: the search for new antihistamines. Nat. Rev. Drug Discov. 7, 41–53.
Vaz, F.M. & Wanders, R.J.A. (2002). Carnitine biosynthesis in mammals. Biochem. J. 361, 417–429.
Vandermosten, L. et al. (2018) Adrenal hormones mediate disease tolerance in malaria. Nat Commun. 9, 4525.
Willert, E. & Phillips, M.A. (2012). Regulation and function of polyamines in African trypanosomes. Trends Parasitol. 28, 66–72.
Woreta, T.A. & Alqahtani, SA. (2014). Evaluation of abnormal liver tests. Med Clin North Am. 98, 1–16.
Zamani, N. &, Hassanian-Moghaddam, H. (2018) Ingestion of Lead-Contaminated Packs of Opium. N Engl J Med. 379, 1861.
Metagegevens
Titel
Aminozuurmetabolisme
Auteur
Prof. dr. F.C. Schuit
Copyright
2019
Uitgeverij
Bohn Stafleu van Loghum
Boek
Leerboek metabolisme en voeding

Print ISBN: 978-90-368-2357-9

Elektronisch ISBN: 978-90-368-2358-6

Copyright: 2019

DOI
https://doi.org/10.1007/978-90-368-2358-6_9