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The principle role of α-crystallin is chaperoning activity that protect other proteins against different stresses. High glucose concentration induces the osmotic stress and results in biomacromolecules glycation, which is subsequently cause their conformational and functional changes. Here, the roles of l-lysine (Lys) on the prevention of α-crystallin glycation in both in vitro and in vivo conditions are investigated. The catalase (CAT) activity was considered as a marker of α-crystallin functionality in both conditions. Streptozotocin-induced diabetic rats were treated with 0.1% of the Lys in drinking water. The purified α-crystallin was also incubated with glucose, in the presence or absence of the Lys and its structure-function was compared. The results showed that the visual cataract score was significantly lower in the diabetic rats treated with Lys. After Lys treatment, CAT, superoxide dismutase, aldose reductase and other biochemical parameters in the lens and serum of the diabetic rats returned to the normal value. Formation of the advanced glycation endproducts (AGEs), protein cross-linking, and the hydrophobicity of α-crystallin were changed due to glycation, but they were reversed by Lys treatment. The glycated α-crystallin lost its chaperone activity against heat denatured-CAT, but in the presence of Lys, it preserved its activity and prevented CAT aggregation. In conclusion, Lys treatment significantly inhibited the progression of diabetic cataract in rats. These effects were due to the Lys antiglycating and antioxidant effects, in addition to its protective effect against α-crystallin chaperoning activity.
This article was published in the following journal.
Name: International journal of biological macromolecules
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The prototypical analgesic used in the treatment of mild to moderate pain. It has anti-inflammatory and antipyretic properties and acts as an inhibitor of cyclooxygenase which results in the inhibition of the biosynthesis of prostaglandins. Aspirin also inhibits platelet aggregation and is used in the prevention of arterial and venous thrombosis. (From Martindale, The Extra Pharmacopoeia, 30th ed, p5)
A protein deglycase that repairs methylglyoxal- and glyoxal-glycated amino acids and proteins, releasing repaired proteins and lactate or glycolate. It deglycates CYSTEINE, ARGININE and LYSINE residues to reactivate proteins by reversing glycation and prevent the formation of ADVANCED GLYCATION END PRODUCTS. It protects cells against OXIDATIVE STRESS and CELL DEATH by functioning as an oxidative stress sensor and redox-sensitive MOLECULAR CHAPERONE and PROTEASE. Mutations in the PARK7 gene are associated with autosomal-recessive, early-onset PARKINSON DISEASE.
A heterogeneous group of compounds derived from rearrangements, oxidation, and cross-linking reactions that follow from non-enzymatic glycation of amino groups in proteins. They are also know as Maillard products. Their accumulation in vivo accelerates under hyperglycemic, oxidative, or inflammatory conditions. Heat also accelerates the formation of advanced glycation end products (AGEs) such seen with the browning of food during cooking under or over high heat.
One of the alpha crystallin subunits. In addition to being expressed in the lens (LENS, CRYSTALLINE), alpha-crystallin B chain has been found in a variety of tissues such as HEART; BRAIN; MUSCLE; and KIDNEY. Accumulation of the protein in the brain is associated with NEURODEGENERATIVE DISEASES such as CREUTZFELDT-JAKOB SYNDROME and ALEXANDER DISEASE.
One of the subunits of alpha-crystallins. Unlike ALPHA-CRYSTALLIN B CHAIN the expression of ALPHA-CRYSTALLIN A CHAIN is limited primarily to the lens (LENS, CRYSTALLINE).
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