Ramana DCV, Vidyullatha V, Sandhya G, Sudhakar K, Reddy PP

Language: English
References: 14
Page: 1-5
PDF size: 25.80 Kb.

ABSTRACT

Introduction. The imparired Ca2⁺ metabolism in diabetes is a result of several wide spectrum of abnormalities correlation between the high levels of glucose to that of Ca2⁺ ATPase activity and erythrocyte Ca2⁺ in non-insulin depent diabetes mellitus (NIDDM) is studied in this paper.
Materials and methods. Heparinized blood samples were collected from 20 patients with NIDDM. Estimation of total Ca2⁺ was carried out with HCl/1 Lanthanum supernatents of erythrocyte suspension by atomic absorption spectrophotometry. Estimations of membrane bound Ca2⁺ATPase activity was determined by coupled enzyme assay and of membrane glycoprotein was carried out by phenolsulphuric acid method.
Results. The levels of erythrocyte membrane Ca2⁺ ATPase was observed to be 0.532 ± 0.019 µg/mg in controls and 0.321 ± 0.041 µg/mg in NIDDM. There is a significant 0.60 fold decrease in NIDDM when compared with the controls. The levels of membrane glycoprotein was observed to be 59.86 ± 6.3 µg/mg in controls and 38.66 ± 6.9 µg/mg in NIDDM. There is a significant 0.64 fold decrease in NIDDM subjects when compared to controls. The erythrocyte membrane Ca2⁺ was observed to be 0.144 ± 0.02 µg/mg in controls and 0.067 ±0.016 µg/mg in NIDDM (0.46 folds decrease in NIDDM subjects when compared to the controls). Erythrocyte total Ca2⁺ is 0.615 ± 0.102 µg/mg in controls and 2.02 ± 0.08 µg/mg in NIDDM (3.2 folds increase in NIDDM patients when compared to controls).
Discussion. Our results sugest that the cellular Ca2⁺ overload is a major impairment in diabetes which leads to the loss of membrane integrity and the loss of membrane glycoprotein, which was observed to decrease as a result of membrane alteration, and increased osmotic fragility.

REFERENCES

1. Ramana-Devi Ch V, Hema-Prasad M, Padmaja-Reddy T, Reddy P P. Glycosylation of Hemoglobin and erythrocyte membrane proteins mediated changes in osmotic fragility of erythrocytes. Indian J Med Sciences 1997; 51:5-9.

2. Somer H, Chion S, Sung, L A, et al. Erithrocytes in Duchenne muscular dystrophy. Neurology 1979; 29:519-22.

3. Levy J, Gavin J R III, Sowers J R. Diabetes mellitus a disease of abnormal cell Ca2+ homeostasis? Am J Med 1995; 99:222-4.

4. Scharfer W, Pripen J, Mannhold R, et al. Ca2+ + Mg2+ - ATPase activity of human red blood cells in healthy and diabetic volunteers. Klin Wochenschr 1987; 65:17-21.

5. Levi J, Stern Z, Gutman A, et al. Plasma Ca2+ and phosphate levels in an adult non-insulin dependent diabetic population. Calcif Tissue 1986; 39:316-8.

6. Dacie JV, Lewis SM. Practical Haematology, International student edition. London: Churchill Livingstone; 1984. p. 179.

7. Turrin F, Naitana A, Mannuzzu L, Prescarmona G, Arese P. Increased red cell calcium, decrease Ca2+ ATPase and altered membrane proteins during fava-bean hemolysis in glucose 6-phosphate dehydrogenase deficient individuals. Blood 1984; 66:302.

8. Neufeld F F, Ginsburg V. Complex Carbohydrate methods. Enzymol 1966; 8:98.

9. Allo S N, Lincoln T M, Wilson G L, et al. Noninsulin dependent diabetes induced defects in cardiac cellular calcium regulation. Am J Physiol 1991; 260:C1165-71.

10. Foster D W. Diabetes Mellitus. In Fauci AS, Braunwald E, Isselbacher KJ, Wilson JA, Martin JB, Kasper DL, Hauser SL, Longo DL, editors. Harrison's Principles of Internal Medicine, 14 th ed. New York: McGraw-Hill; 1998. p. 2060-81.

11. Levi J, Zher Z, Dubar J C. The effect of glucose and calcium on Ca2+ - ATPase in pancreatic islets isolated from a normal and a non-insulin dependent diabetes mellitus rat model. Metabolism 1998; 47:185-9.

12. Gagliardino JJ, Rossi JP. Ca2+-ATPase in pancreatic islets: Its possible role in the regulation of insulin secretions. Diabetes Metab Rev 1994: 10:1-17.

13. Broconlee M, Blassara H, Cerami A. Nonenzymatic glycosylation and the pathogenesis of diabetic complications. Ann Intern Med 1984; 101:527-37.

14. Hunt JV, Dean RT, Wolf SP. Hydroxyl radical production and auto oxidative glycosylation. Biochem J 1988; 256:205.