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OUT-OF-MIND INHIBITORS OF HUMAN SERUM PARAOXONASE 1 (PON1): AN IN VITRO STUDY

Yıl 2017, Cilt: 3 Sayı: 1, 59 - 68, 28.08.2017
https://doi.org/10.23884/mejs.2017.3.1.07

Öz


4-(dimethylamino)benzaldehyde, 3,5-dinitrosalicylic acid, berylliumsulfate tetrahydrate, urea, sodium azide, iron(II)sulfateheptahydrate, 2-thiobarbituric acid, benzidine, and hydrazinium sulfate, which are commonly used in the pharmaceutical industry and medical studies, have been examined as novel type of inhibitors of PON1. PON1 was purified by hydrophobic column of Sepharose-4B-coupled L-tyrosine- 1-naphthylamine. PON1 enzyme activity towards paraoxon substrate was quantified spectrophotometrically. A critical overview of the effects of these nine reagents on PON1 which associated with cardiovascular diseases has been given. The IC50 values were between 1.26×10-4 M and 2.31×10-4 M and benzidine showed the best inhibitory effect (IC50 = 1.26×10-4M) for PON1 enzyme activity.


Kaynakça

  • [1] B. Mackness, P.N. Durrington, M.I. Mackness, Human Serum Paraoxonase, General Pharmacology: The Vascular System. 31 (1998) 329–336.
  • [2] N. Ferré, J. Camps, E. Prats, E. Vilella, A. Paul, L. Figuera, J. Joven, Serum paraoxonase activity: A new additional test for the improved evaluation of chronic liver damage, Clinical Chemistry. 48 (2002) 261–268.
  • [3] N. Forti, J. Diament, Lipoproteínas de alta densidade: aspectos metabólicos, clínicos, epidemiológicos e de intervenção terapêutica. Atualização para os clínicos , Arquivos Brasileiros de Cardiologia . 87 (2006) 671–679.
  • [4] L.G. Costa, A. Vitalone, T.B. Cole, C.E. Furlong, Modulation of paraoxonase (PON1) activity, Biochemical Pharmacology. 69 (2005) 541–550.
  • [5] F.G. Santos, M.K. Becker, V.S. Corrêa, D.N. Garcia, S.C. Vale, J.A. Crespo-Ribeiro, C.C. Barros, A. Schneider, The effect of the paraoxonase 1 (PON1) T(-107)C polymorphism on serum PON1 activity in women is dependent on fatty acid intake, Nutrition Research. 36 (2016) 9–15.
  • [6] T. Suehiro, T. Nakamura, M. Inoue, T. Shiinoki, Y. Ikeda, Y. Kumon, M. Shindo, H. Tanaka, K. Hashimoto, A polymorphism upstream from the human paraoxonase (PON1) gene and its association with PON1 expression, Atherosclerosis. 150 (2000) 295–298.
  • [7] A.S. Go, D. Mozaffarian, V.L. Roger, E.J. Benjamin, J.D. Berry, W.B. Borden, D.M. Bravata, S. Dai, E.S. Ford, C.S. Fox, S. Franco, H.J. Fullerton, C. Gillespie, S.M. Hailpern, J.A. Heit, V.J. Howard, M.D. Huffman, B.M. Kissela, S.J. Kittner, D.T. Lackland, J.H. Lichtman, L.D. Lisabeth, D. Magid, G.M. Marcus, A. Marelli, D.B. Matchar, D.K. McGuire, E.R. Mohler, C.S. Moy, M.E. Mussolino, G. Nichol, N.P. Paynter, P.J. Schreiner, P.D. Sorlie, J. Stein, T.N. Turan, S.S. Virani, N.D. Wong, D. Woo, M.B. Turner, Executive summary: Heart disease and stroke statistics-2013 update: A Report from the American Heart Association, Circulation. 127 (2013) 143–152.
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  • [20] N. Gençer, O. Arslan, Purification human PON1Q192 and PON1R192 isoenzymes by hydrophobic interaction chromatography and investigation of the inhibition by metals., Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences. 877 (2009) 134–40.
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  • [36] R.C. Brown, Z.Q. Han, C. Cascio, V. Papadopoulos, Oxidative stress-mediated DHEA formation in Alzheimer’s disease pathology, NEUROBIOLOGY OF AGING. 24 (2003) 57–65.
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  • [38] X. Brazzolotto, J. Gaillard, K. Pantopoulos, M.W. Hentze, J.M. Moulis, Human cytoplasmic aconitase (iron regulatory protein 1) is converted into its {[}3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding, JOURNAL OF BIOLOGICAL CHEMISTRY. 274 (1999) 21625–21630.
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Yıl 2017, Cilt: 3 Sayı: 1, 59 - 68, 28.08.2017
https://doi.org/10.23884/mejs.2017.3.1.07

Öz

Kaynakça

  • [1] B. Mackness, P.N. Durrington, M.I. Mackness, Human Serum Paraoxonase, General Pharmacology: The Vascular System. 31 (1998) 329–336.
  • [2] N. Ferré, J. Camps, E. Prats, E. Vilella, A. Paul, L. Figuera, J. Joven, Serum paraoxonase activity: A new additional test for the improved evaluation of chronic liver damage, Clinical Chemistry. 48 (2002) 261–268.
  • [3] N. Forti, J. Diament, Lipoproteínas de alta densidade: aspectos metabólicos, clínicos, epidemiológicos e de intervenção terapêutica. Atualização para os clínicos , Arquivos Brasileiros de Cardiologia . 87 (2006) 671–679.
  • [4] L.G. Costa, A. Vitalone, T.B. Cole, C.E. Furlong, Modulation of paraoxonase (PON1) activity, Biochemical Pharmacology. 69 (2005) 541–550.
  • [5] F.G. Santos, M.K. Becker, V.S. Corrêa, D.N. Garcia, S.C. Vale, J.A. Crespo-Ribeiro, C.C. Barros, A. Schneider, The effect of the paraoxonase 1 (PON1) T(-107)C polymorphism on serum PON1 activity in women is dependent on fatty acid intake, Nutrition Research. 36 (2016) 9–15.
  • [6] T. Suehiro, T. Nakamura, M. Inoue, T. Shiinoki, Y. Ikeda, Y. Kumon, M. Shindo, H. Tanaka, K. Hashimoto, A polymorphism upstream from the human paraoxonase (PON1) gene and its association with PON1 expression, Atherosclerosis. 150 (2000) 295–298.
  • [7] A.S. Go, D. Mozaffarian, V.L. Roger, E.J. Benjamin, J.D. Berry, W.B. Borden, D.M. Bravata, S. Dai, E.S. Ford, C.S. Fox, S. Franco, H.J. Fullerton, C. Gillespie, S.M. Hailpern, J.A. Heit, V.J. Howard, M.D. Huffman, B.M. Kissela, S.J. Kittner, D.T. Lackland, J.H. Lichtman, L.D. Lisabeth, D. Magid, G.M. Marcus, A. Marelli, D.B. Matchar, D.K. McGuire, E.R. Mohler, C.S. Moy, M.E. Mussolino, G. Nichol, N.P. Paynter, P.J. Schreiner, P.D. Sorlie, J. Stein, T.N. Turan, S.S. Virani, N.D. Wong, D. Woo, M.B. Turner, Executive summary: Heart disease and stroke statistics-2013 update: A Report from the American Heart Association, Circulation. 127 (2013) 143–152.
  • [8] S. Hsu, V.K. Ton, M. Dominique Ashen, S.S. Martin, T.J. Gluckman, P. Kohli, S.D. Sisson, R.S. Blumenthal, M.J. Blaha, A clinician’s guide to the ABCs of cardiovascular disease prevention: The johns hopkins ciccarone center for the prevention of heart disease and american college of cardiology cardiosource approach to the million hearts initiative, Clinical Cardiology. 36 (2013) 383–393.
  • [9] M. Barton, Prevention and endothelial therapy of coronary artery disease, Current Opinion in Pharmacology. 13 (2013) 226–241.
  • [10] T. Watanabe, S. Haraoka, T. Shimokama, Inflammatory and immunological nature of atherosclerosis, International Journal of Cardiology. 54, Supple (1996) S51–S60.
  • [11] R.F. Redberg, E.J. Benjamin, V. Bittner, L.T. Braun, D.C. Goff Jr., S. Havas, D.R. Labarthe, M.C. Limacher, D.M. Lloyd-Jones, S. Mora, T.A. Pearson, M.J. Radford, G.W. Smetana, J.A. Spertus, E.W. Swegler, ACCF/AHA 2009 performance measures for primary prevention of cardiovascular disease in adults: a report of the American College of Cardiology Foundation/American Heart Association Task Force on Performance Measures (Writing Committee to Develop Performanc, J Am Coll Cardiol. 54 (2009) 1364–1405.
  • [12] S.-Y. Eom, Y.-S. Kim, C.-J. Lee, C.-H. Lee, Y.-D. Kim, H. Kim, Effects of Intronic and Exonic Polymorphisms of Paraoxonase 1 (PON1) Gene on Serum PON1 Activity in a Korean Population, J Korean Med Sci. 26 (2011) 720–725.
  • [13] T. Bhattacharyya, N. SJ, T. EJ, et al, RElationship of paraoxonase 1 (pon1) gene polymorphisms and functional activity with systemic oxidative stress and cardiovascular risk, JAMA. 299 (2008) 1265–1276.
  • [14] T. Ito, H. Yasue, M. Yoshimura, S. Nakamura, M. Nakayama, Y. Shimasaki, E. Harada, Y. Mizuno, H. Kawano, H. Ogawa, Paraoxonase gene Gln192Arg (Q192R) polymorphism is associated with coronary artery spasm, Human Genetics. 110 (2001) 89–94.
  • [15] M. Wang, X. Lang, L. Zou, S. Huang, Z. Xu, Four genetic polymorphisms of paraoxonase gene and risk of coronary heart disease: A meta-analysis based on 88 case–control studies, Atherosclerosis. 214 (2011) 377–385.
  • [16] M.I. Mackness, S. Arrol, C. Abbott, P.N. Durrington, Protection of low-density lipoprotein against oxidative modification by high-density lipoprotein associated paraoxonase, Atherosclerosis. 104 (1993) 129–135.
  • [17] a I. Rupérez, O. López-Guarnido, F. Gil, J. Olza, M. Gil-Campos, R. Leis, R. Tojo, R. Cañete, a Gil, C.M. Aguilera, Paraoxonase 1 activities and genetic variation in childhood obesity., The British Journal of Nutrition. 110 (2013) 1639–47.
  • [18] M. Aviram, M. Rosenblat, C.L. Bisgaier, R.S. Newton, S.L. Primo-Parmo, B.N. La Du, Paraoxonase inhibits high-density lipoprotein oxidation and preserves its functions. A possible peroxidative role for paraoxonase., The Journal of Clinical Investigation. 101 (1998) 1581–1590.
  • [19] S. Sinan, F. Kockar, O. Arslan, Novel purification strategy for human PON1 and inhibition of the activity by cephalosporin and aminoglikozide derived antibiotics., Biochimie. 88 (2006) 565–74.
  • [20] N. Gençer, O. Arslan, Purification human PON1Q192 and PON1R192 isoenzymes by hydrophobic interaction chromatography and investigation of the inhibition by metals., Journal of Chromatography. B, Analytical Technologies in the Biomedical and Life Sciences. 877 (2009) 134–40.
  • [21] K.N. Gan, A. Smolen, H.W. Eckerson, B.N. La Du, Purification of human serum paraoxonase/arylesterase. Evidence for one esterase catalyzing both activities., Drug Metabolism and Disposition: The Biological Fate of Chemicals. 19 (1991) 100–106.
  • [22] M. Stefek, A. Gajdosik, A. Gajdosikova, L. Krizanova, p-dimethylaminobenzaldehyde-reactive substances in tail tendon collagen of streptozotocin-diabetic rats: Temporal relation to biomechanical properties and advanced glycation endproduct (AGE)-related fluorescence, Biochimica et Biophysica Acta - Molecular Basis of Disease. 1502 (2000) 398–404.
  • [23] M.I. Mahmoud, J.J. Potter, O.M. Colvin, J. Hilton, E. Mezey, Effect of 4-(diethylamino)benzaldehyde on ethanol metabolism in mice., Alcoholism, Clinical and Experimental Research. 17 (1993) 1223–1227.
  • [24] S. Yang, P. Savvides, L. Liu, S.L. Gerson, Y. Xu, Development and validation of an LC-MS/MS method for pharmacokinetic study of methoxyamine in phase I clinical trial, Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences. 901 (2012) 25–33.
  • [25] G.L. Miller, Use of Dinitrosalicylic Acid Reagent for Determination of Reducing Sugar, Analytical Chemistry. 31 (1959) 426–428.
  • [26] J.F. Robyt, W.J. Whelan, Reducing value methods for maltodextrins. I. Chain-length dependence of alkaline 3,5-dinitrosalicylate and chain-length independence of alkaline copper., Analytical Biochemistry. 45 (1972) 510–516.
  • [27] S. Akkarachiyasit, P. Charoenlertkul, S. Yibchok-Anun, S. Adisakwattana, Inhibitory activities of cyanidin and its glycosides and synergistic effect with acarbose against intestinal-glucosidase and pancreatic-amylase, International Journal of Molecular Sciences. 11 (2010) 3387–3396.
  • [28] C. Alina, P. Vasilica, M. Eugen, F. Sanda, Spectrophotometric Studies About Amylase Activity in Starch Hydrolysis Reaction, (2012) 1–16.
  • [29] A. Kumar, A. Pandith, H.-S. Kim, Pyrenebutylamidopropylimidazole as a multi-analyte sensor for 3,5-dinitrosalicylic acid and Hg2+ ions, JOURNAL OF LUMINESCENCE. 172 (2016) 309–316.
  • [30] H. Nyambe-Silavwe, J.A. Villa-Rodriguez, I. Ifie, M. Holmes, E. Aydin, J.M. Jensen, G. Williamson, Inhibition of human alpha-amylase by dietary polyphenols, JOURNAL OF FUNCTIONAL FOODS. 19 (2015) 723–732.
  • [31] S.J. Mulware, Trace elements and carcinogenicity: a subject in review, 3 BIOTECH. 3 (2013) 85–96.
  • [32] P. Boffetta, Carcinogenicity of trace elements with reference to evaluations made by the International Agency for Research on Cancer., Scandinavian Journal of Work, Environment & Health. 19 Suppl 1 (1993) 67–70.
  • [33] Some traditional herbal medicines, some mycotoxins, naphthalene and styrene., IARC Monographs on the Evaluation of Carcinogenic Risks to Humans / World Health Organization, International Agency for Research on Cancer. 82 (2002) 1–556.
  • [34] K. V Rajagopalan, Competitive Inhibition of Enzyme by Urea , 236 (1961).
  • [35] C. a S. Rn, Sigma brand products are sold through Sigma-Aldrich, Inc. Sigma-Aldrich, Inc. warrants that its products conform to the information contained in this and other Sigma-Aldrich publications. Purchaser must determine the suitability of the product(s) for thei, Solutions. 173 (2003) 6628.
  • [36] R.C. Brown, Z.Q. Han, C. Cascio, V. Papadopoulos, Oxidative stress-mediated DHEA formation in Alzheimer’s disease pathology, NEUROBIOLOGY OF AGING. 24 (2003) 57–65.
  • [37] Z.Z. Guan, X. Zhang, M. Mousavi, J.Y. Tian, C. Unger, A. Nordberg, Reduced expression of neuronal nicotinic acetylcholine receptors during the early stages of damage by oxidative stress in PC12 cells, JOURNAL OF NEUROSCIENCE RESEARCH. 66 (2001) 551–558.
  • [38] X. Brazzolotto, J. Gaillard, K. Pantopoulos, M.W. Hentze, J.M. Moulis, Human cytoplasmic aconitase (iron regulatory protein 1) is converted into its {[}3Fe-4S] form by hydrogen peroxide in vitro but is not activated for iron-responsive element binding, JOURNAL OF BIOLOGICAL CHEMISTRY. 274 (1999) 21625–21630.
  • [39] K.M. Khan, F. Rahim, A. Khan, M. Shabeer, S. Hussain, W. Rehman, M. Taha, M. Khan, S. Perveen, M.I. Choudhary, Synthesis and structure-activity relationship of thiobarbituric acid derivatives as potent inhibitors of urease., Bioorganic & Medicinal Chemistry. 22 (2014) 4119–23.
  • [40] M.D. Angelica, Y. Fong, NIH Public Access, October. 141 (2008) 520–529.
  • [41] I.H. Bae, J.K. Choi, C. Chough, S.J. Keum, H. Kim, S.K. Jang, B.M. Kim, Potent hepatitis C virus NS5A inhibitors containing a benzidine core, ACS Medicinal Chemistry Letters. 5 (2014) 255–258.
  • [42] A.M. Vetrano, D.E. Heck, T.M. Mariano, V. Mishin, D.L. Laskin, J.D. Laskin, Characterization of the oxidase activity in mammalian catalase, Journal of Biological Chemistry. 280 (2005) 35372–35381.
  • [43] J. Gold, Proposed treatment of cancer by inhibition of gluconeogenesis., Oncology. 22 (1968) 185–207.
  • [44] J. Gold, Inhibition of Walker 256 intramuscular carcinoma in rats by administration of hydrazine sulfate., Oncology. 25 (1971) 66–71.
  • [45] J. Gold, Cancer cachexia and gluconeogenesis., Annals of the New York Academy of Sciences. 230 (1974) 103–110.
  • [46] J. Gold, Inhibition by hydrazine sulfate and various hydrazides, of in vivo growth of Walker 256 intramuscular carcinoma, B-16 melanoma, Murphy-Sturm lymphosarcoma and L-1210 solid leukemia., Oncology. 27 (1973) 69–80.
  • [47] V.M. Dilman, V.N. Anisimov, A.I. Kolosov, L.N. Bulovskaya, On the relationship between the activity of acetylation, growth of experimental tumors and efficacy of their suppression by hydrazine sulphate., Oncology. 33 (1976) 219–221.
  • [48] B. Grubbs, W. Rogers, I. Cameron, Total parenteral nutrition and inhibition of gluconeogenesis on tumor-host responses., Oncology. 36 (1979) 216–223.
  • [49] J. Gold, Enhancement by hydrazine sulfate of antitumor effectiveness of cytoxan, mitomycin C, methotrexate and bleomycin, in walker 256 carcinosarcoma in rats., Oncology. 31 (1975) 44–53.
  • [50] J. Gold, Potentiation by clofibrate of in-vivo tumor inhibition by hydrazine sulfate and cytotoxic agents, in Walker 256 carcinosarcoma., Cancer Biochemistry Biophysics. 3 (1978) 41–45.
  • [51] J. Gold, Hydrazine sulfate: A current perspective, Nutrition and Cancer. 9 (1987) 59–66.
  • [52] J. Gold, Inhibition of gluconeogenesis at the phosphoenolpyruvate carboxykinase and pyruvate carboxylase reactions, as a means of cancer chemotherapy., Oncology. 29 (1974) 74–89.
  • [53] M.O. Kaya, O. Arslan, O.O. Guler, A new affinity method for purification of bovine testicular hyaluronidase enzyme and an investigation of the effects of some compounds on this enzyme., Journal of Enzyme Inhibition and Medicinal Chemistry. 30 (2015) 524–7.
  • [54] Mustafa Oğuzhan Kaya, Yesim Kaya, Gülsah Çelik, Figen Kurtulus, Oktay Arslan, Özen Özensoy Güler, Differential in vitro inhibition studies of some cerium vanadate derivatives on Xanthine\noxidase, 6366 (2015).
Toplam 54 adet kaynakça vardır.

Ayrıntılar

Birincil Dil İngilizce
Bölüm Makale
Yazarlar

Mustafa Oğuzhan Kaya

Yayımlanma Tarihi 28 Ağustos 2017
Gönderilme Tarihi 4 Haziran 2017
Yayımlandığı Sayı Yıl 2017 Cilt: 3 Sayı: 1

Kaynak Göster

IEEE M. O. Kaya, “OUT-OF-MIND INHIBITORS OF HUMAN SERUM PARAOXONASE 1 (PON1): AN IN VITRO STUDY”, MEJS, c. 3, sy. 1, ss. 59–68, 2017, doi: 10.23884/mejs.2017.3.1.07.

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