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.
Keywords: Diabetes mellitus; Erythrocyte membranes; Na+,K+-ATPase; Acetyl choline esterase; Butyryl chotine esterase; Glycosylation
Full Text
The Full Text of this article is available as a PDF (545.3 KB).
References
- 1.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. [PubMed]
- 2.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., Drouin P. Multicenter evaluation of the DCA 2000 system for measuring evaluation of the glycated hemoglobin. Diabetes & Metabolism. 1997;23:195–201. [PubMed] [Google Scholar]
- 3.Rapaport S. I. Blood and Plasma Proteins: Functions and Composition of Blood. In: West J. B., editor. Best and Taylor's Physiological Basis of Medical Practice. 11th edn. Baltimore: Williams and Wilkins; 1985. pp. 334–340. [Google Scholar]
- 4.Kowluru A., Kowluru R. A., Bitensky M. W. Nonenzymatic glycosylation of erythrocyte cytoskeletal proteins in diabetes mellitus. In: Belfiore F., Molinatti G. M., Willianmson J. R., editors. Frontiers in Diabetes. Basel: Karger; 1978. pp. 190–194. [Google Scholar]
- 5.Gamer M. H., Bahador A., Sachs G. Nonenzymatic glycation of Na+,K+ ATPase. J. Biol. Chem. 1990;265:15058–15066. [PubMed] [Google Scholar]
- 6.Ver A., Cserwely P., Banyasz T., Kovacs T., Somogyi J. Alterations in the properties and isoform ratios of brain Na+,K+ ATPase in streptozotocin diabetic rats. Biochim. Biophys. Acta. 1995;1237:143–150. doi: 10.1016/0005-2736(95)00099-O. [DOI] [PubMed] [Google Scholar]
- 7.Ku D. D., Roberts R. B., Sellers B. M., Meezan E. Regression of renal hypertrophy and elevated renal Na+,K+ ATPase activity after insulin treatment in streptozotocin-diabetic rats. Endocrinol. 1987;120:2166–2173. doi: 10.1210/endo-120-5-2166. [DOI] [PubMed] [Google Scholar]
- 8.Agrawal V. R., Rastogi A. K., Sahib M. K., Sagar P. In vitro insulin effect on acetylcholine esterase of erythrocyte membranes of normal and diabetic rats. Acta Diabetol. Lat. 1985;22:359–363. doi: 10.1007/BF02624755. [DOI] [PubMed] [Google Scholar]
- 9.Suhail M., Rizvi S. I. Erythrocyte membrane acetylcholineesterase in type I (insulin-dependent) diabetes mellitus. Biochem. J. 1989;259:897–899. doi: 10.1042/bj2590897. [DOI] [PMC free article] [PubMed] [Google Scholar]
- 10.Patel B. N., Mackness M. I., Harty D. W., Arros S., Boot-Handford R. P., Durrington P. N. Serum esterase activities and hyperlipidaemia in the streptozotocin-diabetic rat. Biochim. Biophys. Acta. 1990;1035:113–116. doi: 10.1016/0304-4165(90)90182-v. [DOI] [PubMed] [Google Scholar]
- 11.Oreskovic K., Kunec-Vajic E. Pseudocholinesterase in alloxan-diabetic rats. Chem. Pathol. Pharmacol. 1992;78:117–120. [PubMed] [Google Scholar]
- 12.Baldini P., Ineerpi S., Pascale E., Rinaldi C., Verna R., Luly P. Insulin effects on human red blood cells. Mol. Cell. Endocrinol. 1986;46:93–102. doi: 10.1016/0303-7207(86)90087-0. [DOI] [PubMed] [Google Scholar]
- 13.Zimmerman B. R. Sulfonylureas. Current therapies of diabetes. 1997;26:511–522. doi: 10.1016/s0889-8529(05)70264-4. [DOI] [PubMed] [Google Scholar]
- 14.Romano G., Patti L., Innelli F., Marino L. D., Annuzzi G., Lavicoli M., Coronel G. A., Riccardi G., Rivellese A. A. Insulin and sulfonylurea therapy in NIDDM patients: Are the effects on lipoprotein metabolism different even with similar blood glucose control? Diabetes. 1997;46:1601–1606. doi: 10.2337/diabetes.46.10.1601. [DOI] [PubMed] [Google Scholar]
- 15.Kumthekar M. M., Katyare S. S. Altered kinetic attributes of Na+,K+ ATPase activity in kidney, brain and erythrocyte membranes in alloxan-diabetic rats. Ind. J. Exptl. Biol. 1992;30:26–32. [PubMed] [Google Scholar]
- 16.Fiske C. H., Subba Row Y. Colorimetric determination of phosphorous. J. Biol. Chem. 1925;66:375–400. [Google Scholar]
- 17.Dixon M., Webb C. Enzymes. London: Longman; 1979. pp. 47–206. [Google Scholar]
- 18.Dave K. R., Syal A. R., Katyare S. S. Tissue cholinesterases. A comparative study of their kinetic properties. Z. Neuroforsch. 2000;55 C:100–108. doi: 10.1515/znc-2000-1-219. [DOI] [PubMed] [Google Scholar]
- 19.Ellman G. L., Courtney K. V., Anders V., Featherstone R. M. A new and rapid colorimetric determination of acetylcholineesterase activity. Biochem. Pharmacol. 1961;7:88–95. doi: 10.1016/0006-2952(61)90145-9. [DOI] [PubMed] [Google Scholar]
- 20.Godkar P. Text Book of Laboratory Technology. Bombay: Bhalani Publishing House; 1994. pp. 93–117. [Google Scholar]
- 21.Lowry O. H., Rosebrough N. J., Farr A. L., Randall R. J. Protein measurement with Folin phenol reagent. J. Biol. Chem. 1951;193:265–275. [PubMed] [Google Scholar]
- 22.Massoulie J., Pezementi L., Bon S., Krejci E., Vallette F-M. Molecular and cellular biology of cholinesterases. Prog. Neurobiol. 1993;41:31–91. doi: 10.1016/0301-0082(93)90040-Y. [DOI] [PubMed] [Google Scholar]
- 23.Robinson J. D., Flashner M. S. The (Na+−K+)-activated ATPase. Enzymatic and transport propeties. Biochim. Biophys. Acta. 1979;549:145–176. doi: 10.1016/0304-4173(79)90013-2. [DOI] [PubMed] [Google Scholar]
- 24.Ido Y., Vindigni A., Chang K., Stramm L., Chance R., Heath W. F., DiMarchi R. D., DiCera E., Williamson J. R. Prevention of vascular and neural dysfunction in diabetic rats by C-peptide. Science. 1998;277:563–566. doi: 10.1126/science.277.5325.563. [DOI] [PubMed] [Google Scholar]
