Caffeine effect on adenosine deaminase catalysis: A new look at the effect of caffeine on adenosine deaminase activity

Document Type: Articles

Authors

1 Department of Biotechnology, Faculty of Chemistry, University of Kashan, Kashan, Iran.

2 Department of Organic Chemistry, Faculty of Chemistry, University of Kashan, Kashan, Iran.

3 Departmentof Biotechnology, Faculty of Biological Sciences, Alzahra University, Tehran, Iran.

Abstract

The effect of physiological concentrations of caffeine (purified from Persian tea) on adenosine deaminase (ADA) activity at physiological and pathological concentrations of adenosine (as substrate) in 50 mM Tris-HCl buffer (pH 7.3) at 37°C was investigated, using UV-VIS spectroscopy. ADA exhibited a bi-phasic activity behavior and both phases showed positive cooperativities indicating adenosine has at least two regulatory sites on ADA molecule. We proposed a mechanism for the inhibitory effect of caffeine on ADA catalytic activity by analyzing ADA kinetic behavior at various physiological concentrations of caffeine (10, 30, 70 mM): Caffeine dominantly resulted in decreased catalytic activity of ADA via reducing the positive homotropic effect of adenosine on ADA activity. Surprisingly, it also showed a very weak but significant activatory effect on ADA activity in a concentration-dependent manner. To the best of our knowledge, this is the first report on the dual effect of caffeine on ADA activity.
 

Keywords


[1] R. Hirchhorn, H. Ratech, Isozymes Curr. Top. Biol. Med. Res. 4 (1980) 131-157.
[2] P.E. Doddona, D.S. Schewach, W.N. Kelly, P. Argos, A.F. Markham, S.H. Orkin, J. Biol. Chem. 259 (1984) 12101-12106.
[3] W.F. Schwindinger, L.J. Mihalcik, K.E. Giger, K.S. Betz, A.M. Stauffer, J. Linden, D. Herve, J. Robishaw, J. Biol. Chem. 285 (2010) 29787-29796.
[4] D.A. Pelligrino, H.L. Xu, F. Vetri, J. Alzheimers Dis. 20 (2010) S51-S62.
[5] A. Adams, R.A. Harkness, Clin. Exp. Immunol. 26 (1976) 647-649.
[6] G.C. Mills, F.C. Schmalstieg, K.B. Trimmer, A.S. Goldman, R.M. Goldblum, Proc. Natl. Acad. Sci. 73 (1976) 2867-2871.
[7] C. Herrera, V. Casado, F. Ciruela, P. Schofield, J. Mallol, C. Lluis, R. Franco, Mol. Pharmacol. 59 (2001) 127-134.
[8] L. Antonioli, M. Fornai, R. Colucci, N. Ghisu, F. Da Settimo, G. Natale, O. Kastsiuchenka, E. Duranti, A. Virdis, C. Vassalle, C. La Motta, L. Mugnaini, M.C. Breschi, C. Blandizzi, M. del Taca, J. Pharmacol. Exp. Ther. 322 (2007) 435-442.
[9] L.S. Singh, R. Sharma, Mol. Cell Biochem. 204 (2000) 127-134.
[10] S. Pornbanlualap, P. Chalopagorn, Protein Expression Purif. 78 (2011) 167-173.
[11] K. Kathiresan, K. Saravanakumar, S.K. Sahu, M. Sivasankaran, 3 Biotech. 4 (2013) 235-239.
[12] G.J. Peters, A. Oosterhof, J.H. Veerkamp, Biol. Neonate 42 (1982) 195-200.
[13] J. Meier, M.S. Coleman, J.J. Hutton, Br. J. Cancer 33 (1976) 312-319.
[14] E. Dolezelova, M. Zurovec, T. Dolezal, P. Simek, P.J. Bryant, Insect Biochem. Mol. Biol. 35 (2005) 381-389.
[15] K. Kroll, M.K. Kelm, K.F. Bürrig, J. Schrader, Circ. Res. 64 (1989) 1147-1157.
[16] A. Borowiec, K. Lechward, K. Tkacz-Stachowska, A.C. Składanowski, Acta Biochim. Pol. 53 (2006) 269-278.
[17] H. Wang, L. Chen, Y. Xu, Q. Zeng, X. Zhang, Q. Zhao, L. Ding, LWT-Food Sci. Technol. 44 (2011) 1490-1495.
[18] A. Senol, A. Aydin, J. Food Eng. 75 (2006) 565-573.
[19] H. İçen, M. Gürü, J. Supercrit. Fluids 55 (2010) 156-160.
[20] J. Tello, M. Viguera, L. Calvo, J. Supercrit. Fluids 59 (2011) 53-60.
[21] N.R. Phillips, R.J. Havel, J.P. Kane, Arteriosclerosis 1 (1981)13-24.
[22] M.L. Nurminen, L. Niittynen, R. Korpela, H. Vapaatalo, Eur. J. Clin. Nutr. 53 (1999) 831-839.
[23] M.B. Katan, E. Schouten, Am. J. Clin. Nutr. 81 (2005) 539-540.
[24] H.M. Dreher, J. Psychosom. Res. 54 (2003) 191-198.
[25] G. Nunnari, E. Argyris, J. Fang, K.E. Mehlman, R.J. Pomerantz, R. Daniel, Virology 335 (2005) 177-184.
[26] G. Cristalli, S. Costanzi, C. Lambertucci, G. Lupidi, S. Vittori, R. Volpini, E. Camaioni, Med. Res. Rev. 21 (2001)105-128.
[27] G. Ataie, F. Zonoozi, A. Divsalar, A.A. Moosavi-Movahedi, A.A. Saboury, S. Safarian, M. Habbibi-Rezaei, L. Gachkar, S. Mardanian, Pejouhandeh J. 10 (2005) 65-72.
[28] A.A. Saboury, A. Divsalar, G.A. Jafari, A.A. Moosavi-Movahedi, M.R. Housaindokht, G.H. Hakimelahi, J. Biochem. Mol. Biol. 35 (2002) 302-305.
[29] A.A. Moosavi-Movahedi, B. Samiee, G.H. Hakimelahi, J. Colloid Interface Sci. 161 (1993) 53-56.
[30] D. Ajloo, A.A. Saboury, N. Haghi-Asli, G. Ataei-Jafarai, A.A. Moosavi-Movahedi, M. Ahmadi, K. Mahnam, S. Namaki, J. Enzyme Inhib. Med. Chem. 22 (2007) 395-406.
[31] S. Alunni, M. Orrù, L. Ottavi, J. Enzyme Inhib. Med. Chem. 23 (2008) 182-189.
[32] A.A. Saboury, A. Divsalar, G. Ataie, M. Amanlou, A.A. Moosavi-Movahedi, G.H. Hakimelahi, Acta Biochim. Pol. 50 (2003) 849-855.
[33] G. Ataie, A.A. Moosavi-Movahedi, A.A. Saboury, G.H. Hakimelahi, J.R. Hwu, S.C. Tsay, Int. J. Biol. Macromol. 27 (2000) 29-33.
[34] T.J. Mason, Chemistry with Ultrasound, 28th Ed., Springer, 1990.
[35] G. Ataie, S. Safarian, A. Divsalar, A.A. Saboury, A.A. Moosavi-Movahedi, B. Ranjbar, G. Cristalli, S. Mardanian, J. Enzyme Inhib. Med. Chem. 19 (2004) 71-78.
[36] A. Levintzki, D.E. Koshland, Proc. Natl. Acad. Sci. 62 (1969) 1121-1128.
[37] G.H. Möser, J. Schrader, A. Deussen, Am. J. Physiol. 256 (1989) 799-806.
[38] M. Claude, L. Marc, V. Xavier, A. Marie-Laure, G. Regis, Crit. Care Med. 28 (2000) 3198-3202.
[39] J.M. Hutzler, T.S. Tracy, Drug Metab. Dispos. 30 (2002) 355-362.
[40] M. Tarnopolsky, C. Cupido, J. Appl. Physiol. 89 (2000) 1719-1724.