The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid
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H. Yan
Abstract
Previously we showed that glycation-induced inactivation and loss of antigenicity of enzymes occur simultaneously. α-Crystallin, a major structural protein of the mammalian lens, prevents the aggregation of other proteins and protects enzyme function against post-translational modification in vitro. However, it is not known whether αcrystallin can also protect against loss of antigenicity of enzymes. Esterase activity in the lens is decreased in senile cataract and diabetes. We investigated the loss of antigenicity of esterase caused by different insults and the ability of α-crystallin to protect. Inactivation of carboxylesterase by sugars, fructose 6-phosphate (F6P) and a steroid, prednisolone-21-hemisuccinate (P-21-H), was measured spectrophotometrically in the presence and absence of α-crystallin, while loss of antigenicity was monitored simultaneously using an immunoprecipitation method. The esterase was progressively inactivated by fructose, F6P, ribose, and P 21-H. Bovine α-crystallin fully protected against inactivation of esterase by all four compounds, and also protected against loss of antigenicity of the esterase by fructose, ribose and P-21-H at a molar ratio of 1:1. The results indicated that α-crystallin, under our experimental conditions, clearly exhibited the ability to prevent loss of antigenicity and inactivation of esterase. The protective effect of αcrystallin against loss of antigenicity indicates a novel aspect of its chaperoning function.
Copyright © 2003 by Walter de Gruyter GmbH & Co. KG
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- Molecular and Functional Interdependence of the Urokinase-Type Plasminogen Activator System with Integrins
- Differential Haemoglobin Gene Expression in the Crustacean Daphnia magna Exposed to Different Oxygen Partial Pressures
- Cloning and Characterization of the Promoter Region of the Mouse Frizzled-Related Protein 4 Gene
- The Bloom's Syndrome Helicase Interacts Directly with the Human DNA Mismatch Repair Protein hMSH6
- Assignment of Disulphide Bridges in Par j 2.0101, a Major Allergen of Parietaria judaica Pollen
- Determination of the NMR Structure of Gln25-Ribonuclease T1
- The Molecular Chaperone, α-Crystallin, Protects against Loss of Antigenicity and Activity of Esterase Caused by Sugars, Sugar Phosphate and a Steroid
- The Activator-Binding Site of Onchocerca volvulus S-Adenosylmethionine Decarboxylase, a Potential Drug Target
- Trans-Sialidase-Like Sequences from Trypanosoma congolense Conserve Most of the Critical Active Site Residues Found in Other Trans-Sialidases
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