Amino Acids and the Mitochondria
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This chapter describes some of the important physiological functions of amino acids in the mitochondria and the alterations caused by specific pathologies. To some extent all of the featured items are dependent upon the movement of amino acids across the highly selective permeability barrier that is the inner mitochondrial membrane. The performance of this transport by specific carriers is the subject of the first section. Once inside the mitochondrial matrix the amino acids become involved in a bewildering number of critical metabolic pathways. The second section elaborates on two of the most significant namely: the malateaspartate shuttle essential for the transfer of reducing equivalents between the cytoplasm and the mitochondria; and the urea cycle, which is responsible for maintaining sub-toxic levels of ammonia. The final section covers the changes to mitochondrial amino acid metabolism that occur under different pathological conditions. In this case three examples have been chosen comprising ischemiareperfusion in heart, myocardial hypertrophy and the special relationship that exists between glutamine and cancer cells.
KeywordsUrea Cycle Excitatory Amino Acid Transporter Cardiac Mitochondrion Argininosuccinate Synthetase Amino Acid Carrier
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- Baggio R, Emig FA, Christianson DW, Ash DE, Chakdar S, Rattan S (1999) Biochemical and functional profile of a newly developed potent and isozyme-selective arginase inhibitor. J Pharmacol Exp Therapeut 290:1409–1416Google Scholar
- Borst P (1963) Hydrogen transport and transport metabolisms. In Karlson, P. (ed.), Functionelle und Morphologische Organisation der Zelle, Springer-Verlag, Berlin, pp. 137–158Google Scholar
- Haas GS, DeBoer LWV, O’Keefe DD, Bodenhamer RM, Geffin MB, Drop LJ, Teplick RS, Daggett WM (1984) Reduction of postischemic myocardial dysfunction by substrate repletion during reperfusion. Circ 70(suppl I):I-65–I73Google Scholar
- Mathews CK, Van Holde KE (1990) Biochemistry. Benjamin Cummings Publishing Company, Redwood City, CaliforniaGoogle Scholar
- Queseda AR, Sánchez-Jiménez F, Perez-Rodriguez J, Márquez J, Medina MA, Núñez de Castro I (1988) Purification of phosphate-dependent glutaminase from isolated mitochondria of Ehrlich ascites tumor cells. Biochem J 255:1031–1036Google Scholar
- Ralphe JC, Bedell K, Segar JL, Scholz TD (2005) Correlation between myocardial malate/aspartate shuttle activity and EAAT1 protein expression in hyper- and hypothyroidism. Am J Physiol. 288:H2521–H2526Google Scholar
- Valdares JRE, Singhai RL, Parulekar MR, Beznak M (1969) Influence of aortic coarctation on myocardial glucose-6-phosphate dehydrogenase. Can J Physiol Pharmacol47:388–391Google Scholar
- Yasuda T, Yamaguchi N, Kobayashi K, Nishi I, Horinouchi H, Jalil A, Li MX, Ushikai M, Lijima M, Kondo I, Saheki T (2000) Identification of two novel mutations in the SLC25A13 gene and detection of seven mutations in 102 patients with adult-onset type II citrullinaemia. Hum Genet 107:537–545CrossRefPubMedGoogle Scholar