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Molecules 2016, 21(2), 143; doi:10.3390/molecules21020143

Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract

1
Department of Clinical Biochemistry, Faculty of Medical Sciences, Tarbiat Modares University (TMU), Tehran P. O. Box 14115-111, Iran
2
Department of Clinical Sciences, Faculty of Veterinary Medicine, University of Tehran, Tehran P. O. Box 14185-746, Iran
3
Department of Biology, Faculty of Science, University of Sistan and Baluchestan, Zahedan P. O. Box 98167, Iran
Present Address: Research Center for Biochemistry and Nutrition in Metabolic Diseases, Kashan University of Medical Sciences, Kashan P. O. Box 87159, Iran
*
Author to whom correspondence should be addressed.
Academic Editors: Maria Z. Tsimidou and Petros A. Tarantilis
Received: 15 November 2015 / Revised: 14 January 2016 / Accepted: 20 January 2016 / Published: 26 January 2016
View Full-Text   |   Download PDF [1125 KB, uploaded 26 January 2016]   |  

Abstract

The current study investigates the inhibitory effect of crocin(s), also known as saffron apocarotenoids, on protein glycation and aggregation in diabetic rats, and α-crystallin glycation. Thus, crocin(s) were administered by intraperitoneal injection to normal and streptozotocin-induced diabetic rats. The cataract progression was recorded regularly every two weeks and was classified into four stages. After eight weeks, the animals were sacrificed and the parameters involved in the cataract formation were measured in the animal lenses. Some parameters were also determined in the serum and blood of the rats. In addition, the effect of crocin(s) on the structure and chaperone activity of α-crystallin in the presence of glucose was studied by different methods. Crocin(s) lowered serum glucose levels of diabetic rats and effectively maintained plasma total antioxidants, glutathione levels and catalase activity in the lens of the animals. In the in vitro study, crocin(s) inhibited α-crystallin glycation and aggregation. Advanced glycation end products fluorescence, hydrophobicity and protein cross-links were also decreased in the presence of crocin(s). In addition, the decreased chaperone activity of α-crystallin in the presence of glucose changed and became close to the native value by the addition of crocin(s) in the medium. Crocin(s) thus showed a powerful inhibitory effect on α-crystallin glycation and preserved the structure-function of this protein. Crocin(s) also showed the beneficial effects on prevention of diabetic cataract. View Full-Text
Keywords: crocin(s); structure-function; streptozotocin; cataract; glycation; oxidative stress crocin(s); structure-function; streptozotocin; cataract; glycation; oxidative stress
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Bahmani, F.; Bathaie, S.Z.; Aldavood, S.J.; Ghahghaei, A. Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract. Molecules 2016, 21, 143.

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