A Study on Proteolytic Enzyme Activity in the Erythrocytes of Diabetic Patients

BS, Varashree and Bhat, Gopalakrishna P (2011) A Study on Proteolytic Enzyme Activity in the Erythrocytes of Diabetic Patients. [Journal (On-line/Unpaginated)]

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The present study demonstrates the possibility of increased proteolytic activities in diabetic individuals. Proteolytic activity was measured by the amount of amino group released by the erythrocyte lysate of the diabetic individual using phenylhydrazine treated hemoglobin as substrate. The proteolytic activity in erythrocyte lysates against oxidatively damaged hemoglobin was significantly increased in diabetic individuals compared to controls (p<0.001).The result of this study indicates that in diabetic individuals, proteolytic enzymes degrade many oxidatively altered proteins preventing the accumulation of altered and damaged proteins in the cell.

Item Type:Journal (On-line/Unpaginated)
Keywords:Oxidative stress; Proteolytic activity; Diabetes mellitus
Subjects:JOURNALS > Online Journal of Health and Allied Sciences
ID Code:7256
Deposited By: Kakkilaya Bevinje, Dr. Srinivas
Deposited On:02 May 2011 17:17
Last Modified:02 May 2011 17:17

References in Article

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1. Bruch CG, Pierce JD. Oxidative stress in critically ill patients. American Journal of Critical Care 2002;11:543-551

2. Droge W. Free radicals in the physiological control of cell function. Physiol Rev 2002;82:48-56.

3. Fagan JM, Waxman L, Goldberg AL. Red blood cells contain a pathway for the degradation of oxidant damaged hemoglobin that does not require ATP or ubiquitin. J of Biological Chemistry 1986;261(13):5705-5713.

4. Raghothama C, Rao P. Increased proteolysis and oxidatively damaged hemoglobin in erythrocyte lysates in diabetes mellitus. Clinica Chimica Acta 1994;225:65-70.

5. Raghothama C, Rao P. Degradation of glycated hemoglobin by erythrocytic proteolytic enzymes. Clinica Chimica Acta 1996;245:201-208

6. Salo DC, Lin SW, Pacifici RE, Davies KJA. Superoxide dismutase is preferentially degraded by a proteolytic system from red blood cells following oxidative modification by hydrogen peroxide. Free Radical Biol Metab 1988;5:335-339.

7. Peterson GL. Determination of total protein. Methods in enzymol 1983;91:95-119

8. Fujino T, Ishikawa T, Inoue M, Beppu M, Kikugawa K. Characterization of membrane bound serine protease related to degradation of oxidatively damaged erythrocyte membrane proteins. Biochem Biophys Acta 1998;1374(1-2):47-55.

9. Fujino T, Watanabe T, Beppu M, Kikugawa K, Yasuda H. Identification of oxidized protein hydrolase of human erythrocytes as acylpeptide hydrolase. Biochem Biophys Acta 2000;1478(1):102-112.

10. Sacchetta P, Battista P, Santarone S, Di Cola D. Purification of human erythrocyte proteolytic enzyme responsible for degradation of oxidant damaged hemoglobin. Evidence for identifying as a member of the multicatalytic proteinase family. Biochim Biophys Acta 1990;1037(3):337-343.

11. Davies KJA, Goldberg AL. Proteins damaged by oxygen radicals are rapidly degraded by RBC extracts. J Biol Chem 1987;262:8227-8234.


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