5′-O-Alkylpyridoxamines: Lipophilic Analogues of Pyridoxamine Are Potent Scavengers of 1,2-Dicarbonyls

Chemical Research in Toxicology

Volumn 28, Issue 7, 2015, Pages 1469-1475

  Amarnath, Venkataraman ^a   Amarnath, Kalyani ^a   Avance, Joshua ^c   Stec, Donald F ^b   Voziyan, Paul ^a  

^a VANDERBILT UNIVERSITY MEDICAL CENTER   (United States)

^b VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

^c BEREA COLLEGE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1,2 CARBONYL; 1,2 DICARBONYL DERIVATIVE; 5' O ALKYLPYRIDOXAMINE; ALKYL GROUP; ARGININE; CARBONYL DERIVATIVE; GLUCOSE; GUANIDINE; LYSOZYME; METHYL GROUP; METHYLGLYOXAL; PYRIDOXAMINE; PYRIDOXINE; UNCLASSIFIED DRUG; FREE RADICAL; HORSERADISH PEROXIDASE; MEMBRANE PROTEIN; SCAVENGER; SUPEROXIDE DISMUTASE;

ARTICLE; AUTOOXIDATION; DRUG SYNTHESIS; ENZYME ACTIVITY; GLUCOSE METABOLISM; LIPOPHILICITY; MACROMOLECULE; TISSUE DISTRIBUTION; BIOCATALYSIS; CHEMICAL PHENOMENA; CHEMISTRY; CONFORMATION; ELECTRON SPIN RESONANCE; METABOLISM; SYNTHESIS; ULTRAVIOLET SPECTROPHOTOMETRY;

BIOCATALYSIS; ELECTRON SPIN RESONANCE SPECTROSCOPY; FREE RADICAL SCAVENGERS; FREE RADICALS; GLUCOSE; HORSERADISH PEROXIDASE; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MEMBRANE PROTEINS; MOLECULAR CONFORMATION; MURAMIDASE; PYRIDOXAMINE; PYRUVALDEHYDE; SPECTROPHOTOMETRY, ULTRAVIOLET; SUPEROXIDE DISMUTASE;

EID: 84937720654     PISSN: 0893228X     EISSN: 15205010     Source Type: Journal    
DOI: 10.1021/acs.chemrestox.5b00148     Document Type: Article

References (33)

1. Rabbani, N. and Thornalley, P. J. (2012) Methylglyoxal, glyoxalase 1 and the dicarbonyl proteome Amino Acids 42, 1133-1141
2. Usui, T., Yanagisawa, S., Ohguchi, M., Kawabata, R., Kishimoto, J., Arai, Y., Aida, K., Watanabe, H., and Hayase, F. (2007) Identification and determination of α-dicarbonyl compounds formed in the degradation of sugars Biosci. Biotechnol. Biochem. 71, 2465-2472
3. Acimovic, J. M., Stanimirovic, B. D., and Mandic, L. M. (2009) The role of the thiol group in protein modification with methylglyoxal J. Serb. Chem. Soc. 74, 867-883
4. Synold, T., Xi, B., Wuenschell, G. E., Tamae, D., Figarola, J. L., Rabbar, S., and Termini, J. (2008) Advanced glycation end products of DNA: Quantification of N2-(1-carboxyethyl)-2′-deoxyguanosine in biological samples by liquid chromatography electrospray ionization tandem mass spectrometry Chem. Res. Toxicol. 21, 2148-2155
5. Gauthier, M. A. and Klok, H. (2011) Arginine-specific modification of proteins with polyethylene glycol Biomacromolecules 12, 482-493
6. Distler, L., Georrgieva, A., Kenkel, I., Huppert, J., and Pischetsrieder, M. (2014) Structure- and concentration-specific assessment of the physiological reactivity of α-dicarbonyl glucose degradation products in peritoneal dialysis fluids Chem. Res. Toxicol. 27, 1421-1430
7. Park, Y., Koh, Y., Takahashi, M., Miyamoto, Y., Suzuki, K., Dohmae, N., Takio, K., Honke, K., and Tanaguchi, N. (2003) Identification of the binding site of methylglyoxal on glutathione peroxidase: Methylglyoxal inhibits glutathione peroxidase activity via binding to glutathione binding sites Arg 184 and 185 Free Radical Res. 37, 205-211
8. Kim, J., Kim, H. K., Sohn, E., Kim, C.-S., and Kim, J. (2010) Methylglyoxal induces cellular damage by increasing argpyrimidine accumulation and oxidative DNA damage in human lens epithelial cells Biochem. Biophys. Res. Commun. 391, 346-351
9. Chetyrkin, S. V., Mathis, M., Pedchenko, V., Sanchez, O. A., McDonald, H., Hachey, D. L., Madu, H., Stec, D., Hudson, B. G., and Vozian, P. A. (2011) Glucose autoxidation induces functional damage to proteins via modification of critical arginine residues Biochemistry 50, 6102-6112
10. Lederer, M. O. and Klaiber, R. G. (1999) Cross-linking of proteins by Maillard processes. Charaterization and detection of lysine-arginine cross-links derived from glyoxal and methylglyoxal. Bioorg. Med. Chem. 7, 2499-2507.
11. Petrova, K. V., Millsap, A. D., Stec, D. F., and Rizzo, C. J. (2014) Characterization of the deoxyguanosine-lysine cross-link of methylglyoxal Chem. Res. Toxicol. 27, 1019-1029
12. Williams, M. E., Bolton, W. K., Khalifah, R. G., Degenhardt, T. P., Schotzinger, R. J., and McGill, J. B. (2007) Effects of pyridoxamine in combined phase 2 studies of patients with Type 1 and Type 2 diabetes and overt nephropathy Am. J. Nephrol. 27, 605-614
13. Lewis, E. J., Greene, T., Spitalewiz, S., Blumethal, S., Berl, T., Atkins, R. C., Reutens, A. T., Packam, D. K., and Lewis, J. B. (2012) Pyridorin in Type 2 diabetic nephropathy J. Am. Soc. Nephrol. 23, 131-136
14. Voziyan, P. A. and Hudson, B. G. (2005) Pyridoxamine: The many virtues of a Maillard reaction inhibitor Ann. N.Y. Acad. Sci. 1043, 807-816
15. Chetyrkin, S. V., Zhang, W., Hudson, B. G., Serianni, A. S., and Vozian, P. A. (2008) Pyridoxamine protects proteins from functional damage by 3-deoxyglucosone: Mechanism of Action of pyridoxamine Biochemistry 47, 997-1006
16. Zagol-Ikapitte, I., Matafonova, E., Amarnath, V., Bodine, C. L., Boutaud, O., Tirona, R. G., Oates, J. A., Roberts, L. J., and Davies, S. S. (2010) Determination of the pharmacokinetics and oral bioavailability of salicylamine, a potent γ-ketoaldehyde scavenger, by LC/MS/MS Pharmaceutics 2, 18-29
17. Wu, Y. K. and Ahlberg, P. (1989) On the formation of isopropylidenepyridoxines. A convenient method for the preparation of 2,2,8-trimethyl-4 H -1,3-dioxino[4,5-c]pyridin-5-ylmethanol from pyridoxine hydrochloride Acta Chem. Scand. 43, 1009-1011
18. Zagol-Ikapitte, I., Amarnath, V., Bala, M., Roberts, L. J., Oates, J. A., and Boutaud, O. (2010) Characterization of scavengers of γ-ketoaldehydes that do not inhibit prostaglandin biosynthesis Chem. Res. Toxicol. 23, 240-250
19. Glomb, M. A. and Lang, G. (2001) Isolation and characterization of glyoxal-arginine modifications J. Agric. Food Chem. 49, 1493-1501
20. Klopfer, A., Spanneberg, R., and Glomb, M. A. (2011) Formation of arginine modifications in a model system of N-α-tert-butoxycarbonyl-arginine with methylglyoxal J. Agric. Food Chem. 59, 394-401
21. Shugar, D. (1952) The measurement of lysozyme activity and the ultra-violet inactivation of lysozyme Biochim. Biophys. Acta 8, 302-9
22. Amarnath, V., Amarnath, K., Amarnath, K., Davies, S., and Roberts, L. J. (2004) Pyridoxamine: An extremely potent scavenger of 1,4-dicarbonyls Chem. Res. Toxicol. 17, 410-415
23. Adrover, M., Vilanova, B., Frau, J., Munoz, F., and Donoso, J. (2009) A comparative study of the chemical reactivity of pyridoxamine, Ac-Phe-Lys and Ac-Cys with various glycating carbonyl compounds Amino Acids 36, 437-448
24. Nagaraj, R. H., Sarkar, P., Mally, A., Biemel, K. M., Lederer, M. O., and Padayatti, P. S. (2002) Effect of pyridoxamine on chemical modification of proteins by carbonyls in diabetic rats: characterization of a major product from the reaction of pyridoxamine and methylglyoxal Arch. Biochem. Biophys. 402, 110-119
25. Metz, T. O., Alderson, N. L., Chachich, M. E., Thorpe, S. R., and Baynes, J. W. (2003) Evidence on the role of lipids in chemical modification of protein and development of diabetic complications J. Biol. Chem. 43, 42012-32019
26. Alcaide, B., Rubio, R., Plumet, J., and Rodrigues-Campos, I. M. (1990) Anatomy of a three species tautomeric process: The ring-chain tautomerism in 5,6-dihydro-2-hydroxy-2,3-dimethyl-2 H -1,4-oxazine Tetrahedron Lett. 31, 4211-4214
27. McDonagh, A. F. and Smith, H. F. (1968) Ring-Chain tautomerism of derivatives if o -hydroxybenzylamine with aldehydes and ketones J. Org. Chem. 33, 1-8
28. Kanatomi, H. and Murase, I. (1970) Reaction of salicylamine with α-dicarbonyl compounds. II. Formation of 2,2′-bibenz-1,3-oxazines Bull. Chem. Soc. Jpn. 43, 226-231
29. Voziyan, P. A., Metz, T. O., Batnes, J. W., and Hudson, B. G. (2002) A post-amadori inhibitor pyridoxamine also inhibits chemical modification of proteins by scavenging carbonyl intermediates of carbohydrate and lipid degradation J. Biol. Chem. 277, 3397-3403
30. Adrover, M., Vilanova, B., Munoz, F., and Donoso, J. (2009) Unexpected isomeric equilibrium in pyridoxamine Schiff bases Bioorg. Chem. 37, 26-32
31. Metzler, D. E. and Snell, E. E. (1955) Spectra and ionization constants of the vitamin B6 group and related 3-hydroxypyridine derivatives J. Am. Chem. Soc. 77, 2431-2437
32. Cotham, W. E., Metz, T. O., Ferguson, L., Brock, W. C., Hinton, D., Thorpe, S. R., Baynes, J. W., and Ames, J. A. (2004) Proteomic analysis of arginine adducts on glyoxal-modified ribonuclease Mol. Cell. Proteomics 3, 1145-1153
33. Flores-Morales, P., Diema, C., Vilaseca, M., Estelrich, J., Luque, F. J., Gutierrez-Oliva, S., Toro-Labbe, A., and Silva, E. (2011) Enhanced reactivity of Lys 182 explains the limited efficacy of biogenic amines in preventing the inactivation of glucose-6-phosphate dehydrogenase by methylglyoxal Bioorg. Med. Chem. 19, 1613-1622