Abstract
New findings on organization of blood cell cytoskeleton represent an exciting aspect of modem cell biology and hematology, which is an interesting investigation to study diabetes. The present study was undertaken in 150 subjects. Out of these, 30 subjects were controls (Group I) and 30 were type-2 diabetics without any complication (Group II), while remaining 90 subjects were type-2 diabetics with complication (Group III). We determined erythrocyte spectrin and hemoglobin glycosylation and also estimated plasma lipid peroxide, nitric oxide and erythrocyte glutathione peroxidase activity to assess the status of oxidative stress. There was a significant increase in spectrin (P<0.001) and hemoglobin (P<0.001) glycosylation in Group II and III as compared to Group I and spectrin glycosylation was nearly three times more as compared to hemoglobin, whereas plasma levels of lipid peroxide (P<0.001) as well as nitric oxide (P<0.001) were found to be significantly increased and GPx activity (P<0.001) was significantly decreased in Group II and III as compared to Group I. However, it was also observed that spectrin (P>0.05) and hemoglobin (P>0.05) glycosylation was not significantly different in Group II and III. In contrast, there was significant rise in lipid peroxide (P<0.001), nitric oxide (P<0.001) and fall in GPx activity (P<0.001) in Group III when compared to Group II. Increased erythrocyte protein glycosylation and oxidative stress is clearly evident from our study. However, to understand the exact interplay between these two mechanisms, further studies are required.
This is a preview of subscription content, log in via an institution to check access.
Similar content being viewed by others
References
Yeolekar ME, Borade PS. Classification of diabetes and its implications. J Gen Med 2002; 14: 7–9.
Raman R, Biswas J. Occular complications of diabetes mellitus. J Gen Med 2002; 14: 21–7.
Scwartz RS, Madsen JW, Raybicky AC, Nagel RL. Oxidation of spectrin and deformability defects in diabetic erythrocytes. Diabetes 1991; 40: 701–8.
Lux SE. Spectrin Actin membrane skeleton of normal and abnormal red blood cells. Semin. in Hematol 1979; 16: 21–51.
McMillan DE, Brooks SM. Erythrocyte spectrin glycosylation in diabetes. Diabetes 1982; 31: 64–9.
Konukoglu D, Kemerli GD, Sabunca T, Hatemi HH. Protein carbonyl content in erythrocyte membrane in type-2 diabetic patients. Horm Metab Res 2002; 34: 367–70.
Resm H, Peketin C, Guner G. Erythrocyte membrane cytoskeletal protein glycation and oxidation in short term diabetic rabbits. Clin Exp Med 2001; 1: 187–93.
Parthibhan A, Vijaylingam S, Shanmughsundaram K, Mohan R. Oxidative stress and the development of diabetic complications, antioxidant and lipid peroxidation in erythrocytes and cell membrane. Bio Int 1995; 19: 987–92.
Aggarwal KK. Diabetes and oxidative stress. Asian J Diabetol 2001; 3: 12.
Pasaoglu H, Suncak B, Bukan N. Lipid peroxidation and resistance to oxidation in patients with type-2 diabetes mellitus. Tohoku J Exp Med 2004; 203: 211–8.
Moncada S, Higgs A. The L-Arginine-Nitric oxide pathway. New Eng J Med 1993; 329: 2002–12.
Irshad M, Chaudhari S. Oxidant antioxidant system; Role and significance in human body. Ind J Exp Bio 2002; 40: 1233–9.
Sekerglu M, Sahin H, Dulger H, Algun E. The effect of dietary treatment on erythrocyte lipid peroxidation, Superoxide dismutase, Glutathione Peroxidase and serum lipid peroxidation in patients with type-2 Diabetes Mellitus. Clin Biochem 2000; 33: 669–74.
Flukiger R, Winterhalter KH. Invitro synthesis of HbA10. Fed. Eur Biochem Soc Lett 1976; 71: 356–60.
Coetzer T, Zail S. Spectrin tetramer-dimmer in hereditary elliptocytosis. Blood 1982; 59: 900–5.
Lowry OH, Rosenbrough NJ, Farr AL, Randall RJ. Protein measurement with folin phenol reagent. J Biol Chem 1951; 193: 265–75.
Parker KM, England JD, Costa JD, Hess RL, Goldstein DE. Improved colorimetric assay for glycosylated hemoglobin. Clin Chem 1981; 27: 666–72.
Satoh K. Serum lipid peroxide in cerebrovascular disorders determined by new colorimetric method. Clin Chim Acta 1978; 90: 37–43.
Cortas NK, Wakid NW. Determination of inorganic nitrate in serum and urine by a kinetic cadmium-reduction method. Clin Chem 1990; 36: 1440–3.
Gurler B, Vural H, Yilmaz N, Oguz H, Satici A, Aksoy N. The role of oxidative stress in diabetic retinopathy. Eye 2000; 14: 730–5.
Lux SE, John KM, Ukena TE. Diminished spectrin extraction from ATP depleted human erythrocytes. Evidences relating spectrin to changes in erythrocyte shape and deformability. J Clin Invest 1978; 61: 815–27.
Moris BJ, Markus A, Gleen CL. Association of a functional inducible nitric oxide synthase promoter varient with complications in type-2 diabetes. J Mol Med 2002; 80: 96–104.
Young IS, Woodside JV. Antioxidant in health and disease. J Clin Path 2001; 34: 176–86.
Condell RA, Tappel AL. Evidence for suitability of glutathione peroxidase as a protective enzyme: Studies of oxidative damage restoration and proteolysis. Arch Biochem Biophys 1983; 223: 407–16.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Mahindrakar, Y.S., Suryakar, A.N., Ankush, R.D. et al. Comparison between erythrocyte hemoglobin and spectrin glycosylation and role of oxidative stress in type-2 diabetes mellitus. Indian J Clin Biochem 22, 91–94 (2007). https://doi.org/10.1007/BF02912888
Issue Date:
DOI: https://doi.org/10.1007/BF02912888