α-Lipoic Acid Alters Post-Translational Modifications and Protects the Chaperone Activity of Lens α-Crystallin in Naphthalene-Induced Cataract

REFERENCES

• Congdon NG, Friedman DS, Lietman T. Important causes of visual impairment in the world today. JAMA. 2003;290:2057–2060.
   PubMed Web of Science ®Google Scholar
• Kupfer C.On presentation of the Friedenwald Award of the Association for Research in Vision and Ophthalmology to Dr. Joram Piatigorsky. Invest Ophthalmol Vis Sci. 1987;28:2–8.
   PubMedGoogle Scholar
• Francis PJ, Berry V, Moore AT, et al. Lens biology: Development and human cataractogenesis. Trends Genet. 1999;15:191–196.
   PubMedGoogle Scholar
• Cherian M, Abraham EC. Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. Biochem Biophys Res Commun. 1995;208:675–679.
   PubMed Web of Science ®Google Scholar
• Wang K, Gawinowicz MA, Spector A. The effect of stress on the pattern of phosphorylation of alphaA and alphaB crystallin in the rat lens. Exp Eye Res. 2000;71:385–393.
   PubMedGoogle Scholar
• Derham BK, Harding JJ. Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res. 1999;18:463–509.
   PubMed Web of Science ®Google Scholar
• Horwitz J. Alpha-crystallin. Exp Eye Res. 2003;76:145–153.
   PubMed Web of Science ®Google Scholar
• Horwitz J. Proctor Lecture. The function of alpha-crystallin. Invest Ophthalmol Vis Sci. 1993;34:10–22.
   PubMed Web of Science ®Google Scholar
• Kojima M, Sun L, Hata I, et al. Efficacy of alpha-lipoic acid against diabetic cataract in rat. Jpn J Ophthalmol. 2007;51:10–13.
   PubMedGoogle Scholar
• Maitra I, Serbinova E, Trischler H, et al. Alpha-lipoic acid prevents buthionine sulfoximine-induced cataract formation in newborn rats. Free Radic Biol Med. 1995;18:823–829.
   PubMed Web of Science ®Google Scholar
• Packer L, Witt EH, Tritschler HJ. alpha-Lipoic acid as a biological antioxidant. Free Radic Biol Med. 1995;19:227–250.
   PubMed Web of Science ®Google Scholar
• Packer L, Kraemer K, Rimbach G. Molecular aspects of lipoic acid in the prevention of diabetes complications. Nutrition. 2001;17:888–895.
   PubMed Web of Science ®Google Scholar
• Cremer DR, Rabeler R, Roberts A, et al. Safety evaluation of alpha-lipoic acid (ALA). Regul Toxicol Pharmacol. 2006;46:29–41.
   PubMed Web of Science ®Google Scholar
• Cremer DR, Rabeler R, Roberts A, et al. Long-term safety of alpha-lipoic acid (ALA) consumption: A 2-year study. Regul Toxicol Pharmacol. 2006;46:193–201.
   PubMed Web of Science ®Google Scholar
• Van Heyningen R, Pirie A. The metabolism of naphthalene and its toxic effect on the eye. Biochem J. 1967;102:842–852.
   PubMed Web of Science ®Google Scholar
• van Heyningen R. Naphthalene cataract in rats and rabbits: A resume. Exp Eye Res. 1979;28:435–439.
   PubMed Web of Science ®Google Scholar
• Xu GT, Zigler JS, Jr Lou, MF. Establishment of a naphthalene cataract model in vitro. Exp Eye Res. 1992;54:73–81.
   PubMed Web of Science ®Google Scholar
• Pandya U, Saini MK, Jin GF, et al. Dietary curcumin prevents ocular toxicity of naphthalene in rats. Toxicol Lett. 2000;115:195–204.
   PubMed Web of Science ®Google Scholar
• Sato S, Sugiyama K, Lee YS, et al. Prevention of naphthalene-1,2-dihydrodiol-induced lens protein modifications by structurally diverse aldose reductase inhibitors. Exp Eye Res. 1999;68:601–608.
   PubMed Web of Science ®Google Scholar
• Cao Guojun MW. Dynamic observation and quantificational analysis of galactose-induced cataract using slit lamp microscope image analysis system. China Medical Herald. 2006;3:146–147.
   Google Scholar
• Fujii N, Takeuchi N, Fujii N, et al. Comparison of post-translational modifications of alpha A-crystallin from normal and hereditary cataract rats. Amino Acids. 2004;26:147–152.
   PubMedGoogle Scholar
• Kelley MJ, David LL, Iwasaki N, et al. alpha-Crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract. J Biol Chem. 1993;268:18844–18849.
   PubMed Web of Science ®Google Scholar
• Jia W, Wu H, Lu H, et al. Rapid and automatic on-plate desalting protocol for MALDI-MS: Using imprinted hydrophobic polymer template. Proteomics. 2007;7:2497–2506.
   PubMedGoogle Scholar
• Zheng X, Hong L, Shi L, et al. Proteomics analysis of host cells infected with infectious bursal disease virus. Mol Cell Proteomics. 2008;7:612–625.
   PubMed Web of Science ®Google Scholar
• Keller A, Nesvizhskii AI, Kolker E, et al. Empirical statistical model to estimate the accuracy of peptide identifications made by MS/MS and database search. Anal Chem. 2002;74:5383–5392.
   PubMed Web of Science ®Google Scholar
• Nesvizhskii AI, Keller A, Kolker E, et al. A statistical model for identifying proteins by tandem mass spectrometry. Anal Chem. 2003;75:4646–4658.
   PubMed Web of Science ®Google Scholar
• Ueda Y, Duncan MK, David LL. Lens proteomics: The accumulation of crystallin modifications in the mouse lens with age. Invest Ophthalmol Vis Sci. 2002;43:205–215.
   PubMedGoogle Scholar
• Ou P, Nourooz-Zadeh J, Tritschler HJ, et al. Activation of aldose reductase in rat lens and metal-ion chelation by aldose reductase inhibitors and lipoic acid. Free Radic Res. 1996;25:337–346.
   PubMed Web of Science ®Google Scholar
• Takemoto L, Emmons T, Horwitz J. The C-terminal region of alpha-crystallin: Involvement in protection against heat-induced denaturation. Biochem J. 1993;294:435–438.
   PubMed Web of Science ®Google Scholar
• Ueda Y, Fukiage C, Shih M, et al. Mass measurements of C-terminally truncated alpha-crystallins from two-dimensional gels identify Lp82 as a major endopeptidase in rat lens. Mol Cell Proteomics. 2002;1:357–365.
   PubMed Web of Science ®Google Scholar
• Nakamura Y, Fukiage C, Shih M, et al. Contribution of calpain Lp82-induced proteolysis to experimental cataractogenesis in mice. Invest Ophthalmol Vis Sci. 2000;41:1460–1466.
   PubMed Web of Science ®Google Scholar
• Kamei A, Hamaguchi T, Matsuura N, et al. Does post-translational modification influence chaperone-like activity of alpha-crystallin? I. Study on phosphorylation. Biol Pharm Bull. 2001;24:96–99.
   PubMedGoogle Scholar
• van Boekel MA, Hoogakker SE, Harding JJ, et al. The influence of some post-translational modifications on the chaperone-like activity of alpha-crystallin. Ophthalmic Res. 1996;28(Suppl 1):32–38.
   PubMedGoogle Scholar
• Jimenez-Asensio J, Colvis CM, Kowalak JA, et al. An atypical form of alphaB-crystallin is present in high concentration in some human cataractous lenses. Identification and characterization of aberrant N- and C-terminal processing. J Biol Chem. 1999;274:32287–32294.
   PubMedGoogle Scholar
• Lapko VN, Smith DL, Smith JB. S-methylated cysteines in human lens gamma S-crystallins. Biochemistry. 2002;41:14645–14651.
   PubMedGoogle Scholar
• Wilmarth PA, Tanner S, Dasari S, et al. Age-related changes in human crystallins determined from comparative analysis of post-translational modifications in young and aged lens: Does deamidation contribute to crystallin insolubility? J Proteome Res. 2006;5:2554–2566.
   PubMed Web of Science ®Google Scholar
• Takemoto L, Horwitz J, Emmons T. Oxidation of the N-terminal methionine of lens alpha-A crystallin. Curr Eye Res. 1992;11:651–655.
   PubMed Web of Science ®Google Scholar
• Bhat SP, Nandy P, Srinivasan A, et al. Expression of recombinant alpha Ains-crystallin and not alpha A-crystallin inhibits bacterial growth. Protein Eng. 1996;9:713–718.
   PubMedGoogle Scholar
• van Rijk AA, de Jong WW, Bloemendal H. Exon shuffling mimicked in cell culture. Proc Natl Acad Sci U S A. 1999;96:8074–8079.
   PubMedGoogle Scholar
• Groenen PJ, Merck KB, de Jong WW, et al. Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. European J Biochem./FEBS 1994;225:1–19.
   PubMedGoogle Scholar