Abstract
Erythrocyte membrane protein glycosylation increase by 3.4 fold in diabetes. Insulin or sulfonylurea treatment did not reduce the extent of glycosylation. The serum protein glycosylation was comparable in all the groups including control. Erythrocyte membrane Na+,K+-ATPase activity decreased in the diabetics; only insulin treatment partly restored the activity. Erythrocyte membrane acetylcholinesterase activity decreased only in the sulfonylurea treated group. Serum butyrylcholinesterase activity was relatively low in the diabetic and insulin treated diabetic groups. The Km and Vmax of the two components of Na+,K+-ATPase from erythrocyte membranes were differently affected in the diabetic and the two treatment groups. The Vmax of acetylcholinesterase decreased only in the sulfonylurea treated group. Diabetic states resulted in decreased Vmax of components I and II of serum butyrylcholinesterase. In insulin-treated diabetics, component II was absent. Sulfonylurea group resembled diabetics.In vitro incubation with insulin differentially affected the Na+,K+-ATPase and serum butyrylcholinesterase activities.
Similar content being viewed by others
References
Cohen, M. P. (1989) Non enzymatic glycation and enhanced polyol pathway activity in the pathogenesis of diabetic nephropathy, In: Diabetes and Kidney. Contrib. Nephrol. Eds. Heidland A., Koch K. M., Heidbereder E, Karger and Basel, vol. 73, 59–72.
Guerci, B., Durain, D., Leblance, H., Rouland, J. C., Godeau, Th., Charbonnel, B., Mathieu Daude, J. C., Boniface, H., Monnier, L., Dauchy F., Slama G. and Drouin, P. (1997) Multicenter evaluation of the DCA 2000 system for measuring evaluation of the glycated hemoglobin. Diabetes & Metabolism 23, 195–201.
Rapaport, S. I. (1985) Blood and Plasma Proteins: Functions and Composition of Blood, In: Best and Taylor's Physiological Basis of Medical Practice Ed. West J. B. 11th edn. Williams and Wilkins: Baltimore, pp. 334–340.
Kowluru, A., Kowluru, R. A. and Bitensky, M. W. (1978) Nonenzymatic glycosylation of erythrocyte cytoskeletal proteins in diabetes mellitus, In: Frontiers in Diabetes, Eds. Belfiore, F., Molinatti, G. M. and Willianmson, J. R. Karger, Basel: pp. 190–194.
Gamer, M. H., Bahador, A. and Sachs G. (1990) Nonenzymatic glycation of Na+,K+ ATPase. J. Biol. Chem. 265, 15058–15066.
Ver, A., Cserwely P., Banyasz, T., Kovacs, T. and Somogyi, J. (1995) Alterations in the properties and isoform ratios of brain Na+,K+ ATPase in streptozotocin diabetic rats. Biochim. Biophys. Acta 1237, 143–150.
Ku, D. D., Roberts, R. B., Sellers, B. M. and Meezan, E. (1987) Regression of renal hypertrophy and elevated renal Na+,K+ ATPase activity after insulin treatment in streptozotocin-diabetic rats. Endocrinol. 120, 2166–2173.
Agrawal, V. R., Rastogi, A. K., Sahib, M. K. and Sagar, P. (1985) In vitro insulin effect on acetylcholine esterase of erythrocyte membranes of normal and diabetic rats. Acta Diabetol. Lat. 22, 359–363.
Suhail, M. and Rizvi, S. I. (1989) Erythrocyte membrane acetylcholineesterase in type I (insulin-dependent) diabetes mellitus. Biochem. J. 259, 897–899.
Patel, B. N., Mackness, M. I., Harty, D. W., Arros S., Boot-Handford, R. P. and Durrington, (1990) P. N. Serum esterase activities and hyperlipidaemia in the streptozotocin-diabetic rat. Biochim. Biophys. Acta 1035, 113–116.
Oreskovic, K. and Kunec-Vajic, E. (1992) Pseudocholinesterase in alloxan-diabetic rats. Chem. Pathol. Pharmacol. 78, 117–120.
Baldini, P., Ineerpi, S., Pascale, E., Rinaldi, C., Verna, R. and Luly, P. (1986) Insulin effects on human red blood cells. Mol. Cell. Endocrinol. 46, 93–102.
Zimmerman, B. R. (1997) Sulfonylureas. Current therapies of diabetes. 26, 511–522.
Romano, G., Patti, L., Innelli, F., Marino, L. D., Annuzzi, G., Lavicoli, M., Coronel, G. A., Riccardi, G. and Rivellese, A. A. (1997) Insulin and sulfonylurea therapy in NIDDM patients: Are the effects on lipoprotein metabolism different even with similar blood glucose control? Diabetes 46, 1601–1606.
Kumthekar, M. M. and Katyare, S. S. (1992) Altered kinetic attributes of Na+,K+ ATPase activity in kidney, brain and erythrocyte membranes in alloxan-diabetic rats. Ind. J. Exptl. Biol. 30, 26–32.
Fiske, C. H. and Subba Row, Y. (1925) Colorimetric determination of phosphorous. J. Biol. Chem. 66, 375–400.
Dixon, M. and Webb, C. (1979) Enzymes Longman, London, p. 47–206.
Dave, K. R., Syal, A. R. and Katyare, S. S. (2000) Tissue cholinesterases. A comparative study of their kinetic properties. Z. Neuroforsch. 55 C, 100–108.
Ellman, G. L., Courtney, K. V., Anders, V. and Featherstone, R. M. (1961) A new and rapid colorimetric determination of acetylcholineesterase activity. Biochem. Pharmacol. 7, 88–95.
Godkar, P. (1994) Text Book of Laboratory Technology, Bhalani Publishing House, Bombay, p. 93–117.
Lowry, O. H., Rosebrough, N. J., Farr A. L. and Randall R. J. (1951) Protein measurement with Folin phenol reagent. J. Biol. Chem. 193, 265–275.
Massoulie, J. Pezementi, L., Bon, S., Krejci, E. and Vallette, F-M, (1993) Molecular and cellular biology of cholinesterases. Prog. Neurobiol. 41, 31–91.
Robinson, J. D. and Flashner, M. S. (1979) The (Na+−K+)-activated ATPase. Enzymatic and transport propeties. Biochim. Biophys. Acta 549, 145–176.
Ido, Y., Vindigni, A., Chang, K., Stramm, L., Chance, R., Heath W. F., DiMarchi, R. D., DiCera, E. and Williamson, J. R. (1998) Prevention of vascular and neural dysfunction in diabetic rats by C-peptide. Science 277, 563–566.
Author information
Authors and Affiliations
Rights and permissions
About this article
Cite this article
Dave, K.R., Patel, T.H. & Katyare, S.S. Insulin or sulfonylurea treatments of the diabetics differentially affect erythrocyte membrane and serum enzymes and extent of protein glycosylation. Indian J Clin Biochem 16, 81–88 (2001). https://doi.org/10.1007/BF02867573
Issue Date:
DOI: https://doi.org/10.1007/BF02867573