Please enter verification code
Sensitivity of Redox Cycle Enzymes in Substantiating the Pathophysiology of Cataract
International Journal of Ophthalmology & Visual Science
Volume 2, Issue 1, February 2017, Pages: 15-21
Received: Feb. 2, 2017; Accepted: Feb. 27, 2017; Published: Mar. 15, 2017
Views 1785      Downloads 137
Syed Parween Ali, Department Medical Laboratory Science, College of Applied Medical Sciences, King Khalid University, Abha, Kingdom of Saudi Arabia
Mohammed Abdul Rasheed, Ministry of Interior, Abha, Kingdom of Saudi Arabia
Mohammed Amanullah, Department of Biochemistry, College of Medicine, King Khalid University, Abha, Kingdom of Saudi Arabia
Article Tools
Follow on us
Oxidative modifications play major role in the formation of cataract. Lens contains several protective mechanisms against oxidizing agents viz. catalase, superoxide dismutase, glutathione reductase, glutathione peroxidase, and ascorbic acid. To explore the oxidative damage that might be occurring with 'Invitro' development of cataracts induced by sugars, H2O2 and steroids. We examined redox status of cataractous lenses by analysing enzymatic defence meachanisms. Lenses were exposed to glucose (50 mM) (Group – I); galactose (35 mM) (Group – II) and xylose (30 mM) (Group – III) and maintained at 37°C for 72 hours so as to induce sugar cataract. H2O2 cataract was produced by adding 50 mM (Group – IV) and 100 mM (Group – V), solution to culture media (AAH). Steroid cataract was generated by adding a freshly prepared l x 10-4 M dexamethasone (mw 392.5) (Group – VI) in absolute alcohol to the culture media (AAH) and incubated at 37°C for 72 hours. Subsequent to the development of the cataract, the lenses were homogenized and the specific activity of the enzymes catalase (CAT), glutathione peroxidase and glutathione reductase was assessed. Catalase activity did not show any significant decrease in sugar cataract and steroid cataract but a significant decrease was observed in H2O2 cataract. However a significant decrease in GSH-Px and GSH-Rx were found in all the three types of experimental cataract as compared to control lenses.
Cataract, Catalase, Glutathione Reductase, Glutathione Peroxidase, Free Radicals
To cite this article
Syed Parween Ali, Mohammed Abdul Rasheed, Mohammed Amanullah, Sensitivity of Redox Cycle Enzymes in Substantiating the Pathophysiology of Cataract, International Journal of Ophthalmology & Visual Science. Vol. 2, No. 1, 2017, pp. 15-21. doi: 10.11648/j.ijovs.20170201.14
Copyright © 2017 Authors retain the copyright of this article.
This article is an open access article distributed under the Creative Commons Attribution License ( which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
Aman S. Kataria, John T. Thompson. Cataract Formation and Progression in Patients Less Than 50 Years of Age after Vitrectomy. Ophthalmology Retina. 2016. Available online 23 November. In Press, Corrected Proof.
Kranti Sorte Gawali, Nilam Bhagat Patil. Catalase Activity and Total Antioxidant Capacity in Lens Epithelial Cells of different morphological types of senile Cataract Patients. Int J Res Med. 2016; 5 (1): 92-96.
B. Sanjeev Heemraz, Chan Ning Lee, Pirro G. Hysi, Carole A. Jones, Christopher J. Hammond, Omar A. Mahroo. Changes in quality of life shortly after routine cataract surgery. Canadian Journal of Ophthalmology. 2016; 51 (4): 282–287.
Ewa Kilanczyk, Sujata Saraswat Ohri, Scott R. Whittemore, and Michal Hetman. Antioxidant Protection of NADPH-Depleted Oligodendrocyte Precursor Cells Is Dependent on Supply of Reduced Glutathione. ASN Neuro. 2016; 8 (4): 759091416660404. doi: 10.1177/1759091416660404.
Kenneth R. Hightower, Sharon E. Harrison. Valinomycin cataract: The relative role of calcium and sodium accumulation. Experimental Eye Research. 1982; 34 (6): 941–943.
Aebi H. Catalase. In Methods of enzymatic analysis, Bergmayer HU (ed.)(eds). Academic Press Inc: New York, 1974: 673–677.
Mills GC, Randall HP. Hemoglobin catabolism. II. The protection of hemoglobin from oxidative breakdown in the intact erythrocyte. J Biol Chem. 1958; 232 (2): 589-98.
Beutler E., Kelley B. M. The effect of sodium nitrate on red cell glutathione. Experientia. 1963;19: 96–97. doi: 10.1007/BF02148042.
Racker E. Glutathione reductase from bakers' yeast and beef liver. J. Biol. Chem. 1955; 217: 855-865.
Carlberg I, Mannervik B. Purification and characterization of the flavoenzyme glutathione reductase from rat liver. J Biol Chem. 1975; 250 (14): 5475-80.
Augusteyn R. C. Proten modification in cataract: possible oxidative mechanism. In: Duncan G (ed) Mechanisms of cataract formation in the human lens. Academic Press, London. 1981; 72–115.
Harqing JJ. In. Biomedical, Molecular and Cellular biology of the eye lens John Wiley, New York 1981; 327-365.
Spector A. In the Ocular Lens (Ed. Maisel. H.) Marcel. Dekker. New York. 1985; 405-38.
Fecondo JV, Augusteyn RC. Superoxide dismutase, catalase and glutathione peroxidase in the human cataractous lens. Exp Eye Res. 1983; 36 (1): 15-23.
Dwivide RS, Pratap VB. Role of lipid peroxidation andtracemetal incataractogenesis. IndianJ. Ophthalmol. 1986; 34: 45–51.
Giblin FJ, McCready JP, Schrimscher L, Reddy VN Peroxide-induced effects on lens cation transport following inhibition of glutathione reductase activity in vitro. Exp Eye Res. 1987; 45 (1): 77-91.
Reddan John R, Frank Giblin, Michael D Sevilla, John T Pena. Propyl gallate is a superoxide dismutase mimic and protects cultured lens epithelial cells from H2O2 insult.. Experimental Eye Research. 2003; 76 (1): 49-59 • DOI: 10.1016/S0014-4835(02)00256-7.
Bhat KS, Rao PV. International Symposium on Biological oxidation systems. Banglaore, India:. Lens oxidant scavenger system in rats with galactose induced cataract. 1989; 48.
Bhuyan KC, Bhuyan DK, Podos SM. Lipid peroxidation in cataract of the human. Life Sci.1986; 38: 1463–71.
Chance Britton. Effect of pH upon the reaction kinetics of the enzyme-substrate compounds of catalase. J. Biol. Chem. 1952; 194: 471–481.
Chance B, Higgins J. Peroxidase kinetics in coupled oxidation; an experimental and theoretical study. Arch Biochem Biophys. 1952; 41 (2): 432–441.
Pirie A. Glutathione peroxidase in lens and a source of hydrogen peroxide in aqueous humour. Biochem. J. 1965; 96: 244-53.
Bhuyan KC and Bhuyan DK. Catalase in ocular tissue and its intracellular distribution in corneal epithelium. Am. J. Ophthalmol. 1970; 69: 147-53.
Bhuyan KC and Bhuyan DK and Katzin HM. Spring Meeting of the Association for Research in vision and ophthalmology. 1973.
Giblin FJ, McCready JP, Reddy VN. The role of glutathione metabolism in the detoxification of H2O2 in rabbit lens. Invest Ophthalmol Vis Sci. 1982; 22 (3): 330-5.
Srivastava SK, Lal AK, Ansari NH. Defense system of the lens against oxidative damage: effect of oxidative challenge on cataract formation in glutathione peroxidase deficient-acatalasemic mice. Exp. Eye Res. 1980; 31: 425-33.
Bhuyan KC Bhuyan DK. Regulation of hydrogen peroxide in eye humors. Effect of 3-amino-l H -1,2,4 triazole on catalase and glutathione peroxidase of rabbit eye. Biockim. Biophys. Acta. 1977; 497: 641-51.
Bhuyan KC Bhuyan DK. Superoxide dismutase of the eye. Relative functioning of superoxide dismutase and catalase in protecting the ocular lens from oxidative damage. Biochim. Biophys. Acta. 1978; 542: 28-38.
Dehghan M. H., Bulakh P. M., et al. Proceedings of 51st Annual Conference of All India Opthol Society. 1993.
Science Publishing Group
1 Rockefeller Plaza,
10th and 11th Floors,
New York, NY 10020
Tel: (001)347-983-5186