Comparison of post-translational modifications of alpha A-crystallin from normal and hereditary cataract rats.

Abstract

In order to investigate the relationship between lens opacities and the various modifications of lens proteins, we analyzed and compared the properties of lens proteins of 85-day old normal Wistar rats and the hereditary cataract model, ICR/f rats. The present study identified many differences between normal and mutant lens proteins. In the ICR/f mutant rats, the relative amounts of gamma-crystallin decreased and high molecular weight (HMW) protein increased. Racemization and isomerization of Asp-151 of alpha A-crystallin was observed in the mutant ICR/f rats, and Met-1 of alpha A-crystallin was oxidized to methionine sulfoxide. These modifications were not found in the age-matched normal rats. These tendencies are consistent with aged and cataractous human lenses.

• Authors: N Fujii, N Takeuchi, N Fujii, T Tezuka, K Kuge, T Takata, A Kamei, T Saito
• Journal: Amino acids (Amino Acids) Vol. 26 Issue 2 Pg. 147-52 (Mar 2004) ISSN: 0939-4451 [Print] Austria
• PMID: 15042443 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Peptides
• alpha-Crystallin A Chain
• Aspartic Acid
• Methionine

Topics

• Aging (physiology)
• Animals
• Aspartic Acid (analogs & derivatives, chemistry, metabolism)
• Cataract (genetics, metabolism)
• Disease Models, Animal
• Humans
• Isomerism
• Lens, Crystalline (chemistry, metabolism)
• Methionine (metabolism)
• Molecular Structure
• Oxidation-Reduction
• Peptides (chemistry)
• Protein Processing, Post-Translational
• Rats
• Rats, Mutant Strains
• Rats, Wistar
• Time Factors
• alpha-Crystallin A Chain (chemistry, metabolism, physiology)