The dual face of endogenous α-aminoketones: Pro-oxidizing metabolic weapons

Comparative Biochemistry and Physiology - C Toxicology and Pharmacology

Volumn 146, Issue 1-2 SPEC. ISS., 2007, Pages 88-110

  Bechara, Etelvino J H ^a   Dutra, Fernando ^b   Cardoso, Vanessa E S ^a   Sartori, Adriano ^a   Olympio, Kelly P K ^a   Penatti, Carlos A A ^c   Adhikari, Avishek ^d   Assunção, Nilson A ^a  

^a UNIVERSITY OF SÃO PAULO   (Brazil)

^b UNIVERSIDADE CRUZEIRO DO SUL   (Brazil)

^c DARTMOUTH MEDICAL SCHOOL   (United States)

^d Och Spine at New York Presbyterian Hospitals   (United States)

Author keywords

5 aminolevulinic acid; Amino acid metabolism; Aminoacetone; Cri du chat syndrome; Diabetes; Hexosamines; Oxidative stress; Porphyrias

Indexed keywords

3 OXOACID COENZYME A TRANSFERASE; 4,5 DIOXOVALERIC ACID; ACETONE; ALDEHYDE DERIVATIVE; ALPHA AMINOKETONE DERIVATIVE; ALPHA OXOALDEHYDE DERIVATIVE; AMINO ACID DERIVATIVE; AMINOLEVULINIC ACID; CARBONYL DERIVATIVE; CERULOPLASMIN; COPPER; DNA; FERRITIN; GABAERGIC RECEPTOR AFFECTING AGENT; GLYCINE; HEXOSAMINE; HEXOSE; IRON; KETONE DERIVATIVE; METHYLGLYOXAL; SCAVENGER; THREONINE; UNCLASSIFIED DRUG; VALERIC ACID DERIVATIVE;

BIOSYNTHESIS; CAT CRY SYNDROME; CROSS LINKING; DIABETES MELLITUS; HUMAN; IN VITRO SELECTION; LEAD POISONING; NONHUMAN; OXIDATION; OXIDATIVE STRESS; POLYMERIZATION; PORPHYRIA; PRIORITY JOURNAL; PROTEIN STRUCTURE; REVIEW; SYNAPTOSOME;

ANIMALIA; OCTOPUS; PHASIANIDAE; RATTUS;

EID: 34447296740     PISSN: 15320456     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpc.2006.07.004     Document Type: Review

References (255)

1. Abordo E.A., Harjit S.M., and Thornalley P.J. Accumulation of alpha-oxoaldehydes during oxidative stress: a role in cytotoxicity. Biochem. Pharmacol. 58 (1999) 641-648
2. Ackroyd R., Brown N., Vernon D., Roberts D., Stephenson T., Marcus S., Stoddard C., and Reed M. 5-aminolevulinic acid photosensitization of dysplastic Barrett's esophagus: a pharmacokinetic study. Photochem. Photobiol. 70 (1999) 656-662
3. Adam W. Determination of chemiexcitation yields in the thermal generation of electronic excitation from 1,2-dioxetane. In: Adam W., and Cilento G. (Eds). Chemical and Biological Generation of Excited States (1982), Academic Press, New York 115-152
4. Ahmed M.U., Frye E.B., Degenhardt T.P., Thorpe S.R., and Baynes J.W. N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem. J. 324 (1997) 565-570
5. Ahmed N., Babaei-Jadidi R., Howell S.K., Thornalley P.J., and Beisswenger P.J. Glycated and oxidized protein degradation products are indicators of fasting and postprandial hyperglycemia in diabetes. Diabetes Care 28 (2005) 2465-2471
6. Akagi S., and Ohmori S. Threonine is the best substrate for d-lactate formation in octopus tentacle. Amino Acids 26 (2004) 169-174
7. Akagi S., Sato K., and Ohmori S. Threonine metabolism in Japanese quail liver. Amino Acids 26 (2004) 235-242
8. Akaike T. Mechanisms of biological S-nitrosation and its measurement. Free Radic. Res. 33 (2000) 461-469
9. α-CBZ-Lysine by methylglyoxal. Bioorg. Med. Chem. Lett. 6 (1996) 1577-1578
10. Anello M., Rabuazzo A.M., Degano C., Caltabiano V., Patané G., Vigneri R., and Purrello F. Fast reversibility of glucose-induced desensitization in rat pancreatic islets. Evidence for an involvement of ionic fluxes. Diabetes 45 (1996) 502-506
11. Anzil A.P., and Dozic S. Peripheral nerve changes in porphyric neuropathy: findings in a sural nerve biopsy. Acta Neuropathol. 42 (1978) 121-126
12. Astrup A., Meinert Larsen T., and Harper A. Atkins and other low-carbohydrate diets: hoax or an effective tool for weight loss?. Lancet 364 (2004) 897-899
13. Atkins T.W., and Thornalley P.J. Erythrocyte glyoxalase activity in genetically obese (ob/ob) and streptozotocin diabetic mice. Diabetes Res. 11 (1989) 125-129
14. Avkin-Burns N., Laegeler A., Kellogg G., and Ercal N. Oxidative effects of lead in young and adult Fisher 344 rats. Arch. Environ. Contam. Toxicol. 44 (2003) 417-420
15. Ayoub F.M., Allen R.E., and Thornalley P.J. Inhibition of proliferation of human leukaemia 60 cells by methylglyoxal in vitro. Leuk. Res. 17 (1993) 397-401
16. Baader W.J., Bohne C., Cilento G., and Dunford H.B. Peroxidase-catalyzed formation of triplet acetone: chemiluminescence form isobutyraldehyde and oxygen. J. Biol. Chem. 260 (1985) 10217-10225
17. Baatrup E. Structural and functional effects of heavy metals on the nervous system, including sense organs of fish. Comp. Biochem. Physiol. C, Comp. Pharmacol. Toxicol. 100 (1991) 253-257
18. Babilas P., Karrer S., Sidoroff A., Landthaler M., and Szeimies R.M. Photodynamic therapy in dermatology - an update. Photodermatol. Photoimmunol. Photomed. 21 (2005) 142-149
19. Balu N., Gamcsik M.P., Colvin M.E., Colvin O.M., Dolan M.E., and Ludeman S.M. Modified guanines representing O(6)-alkylation by the cyclophosphamide metabolites acrolein and chloroacetaldehyde: synthesis, stability, and ab initio studies. Chem. Res. Toxicol. 15 (2002) 380-387
20. Baynes J.W. Role of oxidative stress in development of complications in diabetes. Diabetes 40 (1991) 405-412
21. Bechara E.J.H. A free radical hypothesis for porphyrias with 5-aminolevulinic acid overload. In: Davis K.J., and Ursini F. (Eds). The Oxygen Paradox (1995), CLEUP University Press, Padova 503-513
22. Bechara E.J.H. Oxidative stress in acute intermittent porphyria and lead poisoning may be triggered by 5-aminolevulinic acid. Braz. J. Med. Biol. Res. 29 (1996) 841-851
23. Bechara E.J.H., and Wilson T. Alkyl substituent effects on dioxetane properties. Tetraethyl-, dicyclohexylidene-, and 3,4-dimethyl-3,4-di-n-butyldioxetanes. A discussion of decomposition mechanism. J. Org. Chem. 45 (1980) 5261-5268
24. Bechara E.J.H., Oliveira O.M.M.F., Duran N., Baptista R.C., and Cilento G. Peroxidase catalyzed generation of triplet acetone. Photochem. Photobiol. 30 (1979) 101-110
25. Bechara E.J.H., Medeiros M.H.G., Monteiro H.P., Hermes-Lima M., Pereira B., Demasi M., Costa C.A., Abdalla D.S.P., Onuki J., Wendel C.M.A., and Mascio P. A free radical hypothesis of lead poisoning and inborn porphyrias associated with 5-aminolevulinic acid overload. Quim. Nova 16 (1993) 385-392
26. Bechara E.J.H., Medeiros M.H.G., Catalani L.H., Soares C.H.L., Monteiro H.P., Abdalla D.S.P., Christoff M., Hermes-Lima M., Pereira B., Demasi M., Nantes I.L., Costa C.A., Rocha M.E.M., Di Mascio P., Wendel C.M.A., Onuki J., Penatti C.A.A., and Pinto A.P. Enolizable carbonyl and imino metabolites may act as endogenous sources of reactive oxygen species. Ciênc. Cult. 47 (1995) 346-357
27. Becker D.M., and Kramer S. The neurological manifestations of porphyria: a review. Medicine 56 (1977) 411-423
28. Bekesi J.H., Bekesi E., and Winzler R.J. Inhibitory effect of d-glucosamine and other sugars on the biosynthesis of protein, ribonucleic acid, and deoxyribonucleic acid in normal and neoplastic tissues. J. Biol. Chem. 244 (1969) 3766-3772
29. Bellinger D.C. Lead. Pediatrics 113 (2004) 1016-1022
30. Beyer W.N., Dalgam J., Dudding S., French J.B., Mateo R., Miesner J., Sileo L., and Spann J.S. Zinc and lead poisoning in wild birds in the Tri-State Mining District (Oklahoma, Kansas, Missouri). Arch. Environ. Contam. Toxicol. 48 (2004) 108-117
31. Bird M.I., and Nunn P.B. Metabolic homoeostasis of l-threonine in the normally-fed rat. Importance of liver threonine dehydrogenase activity. Biochem. J. 214 (1983) 687-694
32. Biswas S., Ray M., Misra S., Dutta D.P., and Ray S. Selective inhibition of mitochondrial respiration and glycolysis in human leukaemic leucocytes by methylglyoxal. Biochem. J. 323 (1997) 343-348
33. Bolann B.J., and Ulvik R.J. Release of iron form ferrritin by xanthine oxidase. Role of the superoxide radical. Biochem. J. 243 (1987) 55-59
34. Boomsma F., Van Veldhuisen D.J., Kam P.J., in't Veld A.J.M., Mosterd A., Lie K.I., and Schalekamp M.A.D.H. Plasma semicarbazide-sensitive amine oxidase is elevated in patients with congestive heart failure. Cardiovasc. Res. 33 (1997) 387-391
35. Boomsma F., Van den Meiracker A.H., Winkel S., Aanstoot H.J., Batstra M.R., Veld A.J.M., and Bruining G.J. Circulating semicarbazide-sensitive amine oxidase is raised both in type I (insulin-dependent), in type II (non-insulin-dependent) diabetes mellitus and even in childhood type I diabetes at first clinical diagnosis. Diabetologia 42 (1999) 233-237
36. Boor P.J., Trent M.B., Lyles G.A., Tao M., and Ansari G.A.S. Methylamine metabolism to formaldehyde by vascular semicarbazide-sensitive amine oxidase. Toxicology 73 (1992) 251-258
37. Bourajjaj M., Stehouwer C.D., van Hinsbergh V.W., and Schalkwijk G.G. Role of methylglyoxal adducts in the development of vascular complications in diabetes mellitus. Biochem. Soc. Trans. 2003 (2003) 1400-1402
38. Boylan S.A., and Dekker E.E. l-threonine dehydrogenase. Purification and properties of the homogeneous enzyme from Escherichia coli K-12. J. Biol. Chem. 256 (1981) 1809-1815
39. Brennan M.J.W., and Cantrill R.C. δ-Aminolevulinic acid is a potent agonist for GABA autoreceptors. Nature 280 (1979) 514-515
40. Britton J.E., Goulden V., Stables G., Stringer M., and Sheehan-Dare R. Investigation of the use of the pulsed dye laser in the treatment of Bowen's disease using 5-aminolevulinic acid phototherapy. Br. J. Dermatol. 153 (2005) 780-784
41. Brownlee M. Biochemistry and molecular cell biology of diabetic complications. Nature 414 (2001) 813-820
42. Cadet J., Carvalho V.M., Onuki J., Douki T., Medeiros M.H., and Di Mascio P. Purine DNA adducts of 4,5-dioxovaleric acid and 2,4-decadienal. IARC Sci. Publ. 150 (1999) 103-113
43. Cadet J., Douki T., Pouget J.P., Ravanat J.L., Sauvaigo S., Teixeira P.C., Onuki J., Medeiros M.H.G., Bechara E.J.H., and Di Mascio P. In: Abdulla M., Bost M., Gamon S., Arnaud P., and Chazot G. (Eds). New Aspects of Trace Elements Research (1999), Smith-Gordon, London 163-167
44. Cameron N.E., Cotter M.A., Dines K., and Love A. Effects of aminoguanidine on peripheral nerve function and polyol pathway metabolites in streptozotocin-diabetic rats. Diabetologia 35 (1992) 946-950
45. Cameron N.E., Gibson T.M., Nangle M.R., and Cotter M.A. Inhibitors of advanced glycation end product formation and neurovascular dysfunction in experimental diabetes. Ann. N.Y. Acad. Sci. 1043 (2005) 784-792
46. Campfield L.A., Smith F.J., Guisez Y., Devos R., and Burn P. Recombinant mouse OB protein: evidence for a peripheral signal linking adiposity and central neural networks. Science 269 (1995) 546-549
47. Carvalho H., Bechara E.J.H., Meneghini R., and Demasi M. Haem precursor delta-aminolaevulinic acid induces activation of the cytosolic iron regulatory protein 1. Biochem. J. 328 (1997) 827-832
48. Casas A., Fukuda H., Di Venosa G., and Batlle A. Photosensitization and mechanism of cytotoxicity induced by the use of ALA derivatives in photodynamic therapy. Br. J. Cancer 85 (2001) 279-284
49. Cavanagh J.B., and Mellick R.S. On the nature of the peripheral nerve lesions associated with acute intermittent porphyria. J. Neurol. Neurosurg. Psychiatry 28 (1965) 320-327
50. Ceriello A. New insights on oxidative stress and diabetic complications may lead to a "causal" antioxidant therapy. Diabetes Care 26 (2003) 1589-1596
51. Chalmers J., and Lyles G.A. Aminoacetone metabolism by semicarbazide-sensitive amine oxidase in rat aorta. Biochem. Pharmacol. 49 (1995) 416-419
52. Chaplen F.W.R., Fahl W.E., and Cameron D.C. Evidence of high levels of methylglyoxal in cultured Chinese hamster ovary cells. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 5533-5538
53. Cheatham B. Enough is enough: nutrient sensors and insulin resistance. Endocrinology 145 (2004) 2115-2117
54. Chevion M., Navok T., Glaser G., and Mager J. The chemistry of favism-inducing compounds. The properties of isouramil and divicine and their reaction with glutathione. Eur. J. Biochem. 127 (1982) 405-409
55. Chisolm Jr. J.J. The road to primary prevention of lead toxicity in children. Pediatrics 107 (2001) 581-583
56. Cilento G. Excited electronic states in dark biological systems. Q. Rev. Biophys. 6 (1974) 485-501
57. Cilento G., and Adam W. From free radicals to electronically excited states. Free Radic. Biol. Med. 19 (1995) 103-114
58. Clark A.J., and Scheuhammer A.M. Lead poisoning in upland-foraging birds of prey in Canada. Ecotoxicology 12 (2003) 23-30
59. Cornish K.M., and Pigram J. Developmental and behavioural characteristics of cri du chat syndrome. Arch. Dis. Child. 75 (1996) 448-450
60. Costa C.A., Trivelato G.C., Pinto A.M.P., and Bechara E.J.H. Correlation between plasma 5-aminolevulinic acid concentrations and indicators of oxidative stress in lead-exposed workers. Clin. Chem. 43 (1997) 1196-1202
61. Costa C.A., Trivelato G.C., Demasi M., and Bechara E.J.H. Determination of 5-aminolevulinic acid in blood plasma, tissues and cell cultures by high-performance liquid chromatography with electrochemical detection. J. Chromatogr., B 695 (1997) 245-250
62. Dakin H.D., and Dudley H.W. An enzyme concerned with the formation of hydroxyl acids from ketonic aldehydes. J. Biol. Chem. 14 (1913) 155-157
63. Davis A.J., and Austic R.E. Dietary protein and amino acid levels alter threonine dehydrogenase activity in hepatic mitochondria of Gallus domesticus. J. Nutr. 127 (1997) 738-744
64. De Francisco N., Troya J.D.R., and Aguera E.I. Lead and lead toxicity in domestic and free living birds. Avian Pathol. 32 (2003) 3-13
65. Demasi M., Penatti C.A.A., DeLucia R., and Bechara E.J.H. The prooxidant effect of 5-aminolevulinic acid in the brain tissue of rats: implications in neuropsychiatric manifestations in porphyrias. Free Radic. Biol. Med. 20 (1996) 291-299
66. De Siervi A., Vazquez E.S., Rezaval C., Rossetti M.V., and del Batlle A.M. Delta-aminolevulinic acid cytotoxic effects on human hepatocarcinoma cell lines. BMC Cancer 2 (2002) 6-12
67. Dietrich K.N., Ris M.D., Succop P.A., Berger O.G., and Bornschein R.L. Early exposure to lead and juvenile delinquency. Neurotoxicol. Teratol. 23 (2001) 511-518
68. Douki T., Onuki J., Medeiros M.H., Bechara E.J.H., Cadet J., and Di Mascio P. DNA alkylation by 4,5-dioxovaleric acid, the final oxidation product of 5-aminolevulinic acid. Chem. Res. Toxicol. 11 (1998) 150-157
69. Duez P., Hanocq M., and Dubois J. Photodynamic DNA damage mediated by delta-aminolevulinic acid-induced porphyrins. Carcinogenesis 22 (2001) 771-778
70. Dutra F., Knudsen F.S., Curi D., and Bechara E.J.H. Aerobic oxidation of aminoacetone, a threonine catabolite: iron catalysis and coupled iron release from ferritin. Chem. Res. Toxicol. 14 (2001) 1323-1329
71. Dutra F., Araki D., and Bechara E.J.H. Aminoacetone induces loss of ferritin ferroxidase and iron uptake activities. Free Radic. Res. 37 (2003) 1113-1121
72. Dutra F., Ciriolo M., Calabrese L., and Bechara E.J.H. Aminoacetone induces oxidative modification to human plasma ceruloplasmin. Chem. Res. Toxicol. 18 (2005) 755-760
73. Dwivedi S.K., Swarup D., Dey S., and Patra R.C. Lead poisoning in cattle and buffalo near primary lead-zinc smelter in India. Vet. Hum. Toxicol. 43 (2001) 93-94
74. Eizirik D.L., Korbutt G.S., and Hellerstrom C. Prolonged exposure of human pancreatic islets to high glucose concentrations in vitro impairs the beta-cell function. J. Clin. Invest. 90 (1992) 1263-1268
75. Elliott W.H. Aminoacetone formation by Staphylococcus aureus. Biochem. J. 74 (1960) 478-485
76. Elliott W.H. The estimation of aminoacetone and δ-aminolevulinic acid. Biochem. J. 74 (1960) 90-94
77. Ercal N., Gurer-Orhan H., and Aykin-Burns N. Toxic metals and oxidative stress. Part I: mechanisms involved in metal-induced oxidative damage. Curr. Top. Med. Chem. 1 (2001) 529-539
78. Faure P., Troncy L., Lecomte M., Wiernsperger N., Lagarde M., Ruggiero D., and Halimi S. Albumin antioxidant capacity is modified by methylglyoxal. Diabetes Metab. 31 (2005) 169-177
79. Fernandez-Real J.M., Lopez-Bermejo A., and Ricart W. Cross-talk between iron metabolism and diabetes. Diabetes 51 (2002) 2348-2354
80. Foote C.S. Definition of type I and type II photosensitized oxidation. Photochem. Photobiol. 54 (1991) 659
81. Fraga C.G., Onuki J., Lucesoli F., Bechara E.J.H., and Di Mascio P. 5-Aminolevulinic acid mediates the in vivo and in vitro formation of 8-hydroxy-2′-deoxyguanosine in DNA. Carcinogenesis 15 (1994) 2241-2244
82. Fridovich I. Superoxide dismutase. In: Lennarz W.J., and Lane M.D. (Eds). Encyclopedia of Biological Chemistry (2004), Academic Press, USA 135-138
83. Fuchs J., Weber S., and Kaufmann R. Genotoxic potential of porphyrin type photosensitizers with particular emphasis on 5-aminolevulinic acid: implications for clinical photodynamic therapy. Free Radic. Biol. Med. 28 (2000) 537-548
84. Fujisawa T., Akagi S., Kawase M., Yamamoto M., and Ohmori S. d-lactate metabolism in starved Octopus ocellatus. J. Exp. Zool., A. Comp. Exp. Biol. 303 (2005) 489-496
85. Fukuda H., Casas A., and Batlle A. Aminolevulinic acid: from its unique biological function to its star role in photodynamic therapy. Int. J. Biochem. Cell Biol. 37 (2005) 272-276
86. Gerich J.E. The importance of tight glycemic control. Am. J. Med. 118 (2005) 7S-11S
87. Gerscher S., Connelly J.P., Beijersbergen Van Henegouwen G.M., MacRobert A.J., Watt P., and Rhodes L.E. A quantitative assessment of protoporphyrin IX metabolism and phototoxicity in human skin following dose-controlled delivery of the prodrugs 5-aminolaevulinic acid and 5-aminolaevulinic acid-n-pentylester. Br. J. Dermatol. 144 (2001) 983-990
88. Gibson J.B., and Goldberg A. The neuropathology of acute porphyria. J. Pathol. Bacteriol. 71 (1956) 495-509
89. Gibson K.D., Laver W.G., and Neuberger A. Initial stages in the biosynthesis of porphyrins. 2. The formation of delta-aminolaevulic acid from glycine and succinyl-coenzyme A by particles from chicken erythrocytes. Biochem. J. 70 (1958) 71-81
90. Gokturk C., Nilsson J., Nordquist J., Kristensson M., Svensson K., Soderberg C., Israelson M., Garpenstrand H., Sjoquist M., Oreland L., and Forsberg-Nilsson K. Overexpression of semicarbazide-sensitive amine oxidase in smooth muscle cells leads to an abnormal structure of the aortic elastic laminas. Am. J. Pathol. 163 (2003) 1921-1928
91. Gorchein A. Determination of delta-aminolaevulinic acid in biological fluids by gas-liquid chromatography with electron-capture detection. Biochem. J. 219 (1984) 883-889
92. Gubler J.G., Bargetzi M.J., and Meyer U.A. Primary liver carcinoma in two sisters with acute intermittent porphyria. Am. J. Med. 89 (1990) 540-541
93. Gurer H., and Ercal N. Can antioxidants be beneficial in the treatment of lead poisoning?. Free Radic. Biol. Med. 29 (2000) 927-945
94. Haik G.M., Lo T.W., and Thornalley P.J. Methylglyoxal concentration and glyoxalase activities in the human lens. Exp. Eye Res. 59 (1994) 497-500
95. Halliwell B., and Gutteridge J.M.C. Free Radicals in Biology and Medicine. 3rd ed. (1999), Oxford Science Publications, Oxford, UK
96. Hammes H.P. Pathophysiological mechanisms of diabetic angiopathy. J. Diabetes Its Complicat. 17 (2003) 16-19
97. Hammes H.P., Strodter D., Weiss A., Bretzel R.G., Federlin K., and Brownle M. Secondary intervention with aminoguanidine retards the progression of diabetic retinopathy in the rat model. Diabetologia 38 (1995) 656-660
98. Hazel M., Cooksey R.C., Jones D., Parker G., Neidigh J.L., Witherbee B., Gulve E.A., and McClain D.A. Activation of the hexosamine signaling pathway in adipose tissue results in decreased serum adiponectin and skeletal muscle insulin resistance. Endocrinology 145 (2004) 2118-2128
99. Hermes-Lima M., Pereira B., and Bechara E.J.H. Are free radicals involved in lead poisoning?. Xenobiotica 21 (1991) 1085-1090
100. Hermes-Lima M., Castilho R.F., Valle V.G.R., Bechara E.J.H., and Vercesi A.E. Calcium-dependent mitochondrial oxidative damage promoted by 5-aminolevulinic acid. Biochim. Biophys. Acta 1180 (1992) 201-206
101. Higurashi M., Oda M., Iijima K., Iijima S., Takeshita T., Watanabe N., and Yoneyama K. Livebirth prevalence and follow-up of malformation syndromes in 27,472 newborns. Brain Develop. 12 (1990) 770-773
102. Hindmarsh J.T. The porphyrias: recent advances. Clin. Chem. 32 (1986) 1255-1263
103. Hiraku Y., and Kawanishi S. Involvement of oxidative DNA damage and apoptosis in antitumor actions of aminosugars. Free Radic. Res. 31 (1999) 389-403
104. Hiraku Y., Sugimoto J., Yamaguchiand T., and Kawanishi S. Oxidative DNA damage induced by aminoacetone, an amino acid metabolite. Arch. Biochem. Biophys. 365 (1999) 62-70
105. House J.D., Hall B.N., and Brosnan J.T. Threonine metabolism in isolated rat hepatocytes. Am. J. Physiol: Endocrinol. Metab. 281 (2001) E1300-E1307
106. Hsu P.C., and Guo Y.L. Antioxidant nutrients and lead toxicity. Toxicology 180 (2002) 33-44
107. Hysmith R.M., and Boor P.J. Role of benzylamine oxidase in the cytotoxicity of allylamine toward aortic smooth muscle cells. Toxicology 51 (1988) 133-145
108. Israely I., Costa R.M., Xie C.W., Silva A.J., Kosik K.S., and Liu X. Deletion of the neuron-specific protein δ-catenin leads to severe cognitive and synaptic dysfunction. Curr. Biol. 14 (2004) 1657-1663
109. Kalapos M.P. Mechanisms leading to complications in diabetes mellitus: pathologiacl role of α-oxoaldehydes. Biochem. Educ. 20 (1992) 27-29
110. Kalapos M.P. Methylglyoxal toxicity in mammals. Toxicol. Lett. 73 (1994) 3-24
111. Kalapos M.P. Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implications. Toxicol. Lett. 110 (1999) 145-175
112. Kalapos M.P. On the promine/retine theory of cell division: now and then. Biochim. Biophys. Acta 1426 (1999) 1-16
113. Kalapos M.P., Littauer A., and de Groot H. Has reactive oxygen a role in methylglyoxal toxicity? A study on cultured rat hepatocytes. Arch. Toxicol. 67 (1993) 369-372
114. Kappas A., Sassa S., Galbraith R.A., and Nordmann Y. In: Scriver C. (Ed). The Metabolic Basis of Inherited Disease (1989), McGraw-Hill, New York 1305-1365
115. Kauppinen R. Porphyrias. Lancet 365 (2005) 241-252
116. Kazachkov M., and Yu P.H. A novel HPLC procedure for detection and quantification of aminoacetone, a precursor of methylglyoxal, in biological samples. J. Chromatogr., B. Analyt. Technol. Biomed. Life Sci. 824 (2005) 116-122
117. Kirstein M., Brett J., Radoff S., Ogawa S., Stern D., and Vlassara H. Advanced protein glycosylation induces transendothelial human monocyte chemotaxis and secretion of platelet-derived growth factor: role in vascular disease of diabetes and aging. Proc. Natl. Acad. Sci. U. S. A. 87 (1990) 9010-9014
118. Koller K., Brown T., Spurgeon A., and Levy L. Recent developments in low-level lead exposure and intellectual impairment in children. Environ. Health Perspect. 112 (2004) 987-994
119. Kopecky K.R., and Mumford C. Luminescence in the thermal decomposition of 3,3,4-trimethyl-1,2-dioxetane. Can. J. Chem. 47 (1969) 709-711
120. Kopman J.A., Kim D.M., Rahman S.S., Arandia J.A., Karimbux N.Y., and Fiorellini J.P. Modulating the effects of diabetes on osseointegration with aminoguanidine and doxycycline. J. Periodontol. 76 (2005) 614-620
121. Kovacic P., and Cooksy A.L. Role of diacetyl metabolite in alcohol toxicity and addiction via electron transfer and oxidative stress. Arch. Toxicol. 79 (2005) 123-128
122. 2+ ions. A proposed model for phosphate-stimulated lipid peroxidation. J. Biol. Chem. 271 (1995) 2929-2934
123. Kuhla B., Luth H.J., Haferburg D., Boeck K., Arendt T., and Munch G. Methylglyoxal, glyoxal, and their detoxification in Alzheimer's disease. Ann. N.Y. Acad. Sci. 1043 (2005) 211-216
124. Kuhner U., Busse M., and Buchinger G. Cri-du-chat syndrome with an increased level of proline and threonine. Z. Kinderheilkd. 117 (1974) 259-264
125. Laferrère B., García-Lorda P., Russell C.D., and Pi-Sunyer F.X. Effect of oral glucosamine sulfate on serum leptin levels in human subjects. Nutrition 20 (2004) 321-322
126. Lang K., Lehmann P., Bolsen K., Ruzicka T., and Fritsch C. Aminolevulinic acid: pharmacological profile and clinical indication. Expert Opin. Investig. Drugs 10 (2001) 1139-1156
127. Lee C., Yim M.B., Chock P.B., Yim H.S., and Kang S.O. Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation. J. Biol. Chem. 273 (1998) 25272-25278
128. Lejeune J., Lafourcade J., Berger R., Vialatte J., Boeswillwald M., Seringe P., and Turpin R. 3 cases of partial depletion of the short arm of a 5 chromosome. C. R. Acad. Sci. Paris 257 (1963) 3098-3102
129. Lejeune J., Rethore M.O., Peeters M., de Blois M.C., Rabier D., Parvy P., Bardet J., and Kamoun P. Cri-du-chat disease: plasma and urinary amino acids. Ann. Genet. 33 (1990) 16-20
130. Lewinsohn R. Amine oxidase in human blood vessels and non-vascular smooth muscle. J. Pharm. Pharmacol. 33 (1981) 569-575
131. Lewinsohn R. Mammalian monoamine-oxidizing enzymes, with special reference to benzylamine oxidase in human tissues. Braz. J. Med. Biol. Res. 17 (1984) 223-256
132. Lidsky T.I., and Schneider J.S. Lead neurotoxicity in children: basic mechanisms and clinical correlates. Brain 126 (2003) 5-19
133. Lindsley J.E., and Rutter J. Nutrient sensing and metabolic decisions. Comp. Biochem. Physiol., Part B Biochem. Mol. Biol. 139 (2004) 543-559
134. Lithner F., and Wetterberg L. Hepatocellular carcinoma in patients with acute intermittent porphyria. Acta Med. Scand. 215 (1984) 271-274
135. Lo T.W.C., Selwood T., and Thornalley P.J. The reaction of methylglyoxal with aminoguanidine under physiological conditions and prevention of methylglyoxal binding to plasma proteins. Biochem. Pharmacol. 48 (1994) 1865-1870
136. Luksiene Z., Eggen I., Moan J., Nesland J.M., and Peng Q. Evaluation of protoporphyrin IX production, phototoxicity and cell death pathway induced by hexylester of 5-aminolevulinic acid in Reh and HPB-ALL cells. Cancer Lett. 169 (2001) 33-99
137. Lyles G.A. Properties of mammalian tissue-bound semicarbazide-sensitive amine oxidase: possible clues to its physiological function?. J. Neural Transm., Suppl. 41 (1994) 387-396
138. Lyles G.A., and Mcdougall S.A. The enhanced daily excretion of urinary methylamine in rats treated with semicarbazide or hydralazine may be related to the inhibition of semicarbazide-sensitive amine oxidase activities. J. Pharm. Pharmacol. 41 (1989) 97-100
139. Mainardi P.C., Guala A., Pastore G., Pozzo G., Bricarelli F.D., and Pierluigi M. Psychomotor development in cri du chat syndrome. Clin. Genet. 57 (2000) 459-461
140. Marcus S.L., and McIntyre W.R. Photodynamic therapy systems and applications. Expert Opin. Emerg. Drugs 7 (2002) 321-334
141. Marshall S., Bacote V., and Traxinger R.R. Discovery of a metabolic pathway mediating glucose-induced desensitization of the glucose transport system. Role of hexosamine biosynthesis in the induction of insulin resistance. J. Biol. Chem. 266 (1991) 4706-4712
142. Martin Jr. J.P., and Batkoff B. Homogentisic acid autoxidation and oxygen radical generation: implications for the etiology of alkaptonuric arthritis. Free Radic. Biol. Med. 3 (1987) 241-250
143. Mashino T., and Fridovich I. Superoxide radical initiates the autoxidation of dihydroxyacetone. Arch. Biochem. Biophys. 254 (1987) 547-551
144. Mateo R., Beyer W.N., Spann J.W., and Hoffman D.J. Relation of fatty acid composition in lead-exposed mallards to fat mobilization, lipid peroxidation and alkaline phosphatase activity. Comp. Biochem. Physiol. C 135 (2003) 451-458
145. Matyus P., Dajka-Halasz B., Foldi A., Haider N., Barlocco D., and Magyar K. Semicarbazide-sensitive amine oxidase: current status and perspectives. Curr. Med. Chem. 11 (2004) 1285-1298
146. McClain D.A. Hexosamines as mediators of nutrient sensing and regulation in diabetes. J. Diabetes Its Complicat. 16 (2002) 72-80
147. McLellan A.C., Phillips S.A., and Thornalley P.J. The assay of methylglyoxal in biological systems by derivatization with 1,2-diamino-4,5-dimethoxybenzene. Anal. Biochem. 206 (1992) 17-23
148. Medeiros M.H.G., Marchiori P.E., and Bechara E.J.H. Superoxide dismutase, glutathione peroxidase and catalase activities in the erythrocytes of patients with intermittent acute porphyria. Clin. Chem. 28 (1982) 242
149. Memisogullari R., and Bakan E. Levels of ceruloplasmin, transferrin, and lipid peroxidation in the serum of patients with type 2 diabetes mellitus. J. Diabetes Its Complicat. 18 (2004) 193-197
150. Meretsky V.J., Snyder N.F.R., Beissinger S.R., Clendenen D.A., and Wiley J.W. Demography of the California Condor: implications for reestablishment. Conserv. Biol. 14 (2000) 957-967
151. Meyer U.A., Schuurmans M.M., and Lindberg R.L.P. Acute porphyrias: pathogenesis of neurological manifestations. Semin. Liver Dis. 18 (1998) 43-52
152. Minder E.I. Measurement of 5-aminolaevulinic acid by reversed phase HPLC and fluorescence detection. Clin. Chim. Acta 161 (1986) 11-18
153. Monnier V.M. In: Baynes J.W., and Monnier V.M. (Eds). The Maillard Reaction in Aging, Diabetes and Nutrition (1989), Alan R. Liss, Inc., New York 1-22
154. Monnier V.M., Sell D.R., and Genuth S. Glycation products as markers and predictors of the progression of diabetic complications. Ann. N.Y. Acad. Sci. 1043 (2005) 567-581
155. Monteiro H.P., Abdalla D.S.P., Arcuri S.A., and Bechara E.J.H. Oxygen toxicity related to exposure to lead. Clin. Chem. 31 (1985) 1673-1676
156. Monteiro H.P., Ville G.F., and Winterbourn C.C. Release of iron from ferritin by semiquinone, anthracycline, bipyridyl, and nitroaromatic radicals. Free Radic. Biol. Med. 6 (1988) 587-591
157. Monteiro H.P., Abdalla D.S.P., Augusto O., and Bechara E.J.H. Free radical generation during δ-aminolevulinic acid autoxidation: induction by hemoglobin and connections with porphyrinpathies. Arch. Biochem. Biophys. 271 (1989) 206-216
158. Morley Jr. E., Hirsch H.V.B., Hollocher K., and Lnenicka G.A. Effects of chronic lead exposure on the neuromuscular junction in Drosophila larvae. Neurotoxicology 24 (2003) 35-41
159. Mortensen M.E., and Walson P.D. Chelation therapy for childhood lead poisoning. The changing scene in the 1990s. Clin. Pediatr. 32 (1993) 284-291
160. Mousa H.M., Al-Qarawi A.A., Ali B.H., Rahman H.A.A., and ElMougy S.A. Effect of lead exposure on the erythrocytic antioxidant levels in goats. J. Vet. Med., Ser. A 49 (2002) 531-534
161. Murata K., Sakai T., Morita Y., Iwata T., and Dakeishi M. Critical dose of lead affecting delta-aminolevulinic acid levels. J. Occup. Health 45 (2003) 209-214
162. Murata-Kamiya N., Kamiya H., Kaji H., and Kasai H. Methylglyoxal induces G:C to C:G and G:C to T:A transversions in the supF gene on a shuttle vector plasmid replicated in mammalian cells. Mutat. Res. 468 (2000) 173-182
163. Needleman H. Lead poisoning. Annu. Rev. Med. 55 (2004) 209-222
164. Needleman H.L., McFarland C., Ness R.B., Fienberg S.E., and Tobin M.J. Bone lead levels in adjudicated delinquents. A case control study. Neurotoxicol. Teratol. 24 (2002) 7111-7117
165. Nemet I., Varga-Defterdarovic L., and Turk Z. Preparation and quantification of methylglyoxal in human plasma using reverse-phase high-performance liquid chromatography. Clin. Biochem. 37 (2004) 875-881
166. Neuberg C., and Oertel W. Studies of methylglyoxal formation. Biochem. Z. 55 (1914) 494-503
167. Nickander K.K., McPhee B.R., Low P.A., and Tritschler H. Alpha-lipoic acid: antioxidant potency against lipid peroxidation of neural tissues in vitro and implications for diabetic neuropathy. Free Radic. Biol. Med. 21 (1996) 631-639
168. Niebuhr E. The cri du chat syndrome: epidemiology, cytogenetics, and clinical features. Hum. Genet. 44 (1978) 227-275
169. Niederau C. Diabetes mellitus in hemochromatosis. Z. Gastroenterol. suppl. 1 (1999) 22-32
170. O'Brien P.J., Kaul H., McGirr L., Drolet D., and Silva J.M. Molecular mechanisms for the involvement of the aldehydic metabolites of lipid peroxides in cytotoxicity and carcinogenesis. Pharmacol. Eff. Lipids 3 (1989) 266-280
171. O'Sullivan J., Unzeta M., Healy J., O'Sullivan M.I., Davey G., and Tipton K.F. Semicarbazide-sensitive amine oxidases: enzymes with quite a lot to do. Neurotoxicology 25 (2004) 303-315
172. Ochiai Y., Itoh K., Sakurai E., and Tanaka Y. Molecular cloning and characterization of rat semicarbazide-sensitive amine oxidase. Biol. Pharm. Bull. 28 (2005) 413-418
173. Odani H., Shinzato T., Usami J., Matsumoto Y., Frye E.B., Baynes J.W., and Maeda K. Imidazolium crosslinks derived from reaction of lysine with glyoxal and methylglyoxal are increased in serum proteins of uremic patients: evidence for increased oxidative stress in uremia. FEBS Lett. 427 (1998) 381-385
174. Odani H., Shinzato T., Matsumoto Y., Usami J., and Maeda K. Increase in three alpha,beta-dicarbonyl compound levels in human uremic plasma: specific in vivo determination of intermediates in advanced Maillard reaction. Biochem. Biophys. Res. Commun. 256 (1999) 89-93
175. Oikawa A., and Kawanishi S. Distinct mechanisms of site-specific DNA damage induced by endogenous reductants in the presence of iron(III) and copper(II). Biochim. Biophys. Acta 1399 (1998) 19-30
176. 2+ ions. Biochim. Biophys. Acta 1225 (1994) 259-263
177. Onuki J., Medeiros M.H.G., and Di Mascio P. Genotoxicity of 5-aminolevulinic acid (ALA) in the absence of light. Trends Photochem. Photobiol. 10 (2003) 15-29
178. Oseroff A. Photodynamic therapy. In: Lim H., and Sorter N. (Eds). Clinical Photomedicine (1993), Marcel Dekker, New York 387-402
179. Oteiza P., and Bechara E.J.H. 5-aminolevulinic acid induces lipid peroxidation in cardiolipin-rich liposomes. Arch. Biochem. Biophys. 305 (1993) 282-287
180. Pain D.J., Meharg A.A., Ferrer M., Taggart M., and Penteriani V. Lead concentrations in bones and feathers of the globally threatened Spanish imperial eagle. Biol. Conserv. 121 (2005) 603-610
181. Pech O., Gossner L., May A., Rabenstein T., Vieth M., Stolte M., Berres M., and Ell C. Long-term results of photodynamic therapy with 5-aminolevulinic acid for superficial Barrett's cancer and high-grade intraepithelial neoplasia. Gastrointest. Endosc. 62 (2005) 24-30
182. Penatti C.A.A., Bechara E.J.H., and Demasi M. delta-aminolevulinic acid-induced synaptosomal Ca2+ uptake and mitochondrial permeabilization. Arch. Biochem. Biophys. 335 (1996) 53-60
183. Peng Q., Berg K., Moan J., Kongshaug M., and Nesland J.M. 5-aminolevulinic acid-based photodynamic therapy: principles and experimental research. Photochem. Photobiol. 65 (1997) 235-251
184. Pereira B., Curi R., Kokubun E., and Bechara E.J.H. 5-aminolevulinic acid-induced alterations of oxidative metabolism in sedentary and exercise-trained rats. J. Appl. Physiol. 72 (1992) 226-230
185. Purrello F., Vetri M., Gatta C., Gullo D., and Vigneri R. Effects of high glucose on insulin secretion by isolated rat islets and purified beta-cells and possible role of glycosylation. Diabetes 38 (1989) 1417-1422
186. Raisys V.A., and Winzler R.J. Effect of d-mannosamine on the metabolism of sarcoma 180 ascites cells. P. Soc. Exp. Biol. Med. 138 (1971) 893-898
187. Randell E.W., Vasdev S., and Gill V. Measurement of methylglyoxal in rat tissues by electrospray ionization mass spectrometry and liquid chromatography. J. Pharmacol. Toxicol. Methods 51 (2005) 153-157
188. Ray S., and Ray M. Formation of methylglyoxal from aminoacetone by amine oxidase from goat plasma. J. Biol. Chem. 258 (1983) 3461-3462
189. Ray S., and Ray M. Aminoacetone oxidase from goat liver. Formation of methylglyoxal from aminoacetone. J. Biol. Chem. 262 (1987) 5974-5977
190. Ray S., Dutta S., Halder J., and Ray M. Inhibition of electron flow through complex I of the mitochondrial respiratory chain of Ehrlich ascites carcinoma cells by methylglyoxal. Biochem. J. 303 (1994) 69-72
191. Reddi O.S. Threoninemia - a new metabolic defect. J. Pediatr. 93 (1978) 814-815
192. Redmond R.W., and Gamlin J.N. A compilation of singlet oxygen yields from biologically relevant molecules. Photochem. Photobiol. 70 (1999) 391-475
193. Rocha M.E.M., Ferreira A.M.D.C., and Bechara E.J.H. Roles of phosphate and an enoyl radical in ferritin iron mobilization by 5-aminolevulinic acid. Free Radic. Biol. Med. 29 (2000) 1272-1279
194. Rocha M.E.M., Bandy B., Costa C.A., Barros M.P., Pinto A.M.P., and Bechara E.J.H. Iron mobilization by succinylacetone methyl ester in rats. A model study for hereditary tyrosinemia and porphyrias characterized by 5-aminolevulinic acid overload. Free Radic. Res. 32 (2000) 343-353
195. Rocha M.E.M., Dutra F., Bandy B., Baldini R.L., Gomes S.L., Faljoni-Alario A., Líria C.W., Miranda M.T.M., and Bechara E.J.H. Oxidative damage to ferritin by 5-aminolevulinic acid. Arch. Biochem. Biophys. 409 (2003) 349-356
196. Rossetti L., Giaccari A., and De Fronzo R.A. Glucose toxicity. Diabetes Care 13 (1990) 610-630
197. Royer O.L., Knudsen S.F., Oliveira A.M., Tavares F.M., and Bechara E.J.H. Peroxynitrite-initiated oxidation of acetoacetate and 2-methylacetoacetate esters by oxygen: potential sources of reactive intermediates in keto acidosis. Chem. Res. Toxicol. 17 (2004) 1725-1732
198. Ryter S.W., and Tyrrel R.M. The heme synthesis and degradation pathways: role in oxidant sensitivity. Heme oxygenase has both pro- and antioxidant properties. Free Radic. Biol. Med. 28 (2000) 289-309
199. Sasaki K., Watanabe M., and Tanaka T. Biosynthesis, biotecnological and applications of 5-aminolevulinic acid. Appl. Microbiol. Biotechnol. 58 (2002) 23-29
200. Sasikala Ch., Ramana Ch.V., and Rao P.R. 5-aminolevulinic acid: a potential herbicide/insecticide from microorganisms. Biotechnol. Prog. 10 (1994) 451-459
201. Schmidt A.M., Hori O., Chen J.X., Li J.F., Crandall J., Zhang J., Cao R., Yan S.D., Brett J., and Stern D. Advanced glycation endproducts interacting with their endothelial receptor induce expression of vascular cell adhesion molecule-1 (VCAM-1) in cultured human endothelial cells and in mice. A potential mechanism for the accelerated vasculopathy of diabetes. J. Clin. Invest. 96 (1995) 1395-1403
202. Shamsi F.A., Partal A., Sady C., Glomb M.A., and Nagaraj R.H. Immunological evidence for methylglyoxal-derived modifications in vivo. Determination of antigenic epitopes. J. Biol. Chem. 273 (1998) 6928-6936
203. Shannon M.W., Best D., Binns H.J., Kim J.J., Mazur L.D., Well W.B., Johnson C.L., Reynolds D.W., Roberts J.R., Blackburn E., Johnson R.H., Linet M., Rogan W.J., and Spire P. Lead exposure in children: prevention, detection and management. Pediatrics 116 (2005) 1036-1046
204. Sharpe R.T. An overview of lead poisoning in cattle. Cattle Pract. 12 (2004) 199-203
205. Sheader E.A., Benson R.S.P., and Best L. Cytotoxic action of methylglyoxal on insulin-secreting cells. Biochem. Pharmacol. 61 (2001) 1381-1386
206. Shipanova I.N., Glomb M.A., and Nagaraj R.H. Protein modification by methylglyoxal: chemical nature and synthetic mechanism of a major fluorescent adduct. Arch. Biochem. Biophys. 344 (1997) 29-36
207. Singh R., Barden A., Mori T., and Beilin L. Advanced glycation end-products: a review. Diabetologia 44 (2001) 129-146 (Erratum in: Diabetologia 2002 45, 293)
208. Sithisarankul P., Cadorette M., Davoli C.T., Serwint J.R., Chisolm J.J., and Strickland P.T. Plasma 5-aminolevulinic acid concentration and lead exposure in children. Environ. Res. 80 (1999) 41-49
209. Soulis-Liparota T., Cooper M., Papazoglou D., Clarke B., and Jerums G. Retardation by aminoguanidine of development of albuminuria, mesangial expansion, and tissue fluorescence in streptozocin-induced diabetic rat. Diabetes 40 (1991) 1328-1334
210. Stein J.A., and Tschudy D.P. Acute intermittent porphyria. A clinical and biochemical study of 46 patients. Medicine 49 (1970) 1-16
211. Stohs S.J., and Bagchi D. Oxidative mechanism in the toxicity of metal ions. Free Radic. Biol. Med. 18 (1995) 321-336
212. Stretesky P.B., and Lynch M.J. The relationship between lead and crime. J. Health Soc. Behav. 45 (2004) 214-229
213. Sugimoto K., and Yagihashi S. Effects of aminoguanidine on structural alterations of microvessels in peripheral nerve of streptozotocin diabetic rats. Microvasc. Res. 53 (1997) 105-120
214. Swanson R., Locher M., and Hochstrasser M. A conserved ubiquitin ligase of the nuclear envelope/endoplasmic reticulum that functions in both ER-associated and Matalpha2 repressor degradation. Genes Dev. 15 (2001) 2660-2674
215. Szent-Györgyi A. A study of energy levels in biochemistry. Nature 148 (1941) 157-159
216. Szent-Györgyi A. Bioelectronics - intermolecular electron transfer may play a major role in biological regulation defense and cancer. Science 161 (1968) 988-990
217. Szent-Györgyi A. Bioelectronics and cancer. Bioenergetics 4 (1973) 533-562
218. Takatori A., Ishii Y., Itagaki S., Kyuwa S., and Yoshikawa Y. Amelioration of the beta-cell dysfunction in diabetic APA hamsters by antioxidants and AGE inhibitor treatments. Diabetes Metab. Res. Rev. 20 (2004) 211-218
219. Theil E.C. Ferritin: structure, gene regulation, and cellular function in animals, plants, and microorganisms. Ann. Rev. Biochem. 56 (1987) 289-315
220. Thornalley P.J. Monosaccharide autoxidation in health and disease. Environ. Health Perspect. 64 (1985) 297-307
221. Thornalley P.J. The glyoxalase system: new developments towards functional characterization of a metabolic pathway fundamental to biological life. Biochem. J. 269 (1990) 1-11
222. Thornalley P.J. Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification-a role in pathogenesis and antiproliferative chemotherapy. Gen. Pharmacol. 27 (1996) 565-573
223. Thornalley P.J. Glutathione-dependent detoxification of alpha-oxoaldehydes by the glyoxalase system: involvement in disease mechanisms and antiproliferative activity of glyoxalase I inhibitors. Chem. Biol. Interact. 111-112 (1998) 137-151
224. Thornalley P.J. The clinical significance of glycation. Clin. Lab. (Heidelberg) 45 (1999) 263-273
225. Thornalley P.J. Glycation in diabetic neuropathy: characteristics, consequences, causes, and therapeutic options. Int. Rev. Neurobiol. 50 (2002) 37-57
226. Thornalley P.J., Yurek-George A., and Argirov O.K. Kinetics and mechanism of the reaction of aminoguanidine with the α-oxoaldehydes glyoxal, methylglyoxal, and 3-deoxyglucosone under physiological conditions. Biochem. Pharmacol. 60 (2000) 55-65
227. Thunnissen P.L.M., Meyer J., and Dekoning R.W. Acute intermittent porphyria and primary liver cell carcinoma. Neth. J. Med. 38 (1991) 171-174
228. {radical dot}-. Free Radic. Biol. Med. 27 (1999) 329-333
229. Tressel T., Thompson R., Zieske L.R., Menendez M.I.T.S., and Davis L. Interaction between l-threonine dehydrogenase and aminoacetone synthetase and mechanism of aminoacetone production. J. Biol. Chem. 261 (1986) 16428-16437
230. Tripathy B.C., and Singhal G.S. Oxidative stress in photodynamic herbicidal action of 5-aminolevulinic acid. Concepts Photobiol. (1999) 668-688
231. Twigg S.M., Cao Z., McLennan S.V., Burns W.C., Brammar G., Forbes J.M., and Cooper M.E. Renal connective tissue growth factor induction in experimental diabetes is prevented by aminoguanidine. Endocrinology 143 (2002) 4907-4915
232. Urata G., and Granick S. Biosynthesis of alpha-aminoketones and the metabolism of aminoacetone. J. Biol. Chem. 238 (1963) 811-820
233. Usta M.F., Bivalacqua T.J., Koksal I.T., Toptas B., Surmen S., and Hellstrom W.J. The protective effect of aminoguanidine on erectile function in diabetic rats is not related to the timing of treatment. BJU Int. 94 (2004) 429-432
234. van Dijk J., and Boomsma F. Stability of semicarbazide-sensitive amine oxidase in human blood and plasma. Clin. Chim. Acta 270 (1998) 189-194
235. Vander Jagt D.L., Hassebrook R.K., Hunsaker L.A., Brown W.M., and Royer R.E. Metabolism of the 2-oxoaldehyde methylglyoxal by aldose reductase and by glyoxalase-I: roles for glutathione in both enzymes and implications for diabetic complications. Chem. Biol. Interact. 130-132 (2001) 549-562
236. Vlassara H., Brownlee M., Monogue K.R., Dinarello C.A., and Pasagian A. Cachectin/TNF and IL-1 induced by glucose-modified proteins: role in normal tissue remodeling. Science 240 (1988) 1546-1548
237. Vlassara H., Fuh H., Donnelly T., and Cybulsky M. Advanced glycation endproducts promote adhesion molecule (VCAM-1, ICAM-1) expression and atheroma formation in normal rabbits. Mol. Med. 1 (1995) 447-456
238. Wallace W.J., Houtchens R.A., Maxwell J.C., and Caughey W.S. Mechanism of autooxidation for hemoglobins and myoglobins. Promotion of superoxide production by protons and anions. J. Biol. Chem. 257 (1982) 4966-4977
239. Wang J., Liu R., Hawkins M., Barzilai N., and Rossetti L. A nutrient-sensing pathway regulates leptin gene expression in muscle and fat. Nature 393 (1998) 684-688
240. Webster J., Urban C., Berbaum K., Loske C., Alpar A., Gartner U., de Arriba S.G., Arendt T., and Munch G. The carbonyl scavengers aminoguanidine and tenilsetam protect against the neurotoxic effects of methylglyoxal. Neurotox. Res. 7 (2005) 95-101
241. Weishaupt K.R., Gomer C.J., and Dougherty T.J. Identification of singlet oxygen as the cytotoxic agent in photoinactivation of a murine tumor. Cancer Res. 36 (1976) 2326-2329
242. Welch K.D., Davis T.Z., and Aust S.D. Iron autoxidation and free radical generation: effects of buffers ligands, and chelators. Arch. Biochem. Biophys. 397 (2002) 360-369
243. Westwood M.E., and Thornalley P.J. Molecular characteristics of methylglyoxal-modified bovine and human serum albumins. Comparison with glucose-derived advanced glycation endproduct-modified serum albumins. J. Protein Chem. 14 (1995) 359-372
244. Westwood M.E., and Thornalley P.J. Cytokine synthesis and secretion induced by methylglyoxal-modified proteins. Diabetic Med. 12 suppl.2-10 (1995) 549
245. Westwood M.E., Argirov O.K., Abordo E.A., and Thornalley P.J. Methylglyoxal-modified arginine residues-a signal for receptor-mediated endocytosis and degradation of proteins by monocytic THP-1 cells. Biochim. Biophys. Acta 1356 (1997) 84-94
246. White E.H., Wiecko J., and Roswell D.F. Photochemistry without light. J. Am. Chem. Soc. 91 (1969) 51-94
247. Wilkins L.E., Brown J., and Wolf B. Psychomotor development in 65 home-reared children with cri-du-chat syndrome. J. Pediatr. 97 (1980) 401-405
248. Wolfsen H.C., and Ng C.S. Cutaneous consequences of photodynamic therapy. Cutis 69 (2002) 140-142
249. Wu Q., Niebuhr E., Yang H., and Hansen L. Determination of the 'critical region' for cat-like cry of cri-du-chat syndrome and analysis of candidate genes by quantitative PCR. Eur. J. Hum. Genet. 13 (2005) 475-485
250. Yan S.D., Schmidt A.M., Anderson G.M., Zhang J., Brett J., Zou Y.S., Pinsky D., and Stern D. Enhanced cellular oxidant stress by the interaction of advanced glycation end products with their receptors/binding proteins. J. Biol. Chem. 269 (1994) 9889-9897
251. Young I.S., Tate S., Lightbody J.H., McMaster D., and Trimble E.R. The effects of desferrioxamine and ascorbate on oxidative stress in the streptozotocin diabetic rat. Free Radic. Biol. Med. 18 (1995) 833-840
252. Yu P.H. Deamination of methylamine and angiopathy; toxicity of formaldehyde, oxidative stress and relevance to protein glycoxidation in diabetes. J. Neural Transm. 52 (1998) 201-216
253. Yu P.H., and Zuo D.M. Aminoguanidine inhibits semicarbazide-sensitive amine oxidase activity: implications for advanced glycation and diabetic complications. Diabetologia 40 (1997) 1243-1250
254. Yu P.H., Zuo D., and Davis B.A. Characterization of human serum and umbilical artery semicarbazide-sensitive amine oxidase (SSAO). Species heterogeneity and stereoisomeric specificity. Biochem. Pharmacol. 47 (1994) 1055-1059
255. Yu P.H., Wright S., Fan E.H., Lun Z.R., and Gubisne-Harberle D. Physiological and pathological implications of semicarbazide-sensitive amine oxidase. Biochim. Biophys. Acta 1647 (2003) 193-199