Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract
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 rat...
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2016-01-01
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author | Fereshteh Bahmani Seyedeh Zahra Bathaie Seyed Javid Aldavood Arezou Ghahghaei |
author_facet | Fereshteh Bahmani Seyedeh Zahra Bathaie Seyed Javid Aldavood Arezou Ghahghaei |
author_sort | Fereshteh Bahmani |
collection | DOAJ |
description | 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. |
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spelling | doaj.art-c199f14d3c8547fbbc3d795998ccc2c22022-12-22T02:08:01ZengMDPI AGMolecules1420-30492016-01-0121214310.3390/molecules21020143molecules21020143Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic CataractFereshteh Bahmani0Seyedeh Zahra Bathaie1Seyed Javid Aldavood2Arezou Ghahghaei3Department of Clinical Biochemistry, Faculty of Medical Sciences, Tarbiat Modares University (TMU), Tehran P. O. Box 14115-111, IranDepartment of Clinical Biochemistry, Faculty of Medical Sciences, Tarbiat Modares University (TMU), Tehran P. O. Box 14115-111, IranDepartment of Clinical Sciences, Faculty of Veterinary Medicine, University of Tehran, Tehran P. O. Box 14185-746, IranDepartment of Biology, Faculty of Science, University of Sistan and Baluchestan, Zahedan P. O. Box 98167, IranThe 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.http://www.mdpi.com/1420-3049/21/2/143crocin(s)structure-functionstreptozotocincataractglycationoxidative stress |
spellingShingle | Fereshteh Bahmani Seyedeh Zahra Bathaie Seyed Javid Aldavood Arezou Ghahghaei Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract Molecules crocin(s) structure-function streptozotocin cataract glycation oxidative stress |
title | Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract |
title_full | Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract |
title_fullStr | Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract |
title_full_unstemmed | Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract |
title_short | Inhibitory Effect of Crocin(s) on Lens α-Crystallin Glycation and Aggregation, Results in the Decrease of the Risk of Diabetic Cataract |
title_sort | inhibitory effect of crocin s on lens α crystallin glycation and aggregation results in the decrease of the risk of diabetic cataract |
topic | crocin(s) structure-function streptozotocin cataract glycation oxidative stress |
url | http://www.mdpi.com/1420-3049/21/2/143 |
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