Diabetes mellitus (DM) is a chronic disease caused by disorder of insulin secretion in pancreatic β-cells, and/or its effect in tissues. Insulin acts to lower blood glucose by stimulation of glucose transport to muscle and fat cells and inhibition of its generation in the liver. Insulin promotes storage of the polysaccharide glycogen in the liver and muscles and stimulates glycogen synthesis.
Classification of DM is based on etiopathogenic mechanisms. Type 1 (characterized by β-cell destruction), type 2 (resistance to insulin action), other specific forms (mitochondrial DM included) and pregnancy diabetes.
Chronic hyperglycemia destroys many organs: eyes, kidneys, nervous tissue, heart and blood vessels. These changes are manifested as chronic diabetic complications.
Insulin deficiency and resistance to insulin action lead not only to changes in the metabolism of saccharides but also of proteins and lipids. The main pathobiochemical mechanisms of these changes are: (a) glycation of proteins, lipids, lipoproteins and DNA, (b) oxidative stress induced by hyperglycemia, (c) elevated flux via polyolic metabolic pathway of glucose, (d) changes linked with insulin signal pathway.
Abnormalities in metabolism which are typical for DM influence also functions of mitochondria. Disbalance between oxidative and reductive forms of supporting redox system create conditions for dysfunction of terminal oxidation. Mitochondria are assumed to be the key location for free radical generation because of the higher potential of reduced forms in this system (NADH). There is also a correlation between lower respiratory function of mitochondria and glycation of proteins in Complex II in the respiratory chain.
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References
Alberti KG, Zimmet PY (1998) Definition, diagnosis and classification of diabetes mellitus and its complications. Part 1: diagnosis and classification of diabetes mellitus; provisional report of a WHO consultation. Diabet Med 15:539–553
Baynes JW (1991) Role of oxidative stress in development of complications in diabetes. Diabetes 40:205–212
Baynes JW, Thorpe SR, Alderson NA, Chachich ME, Metz TO (2003) Pyridoxamine inhibits chemical modification of proteins by lipids in obese and diabetic rats: mechanism of action of pyridoxamine. In: Abstracts of the 18th International Diabetes Federation Congress, Paris, 24–29 August 2003
Beck-Nielsen H (1997) Clinical disorders of insulin resistance. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 531–550
Bennetd PH, Bogardus C, Tuomilehto J, Zimmet P (1997) Epidemiology and natural history of NIDDM: Non–obese and obese. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 147–176
Bierhaus A, Hofmann MA, Ziegler R, Nawroth PP (1998) AGEs and their interaction with AGE-receptors in vascular disease and diabetes mellitus; the AGE concept. Cardiovas Res 37:586–600
Borch-Johnsen K, Deckert T (1997) Complications of diabetes. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 2. Wiley, New York, pp 1213–1222
Brownlee M (1994) Glycation and diabetic complications. Diabetes 43:836–841
Brownlee M., Vlassara H., Kooney A, Ulrich P, Cerami A (1986) Aminoguanidine prevents diabetes-induced arterial wall protein cross-linking. Science 232(4758):1629–1632
Bucala R, Makita Z, Koschinsky T, Cerami A, Vlassara H (1993) Lipid advanced glycosylation: pathway for lipid oxidation in vivo. Proc Natl Acad Sci USA 90:6434–6438
Bucala R, Cerami A (1996) DNA-advanced glycosylation. In: Ikan R (ed.) The Maillard Reaction /Consequences for the Chemical and Life Sciences. Wiley, New York
Carnevale Schianca GP, Rossi A, Sainaghi PP, Maduli E, Bartoli E (2003) The significance of impaired fasting glucose vs. impaired glucose tolerance: importance of insulin secretion and resistance. Diabetic Care 26:1333–1337
Coletta A, Amiconi G, Bellelli A, Bertollini A, Čársky J, Castagnola M, Condo S, Brunori M (1988) Alteration of T-state binding properties of naturally glycated hemoglobin HbA1c. J Mol Biol 203:233–239
Coughlan MT, Thorburn DR, Fukami K, Laskowski A, Thallas-Bonke V, Long DM, Brownlee M, Cooper ME, Forbes JM (2005) Renal intra-mitochondrial glycation drives deficiencies in the activity of manganase superoxide dismutase and complex I of the mitochondrial respiratory chain in diabetes. In: Abstracts of the 41st EASD Annual Meeting, Athens, 10–15 September 2005
Čársky J (1999) Vol’né radikály a diabetes mellitus. In: Ďuračková Z, Bergendi L’, Čársky J (eds) Vol’né radikály a antioxidanty v medicíne (II) Slovak Academic Press Bratislava (Free radicals and diabetes mellitus. In: Free Radicals and Antioxidants in Medicine. III. In Slovak)
Ditzel J, Anderson H, peters ND (1975) Oxygen affinity of hemoglobin and red cell 2, 3-diphosphoglycerate in childhood diabetes. Acta Pediatr Scand 64:355–361
Dotta F, Eisenbarth G (1997) Aethiopathogenesis of type 1 diabetes in western society. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 107–127
Dyer DG, Dunn JE, Thorpe SR, Bailie KE, Lyons TJ, McCance DR, Baynes JW (1993) Accumulation of Maillard reaction products in skin collagen in diabetes and aging. J Clin Invest 91:2463–2469
Edelstein E, Brownlee M (1992) Mechanistic studies of advanced glycosylation end product inhibition by aminoguanidine. Diabetes 41:26–29
Ekoe JM (1997) Epidemiology and Etiopathogenesis of IDDM in other ethnic groups. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 129–146
Ferranini E, DeFronzo RA (1997) Insulin action in vivo: glucose metabolism. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 409–438
Forbes JM, Coughlan MT, Fukami K, Laskowski A, Thallas-Bonke V, Dinh D, Long DM, Brownlee M, Cooper ME, Thorburn DR (2005) Do extracellular (circulating or dietary) advanced glycation end products mediate mitochondrial dysfunction in the kidney. In: Abstracts of the 41st EASD Annual Meeting, Athens, 10–15 September 2005
Fu MX, Baynes JW (1994) Glycation, glycooxidation and cross-linking of collagen by glucose kinetics, mechanism and inhibition of late stages of the Maillard reaction. Diabetes 43:676–683
Fulcher GR, Walker M, Alberti KGMM (1997) The assessment of insulin action in vivo. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 513–529
Gašperíková D, Šeböková, Klimeš I (2004) Mitochondriálna DNA a diabetes. In: Kreze A, Langer P, Klimeš I, Stárka L, Payer J, Michálek J (eds) Všeobecná a klinická endokrinológia. Academic Electronic Press, Bratislava, pp 620–623 (Mitochodrial DNA and diabetes. In: General and Clinical Endocrinology. In Slovak)
Harris MI, Zimmet P (1997) Classification of diabetes mellitus and other categories of glucose intolerance. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 3–18
Hunt JV, Wolf SP (1991) Oxidative glycation and free radical production: a causal mechanism of diabetic complications. Free Radic Res Commun 12–13(1):115–123
Idris I, Gray S, Donnelly R (2001) Protein kinase C activation: isozyme-specific effects on metabolism and cardiovascular complications in diabetes. Diabetologia 44:659–673
Jain SK, Lim G (2001) Pyridoxine and pyridoxamine inhibits superoxide radicals and prevents lipid peroxidation, protein glycosylation and (Na +, K+)-ATP-ase activity reduction in high glucose-treated human erythrocytes. Free Radic Biol Med 30:232–237
Jakuš V, Hrnčiarová M, Čársky J, Krahulec B, Riedbrock N (1999) Inhibition of nonenzymatic protein glycation and lipid peroxidation by drugs with antioxidative activity. Life Sci 65:1991–1993
Keen H (1997) Diabetes Diagnosis. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 19–33
Kishimoto M, Hashiramoto M, Araki S, Ishida Y, Kazummi T, Kanda E, Kasuga M (1995) Diabetes mellitus carrying a mutation in the mitochondrial tRNA (Leu(UUR) ) gene. Diabetologia 38:193–200
Klimeš I, Šeböková E, Tkáč I (2004) Metabolický syndróm. In: Kreze A, Langer P, Klimeš I, Stárka L, Payer J, Michálek J (eds) Všeobecná a klinická endokrinológia. Academic Electronic Press, Bratislava, pp 610–613 (The metabolic syndrome. In: Genenral and Clinical Endocrinology. In Slovak)
Lee HK (2005) Mitochondria in diabetes mellitus. In: Berdanier CD (ed.) Mitochodria in Health and Disease. CRC Press, Taylor & Francis p 619
Lee AT, Cerami A (1989) Nonenzymatic glycosylation of DNA by reducing sugars. In. Baynes JW, Monnier VM (eds) Progress in Clinical and Biological Research, Vol. 304. Alan R Liss, New York
Lomezi M, Montisano DF, Toledo S, Barrieux A (1986) High glucose and DNA damage in endothelial cells. J Clin Invest 77:322–325
Maasen JA, Hart LM, van Essen E (2004) Mitochondrial diabetes molecular mechanism and clinical presentation. Diabetes 53(Suppl 1):103–109
Makita Z, Vlassara H, Rayfield E, Cartwright K, Friedman E, Rodby R, Cerami A, Bucala R (1992) Hemoglobin-AGE: Circulating marker of advanced glycosylation. Science 258:651–653
Martinka E (2004) Patogenéza diabetes mellitus 1. typu. In: Kreze A, Langer P, Klimeš I, Stárka L, Payer J, Michálek J (eds) Všeobecná a klinická endokrinológia. Academic Electronic Press, Bratislava, pp 610–613 (Pathogenesis of diabetes mellitus type I. In: General and Clinical Endocrinology. In Slovak)
Muchová J, Liptáková A, Országová Z, Garaiová I, Tisoň P, Čársky J, Ďuračková Z (1999) Antioxidant system in polymorphonuclear leukocytes of type 2 diabetes mellitus. Diabet Med 16:74–78
Muchová J, Liptáková A, Országová Z, Garaiová I, Tisoň P, Čársky J, Ďuračková Z (1999) Antioxidant system in polymorphonuclear leukocytes of type 2 diabetes mellitus. Diabet Med 16:74–78
Nagaraj RH, Prabhakaram M, Ortwerth BJ, Monnier VM (1994) Suppression of pentosidine formation in galactosaemic rat lens by an inhibitor of aldose reductase. Diabetes 43:580–586
Niwa T, Katsuzaki T, Miyazaki S, Miyazaki T, Ishizaki Y, Hayase F, Tatemichi N, Takei Y (1997) Immunohistochemical detection of imidazolone, a novel advanced glycation end product, in kidney and aortas of diabetic patients. J Clin Invest 99:1272–1280
Njoroge FG, Monnier VM (1989) The chemisttry of the Maillard reaction under physiological conditions: a revue. In: Baynes JW, Monnier VM (ed.) The Maillard Reaction in Aging, Diabetes and Nutrition. Alan R Liss, New York
Obrosova IG, Minchenko AG, Vasupuram R, White L, Abatan OI, Kumagai AK, Frank RN, Stevens MJ (2003) Aldose reductase inhibitor fidarestat prevents retinal oxidative stress and vascular endothelial growth factor overexpression in streptozotocin-diabetic rats. Diabetes 52:864–871
Person B, Hanson U, Lunell N-O (1997) Diabetes mellitus and pregnacy. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 2. Wiley, New York, pp 1085–1102
Peters AL, Davidson MB (1997) Aging and diabetes. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 2. Wiley, New York, pp 1103–1128
Petersen KF, Befroy D, Dufour S, Dziura J, Ariyan C, Rothman DL, DiPietro L, Cline GW, Shulman GI (2003) Mitochondrial dysfunction in the eldery: possible role in insulin resistance. Science 300:1140–1142
Průhová Š, Lebl J (2004) MODY Maturity onset diabetes of the young. In: Kreze A, Langer P, Klimeš I, Stárka L, Payer J, Michálek J (eds) Všeobecná a klinická endokrinológia. Academic Electronic Press, Bratislava, pp 614–619 (In: General Sand Clinical Endocrinology.)
Rabini RA, Galassi R, Staffolani R, Vasta M, Furnelli P, Mazzanti L (1993) Alterations in Na+, K+-ATPase activity and fluidity of erythrocyte membranes from relatives of insulin dependent diabetic patients. Diab Res 22:33–40
Rácz O, Šipulová A (2004) Patogenéza chronickych komplikácií. In: Kreze A, Langer P, Klimeš I, Stárka L, Payer J, Michálek J (eds) Všeobecná a klinická endokrinológia. Academic Electronic Press, Bratislava, pp 654–660. (Pathogenesis of chronic complications. In: General and Clinical Endocrinology. In Slovak)
Rahbar S, Yernini KK, Scott S, Gonzales N, Lalezari I (1999) Novel inhibitors of advanced glycation endproducts. Biochem Biophys Res Commun 262:651–656
Raskin P, Rosenstock J (1997) The genesis of diabetes complication: blood glucose and genetic susceptibility. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 2. Wiley, New York, pp 1225–1244
Requena JR, Ahmed MU, Fountain CW, Degenhardt TP, Reddy S, Perey C, Lyons TJ, Jenkins AJ, Baynes JW, Thorpe SR (1997) Carboxymetylethanolamine, a biomarker of phospholipid modification during the Maillard reaction in vivo. J Biol Chem 272(28):17473–17479
Rosca MG, Mustata TG, Kinter MT, Ozdemir AM, Kern TS, Szweda LI, Brownlee M, Monnier VM, Weiss MF (2005) Glycation of mitochondrial proteins from diabetic rat kidney is associated with excess superoxide formation. Am J Physiol Renal Physiol 289(2): 420–430
Sajithlal GB, Chithra P, Chandrakasan G (1998) The role of metal-catalyzed oxidation in the formation of advanced glycation end products: an in vitro study on collagen. Free Radic Biol Med 25:265–269
Sakurai T, Kimura S, Nakano M, kimura H (1991) Oxidative modification of glycated low density lipoprotein in the presence of iron. Biochem Biophys Res Commun 177:433–439
Schmidt AM, Hori O, Cao R, Yan SD, Brett j, Wautier JL, Ogawa S, Kuwabara K, Matsumoto M, Stern D (1996) RAGE a novel cellular receptor for advanced glycation end products. Diabetes 45:77–80
Simonson DC, Ronetti L, Giaccari A, DeFronzo RA (1997) Glucose toxicity. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 635–667
Singh R, Barden A, Mori T, Beilin L (2001) Advanced glycation end-products: a review. Diabetologia 44:126–129
Suzuki S, Hinokio Y, Hirai S, Onoda M, Matsumoto M, Kawasaki H, Satoh Y, Akai H, Abe K (1994) Pancreatic β-cell secretory defect associated with mitochondrial point mutation of the tRNA (LEU(UUR) ) gene: a study in seven families with mitochondrial encephalomyopathy, lactic acidosis and stroke-like episodes (MELAS). Diabetologia 37:818–825
Taguchi T, Sugiura M, Hamada Y, Miwa I (1999) Inhibition of advanced protein glycation by a Schiff base between aminoguanidine and pyridoxal. Eur J Pharmacol 378:283–289
Taniguchi N, Kinoshita N, Arai K, Iizuka S, Usui M, Naito K (1989) Inactivation of erythrocyte Cu-Zn-superoxide dismutase through nonenzymatic glycosylation. In: Baynes JW Monnier VM (eds) Progress in Clinical and Biological Research, Vol. 304. Alan R Liss, New York
Thorsby E, Ronningen KS (1992) Role of HLA genes in predisposition to develop insulin-dependent diabetes mellitus. Ann Med 24:523–531
Thornalley P (1999) The clinical significance of glycation. Clin Lab 45:263–273
Tošerová E (2004) Gravidita a diabetes. In: Kreze A, Langer P, Klimeš I, Stárka L, Payer J, Michálek J (eds) Všeobecná a klinická endokrinológia. Academic Electronic Press, Bratislava, pp 719–725 (Pregnancy and diabetes. In: General and Clinical Endocrinology. In Slovak)
Tull E, LaPorte RE (1997) Epidemiology of insulin dependent diabetes mellitus: Aproaches to study. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 99–105
Vadheim CM, Rotter JI (1997) Genetics of diabetes mellitus. In: Alberti KGMM, DeFronzo RA, Keen H, Zimmet P (eds) International Textbook of Diabetes Mellitus, Vol. 1. Wiley, New York, pp 31–98
Vertommen J, Van den Enden M, De Leeuw I (1994) Flavonoid treatment reduces glycation and lipid peroxidation in experimental diabetic rats. Phytother Res 8:430–432
Vozár J (2004) História klasifikácia a diagnostika diabetu. In: Kréze A, Langer P, Klimeš I, Stárka L, Payer J, Michálek J (eds) Všeobecná a klinická endokrinológia. Academic Electronic Press, Bratislava, pp 567–576 (History, classification and diagnosis of diabetes. In: General and Clinical Endocrinology. In Slovak.)
Waczuliková I, Ziegelhoffer A, Országová Z, Čársky J (2002) Fluidising effect of resorcylidene aminoguanidine on sarcolemmal membranes in streptozotocin-diabetic rats: blunted adaptation of diabetic myocardium to Ca2+ overload. J Physiol Pharmacol 53:727–739
Wels-Knecht KJ, Zyzak DV, Litchfield JF, Thorpe SR, Baynes JW (1995) Mechanism of autooxidative glycosylation – identification of glyoxal and arabinose as intermediates in the autooxidative modification of proteins by glucose. Biochemistry 34:3702–3709
Wolff SP (1996) Free radicals and glycation theory. In: Ikan R (ed.) The Maillard Reaction (Consequences for the Chemical and Life Sciences). Wiley, New York, pp 74–88
Wolff SP, Yang ZY, Hunt JV (1991) Protein glycation and oxidative stress in diabetes mellitus and aging. Free Radic Biol Med 10:339–352
Yan SD, Stern D, Schmidt AM (1997) What’s the RAGE? The receptor for advanced glycation end products (RAGE) and the dark side of glucose. Eur J Clin Invest 27:179–181
References
Dias AS, Porawski M, Alonso M, Morroni N, Collado PS, Gonzales-Gallego J (2005) Quercetin decreases oxidative stress, NF-kB activation, and iNOS overexpression in liver of streptozotocin-induced diabetic rats. J Nutr 135:2299–2304
Green K, Brand MD, Murphy MP (2004) Prevention of mitochondrial oxidative damage as a therapeutic strategy in diabetes. Diabetes (Suppl 1):S110–S118
Gvozdjáková A, Kucharská J, Braunová Z, Kolesár P (1998) Beneficial effect of CoQ10 on the antioxidative status and metabolism of fats and sugars in diabetics patients. First Conference of the International Coenzyme Q 10 Association, Boston, 21–24 May 1998, abtract book pp 95–97
Gvozdjáková A, Kucharská J, Sumbalová Z, Zaušková P, Mlynárik V, Bystrický P, Uličná O, Vančová O, Singh RB (2002) Can coenzyme Q10 and omega-3 fatty acids protect damaged function of brain and heart mitochondria in diabetic rats? Third Conference of the International Coenzyme Q 10 Association, London, UK, 22–24 November 2002, abstract book pp 109–111
Gvozdjáková A, Kucharská J, Sumbalová Z, Uličná O, Vančová O, Božek P, Singh RB (2005) Coenzyme Q10 and omega-3-polyunsaturated fatty acids protect heart and brain mitochondria in diabetes. Mitochondrion 5(3):226–227. Mitochondrial Medicine, St. Louis, 14–19 June 2005
Inui K, Fukushima H, Tsakamato H et al. (1992) Mitochondrial encephalomyopathies with the mutation of the tRNA Leu(UUR) gene. J Pediatr 120:62–66
Kristal BS, Jackson CT, Chung H-Y, Matsuda M, Nguyen HD, Yu BP (1997) Defects at center P underlie diabetes-associated mitochondrial dysfunction. Free Radic Biol Med 22(5):823–833
Kucharská J, Braunová Z, Uličná O, Zlatoš L, Gvozdjáková A (2000) Deficit of coenyzme Q in heart and liver mitochondria of rats with streptozotocin-induced diabetes. Physiol Res 49:411–418
Maechler P, Wollheim CB (2001) Mitochondrial function in normal and diabetic beta-cells. Nature 414(6865):807–812
Mohan IK, Das UN (2000) Effect of L-arginine-nitric oxide system on the metabolism of essential fatty acids in chemically induced diabetes mellitus. Prostaglandins Leucot Essent Fatty Acids 62(1):35–46
Niaudet P, Rotig A (1997) The kidney in mitochondrial cytopathies. Kidney Int 51:1000–1007
Santos DL, Palmiera CM, Seica R, Dias J, Mesquita J, Moreno AJ, Santos MS (2003) Diabetes and mitochondrial oxidative stress: a study using heart mitochondria from the diabetic Goto-Kakizaki rat. Mol Cell Biochem 246(1–2):163–170
Sumbalová Z, Kucharská J, Kašparová S, Mlynárik V, Bystrický P, Božek P, Uličná O, Vančová O, Singh RB, Gvozdjáková A (2005) Brain energy metabolism in experimental chronic diabetes: effect of long-term administration of coenzyme Q10 and ω-3 polyunsaturated fatty acids. Biologia 60(Suppl 17):105–108
Ziefelhoffer A, Ravingerová T, Waczulíková I, Barančík M, Ferko M, Gvozdjáková A, Strnisková M, Šimončíková P (2004) Sarcolemma to mitochondria crosstalk in the diabetic heart: endogenous protection of cell energetics. J Mol Cell Cardiol 36:772–773
References
Gvozdjáková A, Kucharská J, Cornélissen G, Mikulecký M, Singh RB, Halberg F (2004) Variations in cardiac mitochondrial coenzyme Q10 and oxidative phosphorylation. Int J Cardiol 97, Suppl 2, S15. The 3rd International Congress on Cardiovascular Disease, Thaiwan, Taipei, November 26–28, 2004
Gvozdjáková A, Kucharská J, Cornélissen G, Mikulecký M, Singh RB, Halberg F (2005) Fourth Conference of the International Coenzyme Q 10 Association, Los Angeles, April 14–17, Abstract Book: 113–115
Gvozdjáková A, Kucharská J, Cornélissen G, Mikulecký M, Singh RB, Halberg F (2005) Heart mitochondrial coenzyme “Q10-chronome” and variations of oxidative phosphorylation in diabetic rats. Mitochondrial Medicine 2005, St. Louis, USA, June 14–19. Mitochondrion, 2005, 5/3:226–227
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Čársky, J., Gvozdjáková, A., Mikulecký, M., Kucharská, J., Singh, R.B. (2008). Mitochondrial Diabetology. In: Gvozdjáková, A. (eds) Mitochondrial Medicine. Springer, Dordrecht. https://doi.org/10.1007/978-1-4020-6714-3_8
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