Insights into potentially toxic effects of 4-aminoantipyrine on the antioxidant enzyme copper-zinc superoxide dismutase

Journal of Hazardous Materials

Volumn 262, Issue , 2013, Pages 318-324

  Teng, Yue ^a   Liu, Rutao ^b  

^a JIANGNAN UNIVERSITY   (China)

^b SHANDONG UNIVERSITY   (China)

Author keywords

Antioxidant enzyme; Docking studies; Multi spectroscopic techniques; Toxicity evaluation

Indexed keywords

4-AMINOANTIPYRINE; ANALGESIC DRUGS; ANTIOXIDANT ENZYME; DOCKING STUDIES; MOLECULAR DOCKING SIMULATIONS; MOLECULAR LEVELS; MULTI-SPECTROSCOPIC TECHNIQUES; SUPER OXIDE DISMUTASE;

ANTIOXIDANTS; DRUG INTERACTIONS; HYDROGEN BONDS; MOLECULAR MODELING; OXYGEN; TOXICITY; VAN DER WAALS FORCES;

ENZYMES;

4 AMINOPHENAZONE; COPPER ZINC SUPEROXIDE DISMUTASE; ANTIOXIDANT; SUPEROXIDE DISMUTASE;

ANTIOXIDANT; ENZYME ACTIVITY; MOLECULAR ANALYSIS; NUMERICAL MODEL; ORGANIC COMPOUND; POLLUTION EFFECT; TOXICITY;

ABSORPTION SPECTROSCOPY; ARTICLE; BINDING AFFINITY; BINDING SITE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVITY; HUMAN; HYDROGEN BOND; MOLECULAR DOCKING; MOLECULAR MODEL; THERMODYNAMICS; TOXICITY TESTING; ANIMAL; METABOLISM; SPECTROFLUOROMETRY; SWINE; TOXICITY; ULTRAVIOLET SPECTROPHOTOMETRY;

AMPYRONE; ANIMALS; ANTIOXIDANTS; CIRCULAR DICHROISM; MOLECULAR DOCKING SIMULATION; SPECTROMETRY, FLUORESCENCE; SPECTROPHOTOMETRY, ULTRAVIOLET; SUPEROXIDE DISMUTASE; SWINE;

EID: 84884375269     PISSN: 03043894     EISSN: 18733336     Source Type: Journal    
DOI: 10.1016/j.jhazmat.2013.08.047     Document Type: Article

References (46)

1. Reuter S., Gupta S.C., Chaturvedi M.M., Aggarwal B.B. Oxidative stress, inflammation, and cancer. How are they linked?. Free Radical Biol. Med. 2010, 49:1603-1616.
2. Kehrer J.P. The Haber-Weiss reaction and mechanisms of toxicity. Toxicology 2000, 149:43-50.
3. Kim S.Y., Kwon O.J., Park J.W. Inactivation of catalase and superoxide dismutase by singlet oxygen derived from photoactivated dye. Biochimie 2001, 83:437-444.
4. Evans M.D., Dizdaroglu M., Cooke M.S. Oxidative DNA damage and disease: induction, repair and significance. Mutat. Res. -Rev. Mutat. 2004, 567:1-61.
5. Chen A.F., Davies C.M., De Lin M., Fermor B. Oxidative DNA damage in osteoarthritic porcine articular cartilage. J. Cell. Physiol. 2008, 217:828-833.
6. Xie L., Zhu X., Hu Y., Li T., Gao Y., Shi Y., Tang S. Mitochondrial DNA oxidative damage triggering mitochondrial dysfunction and apoptosis in high glucose-induced HRECs. Invest. Ophthalmol. Vis. Sci. 2008, 49:4203-4209.
7. Gromadzinska J., Wasowicz W., Andrijewski M., Sklodowska M., Quispe O.Z., Wolkanin P., Olborski B., Pluzanska A. Glutathione and glutathione metabolizing enzymes in tissues and blood of breast cancer patients. Neoplasma 1997, 44:45-51.
8. Upadhya S., Upadhya S., Mohan S.K., Vanajakshamma K., Kunder M., Mathias S. Oxidant-antioxidant status in colorectal cancer patients-before and after treatment. Indian J. Clin. Biochem. 2004, 19:80-83.
9. Subapriya R., Kumaraguruparan R., Ramachandran C.R., Nagini S. Oxidant-antioxidant status in patients with oral squamous cell carcinomas at different intraoral sites. Clin. Biochem. 2002, 35:489-493.
10. Aaseth J., Stoa-Birketvedt G. Glutathione in overweight patients with poorly controlled type 2 diabetes. J. Trace Elem. Exp. Med. 2000, 13:105-111.
11. Banaclocha M.M., Hernandez A.I., Martinez N., Ferrandiz M.L. N-acetylcysteine protects against age-related increase in oxidized proteins in mouse synaptic mitochondria. Brain Res. 1997, 762:256-258.
12. Strasser E.M., Wessner B., Manhart N., Roth E. The relationship between the anti-inflammatory effects of curcumin and cellular glutathione content in myelomonocytic cells. Biochem. Pharmacol. 2005, 70:552-559.
13. Polidoro G., Di Ilio C., Arduini A., La Rovere G., Federici G. Superoxide dismutase, reduced glutathione and TBA-reactive products in erythrocytes of patients with multiple sclerosis. Int. J. Biochem. 1984, 16:505-509.
14. Amer J., Ghoti H., Rachmilewitz E., Koren A., Levin C., Fibach E. Red blood cells, platelets and polymorphonuclear neutrophils of patients with sickle cell disease exhibit oxidative stress that can be ameliorated by antioxidants. Br. J. Haematol. 2006, 132:108-113.
15. Sies H. Oxidative stress: from basic research to clinical application. Am. J. Med. 1991, 91:31S-38S.
16. Miao L., St Clair D.K. Regulation of superoxide dismutase genes: implications in disease. Free Radical Biol. Med. 2009, 47:344-356.
17. Giustarini D., Dalle-Donne I., Tsikas D., Rossi R. Oxidative stress and human diseases: Origin, link, measurement, mechanisms, and biomarkers. Crit. Rev. Clin. Lab. Sci. 2009, 46:241-281.
18. Chen Y.M., Chen Y.P. Measurements for the solid solubilities of antipyrine, 4-aminoantipyrine and 4-dimethylaminoantipyrine in supercritical carbon dioxide. Fluid Phase Equilibr. 2009, 282:82-87.
19. Lang A., Hatscher C., Wiegert C., Kuhl P. Protease-catalysed coupling of N-protected amino acids and peptides with 4-aminoantipyrine. Amino Acids 2009, 36:333-340.
20. Cunha S., Oliveira S.M., Rodrigues M.T., Bastos R.M., Ferrari J., de Oliveira C.M.A., Kato L., Napolitano H.B., Vencato I., Lariucci C. Structural studies of 4-aminoantipyrine derivatives. J. Mol. Struct. 2005, 752:32-39.
21. Prasad S., Agarwal R.K. Cobalt(II) complexes of various thiosemicarbazones of 4-aminoantipyrine: syntheses, spectral, thermal and antimicrobial studies. Transit. Metal Chem. 2007, 32:143-149.
22. van Staden J.F., Beyene N.W., Stefan R.I., Aboul-Enein H.Y. Sequential injection spectrophotometric determination of ritodrine hydrochloride using 4-aminoantipyrine. Talanta 2005, 68:401-405.
23. Kasthuri J., Santhanalakshmi J., Rajendiran N. Platinum nanoparticle catalysed coupling of phenol derivatives with 4-aminoantipyrine in aqueous medium. Transit. Metal Chem. 2008, 33:899-905.
24. Katsaounos C.Z., Paleologos E.K., Giokas D.L., Karayannis M.I. The 4-aminoantipyrine method revisited: Determination of trace phenols by micellar assisted preconcentration. Int. J. Environ. Anal. Chem. 2003, 83:507-514.
25. Vinagre A.M., Collares E.F. Effect of 4-aminoantipyrine on gastric compliance and liquid emptying in rats. Braz. J. Med. Biol. Res. 2007, 40:903-909.
26. Sunderji S.G., El Badry A., Poore E.R., Figueroa J.P., Nathanielsz P.W. The effect of myometrial contractures on uterine blood flow in the pregnant sheep at 114 to 140 days' gestation measured by the 4-aminoantipyrine equilibrium diffusion technique. Am. J. Obstet. Gynecol. 1984, 149:408-412.
27. El Badry A., Figueroa J.P., Poore E.R., Sunderji S., Levine S., Mitchell M.D., Nathanielsz P.W. Effect of fetal intravascular 4-aminoantipyrine infusions on myometrial activity (contractures) at 125 to 143 days' gestation in the pregnant sheep. Am. J. Obstet. Gynecol. 1984, 150:474-479.
28. Pierre S.C., Schmidt R., Brenneis C., Michaelis M., Geisslinger G., Scholich K. Inhibition of cyclooxygenases by dipyrone. Br. J. Pharmacol. 2007, 151:494-503.
29. Teng Y., Liu R., Li C., Xia Q., Zhang P. The interaction between 4-aminoantipyrine and bovine serum albumin: multiple spectroscopic and molecular docking investigations. J. Hazard. Mater. 2011, 190:574-581.
30. Teng Y., Liu R., Yan S., Pan X., Zhang P., Wang M. Spectroscopic investigation on the toxicological interactions of 4-aminoantipyrine with bovine hemoglobin. J. Fluoresc. 2010, 20:381-387.
31. Sakoguchi T., Kobayashi K., Kimura M., Hase A., Shimozawa M., Matsuoka A. Influence of blood proteins on biomedical analysis. VI. Effect of bovine serum albumin on the color reaction of xanthurenic acid with 4-aminoantipyrine - inhibition of antipyrine red production by bovine serum albumin. Chem. Pharm. Bull. 1984, 32:1219-1223.
32. Ma L.L., Ze Y.G., Liu J., Liu H.T., Liu C., Li Z.R., Zhao J.F., Yan J.Y., Duan Y.M., Xie Y.N., Hong F.S. Direct evidence for interaction between nano-anatase and superoxide dismutase from rat erythrocytes. Spectrochim. Acta A 2009, 73:330-335.
33. Beauchamp C., Fridovich I. Superoxide dismutase: improved assays and an assay applicable to acrylamide gels. Anal. Biochem. 1971, 44:276-287.
34. Sun Y., Oberley L.W., Li Y. A simple method for clinical assay of superoxide dismutase. Clin. Chem. 1988, 34:497-500.
35. Frisch M.J., Trucks G.W., Schlegel H.B., Scuseria G.E., Robb M.A., Cheeseman J.R., Montgomery J.A., Vreven J.T., Kudin K.N., Burant J.C., Millam J.M., Iyengar S.S., Tomasi J., Barone V., Mennucci B., Cossi M., Scalmani G., Rega N., Petersson G.A., Nakatsuji H., Hada M., Ehara M., Toyota K., Fukuda R., Hasegawa J., Ishida M., Nakajima T., Honda Y., Kitao O., Nakai H., Klene M., Li X., Knox J.E., Hratchian H.P., Cross J.B., Bakken V., Adamo C., Jaramillo J., Gomperts R., Stratmann R.E., Yazyev O., Austin A.J., Cammi R., Pomelli C., Ochterski J.W., Ayala P.Y., Morokuma K., Voth G.A., Salvador P., Dannenberg J.J., Zakrzewski V.G., Dapprich S., Daniels A.D., Strain M.C., Farkas O., Malick D.K., Rabuck A.D., Raghavachari K., Foresman J.B., Ortiz J.V., Cui Q., Baboul A.G., Clifford S., Cioslowski J., Stefanov B.B., Liu G., Liashenko A., Piskorz P., Komaromi I., Martin R.L., Fox D.J., Keith T., Al-Laham M.A., Peng C.Y., Nanayakkara A., Challacombe M., Gill P.M.W., Johnson B., Chen W., Wong M.W., Gonzalez C., Pople J.A. Gaussian 03 2004, Gaussian, Inc., Wallingford CT.
36. Jiang Y., Wong J.H., Pi Z.F., Ng T.B., Wang C.R., Hou J., Chen R.R., Niu H.J., Liu F. Stimulatory effect of components of rose flowers on catalytic activity and mRNA expression of superoxide dismutase and catalase in erythrocytes. Environ. Toxicol. Pharmacol. 2009, 27:396-401.
37. Clemens M.R., Waller H.D. Lipid peroxidation in erythrocytes. Chem. Phys. Lipids 1987, 45:251-268.
38. Lu J.Q., Jin F., Sun T.Q., Zhou X.W. Multi-spectroscopic study on interaction of bovine serum albumin with lomefloxacin-copper(II) complex. Int. J. Biol. Macromol. 2007, 40:299-304.
39. Wu T., Wu Q., Guan S., Su H., Cai Z. Binding of the environmental pollutant naphthol to bovine serum albumin. Biomacromolecules 2007, 8:1899-1906.
40. Chen L.H., Tianqing L.Q. Interaction behaviors between chitosan and hemoglobin. Int. J. Biol. Macromol. 2008, 42:441-446.
41. Sreerama N., Woody R.W. On the analysis of membrane protein circular dichroism spectra. Protein Sci. 2004, 13:100-112.
42. Zhang Y.Z., Zhou B., Zhang X.P., Huang P., Li C.H., Liu Y. Interaction of malachite green with bovine serum albumin: determination of the binding mechanism and binding site by spectroscopic methods. J. Hazard. Mater. 2009, 163:1345-1352.
43. Lakowicz J.R., Weber G. Quenching of protein fluorescence by oxygen. Detection of structural fluctuations in proteins on the nanosecond time scale. Biochemistry 1973, 12:4171-4179.
44. Ware W.R. Oxygen quenching of fluorescence in solution: an experimental study of the diffusion process. J. Phys. Chem. 1962, 66:455-458.
45. Ojha B., Das G. The interaction of 5-(alkoxy)naphthalen-1-amine with bovine serum albumin and its effect on the conformation of protein. J. Phys. Chem. B 2010, 114:3979-3986.
46. Ross P.D., Subramanian S. Thermodynamics of protein association reactions: forces contributing to stability. Biochemistry 1981, 20:3096-3102.