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Effect of curcumin and quercetin on lysosomal enzyme activities in streptozotocin-induced diabetic rats.
- Source :
- Clinical Nutrition; Oct2012, Vol. 31 Issue 5, p749-755, 7p
- Publication Year :
- 2012
-
Abstract
- Summary: Background & aims: Diabetes causes impairment of various enzyme activities in the physiological system, including lysosomal enzymes. The effect of feeding curcumin, quercetin and aminoguanidine on lysosomal enzyme activities viz., N-acetyl-β-d-glucosaminidase, β-d-glucuronidase, β-d-galactosidase and acid phosphatase were studied in different tissues of streptozotocin-induced diabetic rats. Method: Rats were divided into four control groups and four diabetic groups. Experimental groups were fed with diet supplemented with curcumin (0.5%) or quercetin (0.1%) or aminoguanidine (0.05%). Lysosomal enzyme activities were determined in various tissues. Results: The specific activity of N-acetyl-β-d-glucosaminidase in liver of diabetic rats was decreased when compared to control rats and was ameliorated with curcumin and quercetin treatment by 67% and 78%, respectively. On the other hand, β-d-glucuronidase activity was higher in the brain of diabetic rats (0.90 ± 0.04 nmol/mg protein/min), when compared to control rats (0.45 ± 0.02 nmol/mg protein/min) and was decreased in curcumin (0.75 ± 0.05 nmol/mg protein/min) and quercetin (0.74 ± 0.11 nmol/mg protein/min) treated rats. β-d-galactosidase activity in spleen of curcumin and quercetin fed diabetic group rats was ameliorated by 68% and 58%, respectively, in comparison to diabetic rats. Acid phosphatase activity in diabetic rats decreased in testis when compared to control. Conclusion: Curcumin and quercetin feeding modulated lysosomal enzyme activities in different tissues during diabetes and the effect was comparable to well-known anti-glycative agent - aminoguanidine. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 02615614
- Volume :
- 31
- Issue :
- 5
- Database :
- Supplemental Index
- Journal :
- Clinical Nutrition
- Publication Type :
- Academic Journal
- Accession number :
- 104420864
- Full Text :
- https://doi.org/10.1016/j.clnu.2012.02.003