Effect of Proteolysis in Erythrocyte Damage of Diabetic Complications

Diabetes is a complex metabolic disorder characterized by defects in the body’s ability to control glucose and insulin homeostasis, and it is estimated that in the future, the annual incidence rate of diabetes will continue to increase worldwide. Currently, it is believed that various complications of diabetes mellitus result from oxidative stress wherein increased free radical production is coupled with low levels of cellular antioxidants (1). Because the human erythrocyte plays a role as an O2 and CO2 transporter, it is constantly exposed to reactive oxygen species (ROS) and oxidative stress. Oxidative stress occurs in cells or tissues when ROS concentration exceeds antioxidant concentration (2). Oxidant damage to proteins makes them more vulnerable to proteolytic degradation by enzymes that recognize modifications like conformational changes and fragmentation. A combination of increased oxidant production and decreased antioxidant levels in the erythrocytes in a diabetes mellitus patient contributes to the vulnerability of glycated hemoglobin to oxidant damage and subsequent proteolytic degradation. Oxidant-damaged hemoglobin is c 2011 Kowsar M.P.Co. All rights reserved. Please cite this paper as: Saravanan G. Effect of Proteolysis in Erythrocyte Damage of Diabetic Complications. Int J Endocriol Metab. 2011; 9(1): 276-7. DOI: 10.5812/Kowsar.1726913X.2068

[1]  P. Ponmurugan,et al.  Ameliorative potential of S-allyl cysteine on oxidative stress in STZ induced diabetic rats. , 2011, Chemico-biological interactions.

[2]  B. Gopalakrishna,et al.  OXIDATIVE STRESS AND PROTEOLYTIC ACTIVITY IN ERYTHROCYTES OF DIABETIC PATIENTS , 2010 .

[3]  S. Manoharan,et al.  Antihyperglycemic and antilipidperoxidative effects ofTephrosia purpurea seed extract in streptozotocin induced diabetic rats , 2007, Indian Journal of Clinical Biochemistry.

[4]  T. Hosaka,et al.  Presence of oxidized protein hydrolase in human cell lines, rat tissues, and human/rat plasma. , 2000, Journal of biochemistry.

[5]  K. Kikugawa,et al.  Purification and characterization of a serine protease in erythrocyte cytosol that is adherent to oxidized membranes and preferentially degrades proteins modified by oxidation and glycation. , 1998, Journal of biochemistry.

[6]  P. Rao,et al.  Increased proteolysis of oxidatively damaged hemoglobin in erythrocyte lysates in diabetes mellitus. , 1994, Clinica chimica acta; international journal of clinical chemistry.

[7]  J. V. Hunt,et al.  Oxidative alterations in the experimental glycation model of diabetes mellitus are due to protein-glucose adduct oxidation. Some fundamental differences in proposed mechanisms of glucose oxidation and oxidant production. , 1993, The Biochemical journal.

[8]  S. Wolff,et al.  Autoxidative Glycosylation and Possible Involvement of Peroxides and Free Radicals in LDL Modification by Glucose , 1990, Diabetes.