Conformational study of N?-(carboxymethyl)lysine adducts of recombinant a-crystallins

References

• Monnier VM, Cerami A. Nonenzymatic browning iin vivo:i possible process for aging of long-lived proteins. iSci-encei 1981;211:491–493.
   PubMed Web of Science ®Google Scholar
• Liang JN, Rossi MT. iIn vitroi non-enzymatic glycation and formation of browning products in the bovine lens a-crystallin. iExp Eye Res.i 1990;50:367–371.
   PubMedGoogle Scholar
• Nagaraj RH, Monnier VM. Isolation and characteriza-tion of a blue fluorophore from human eye lens crys-tallins: iin vitroi formation from Maillard reaction with ascorbate and ribose. iBiochim Biophys Actai 1992;1116: 34–42.
   PubMedGoogle Scholar
• Prabhakaram M, Ortwerth BJ. The glycation and cross-linking of isolated lens crystallins by ascorbic acid. iExp Eye Res.i 1992;55:451–459.
   PubMed Web of Science ®Google Scholar
• Cohen MP. Diabetes and protein glycation. Philadelphia, PA: JC Press. 1996:5–31.
   Google Scholar
• Lyons TJ, Silvestri G, Dunn JA, Dyer DG, Baynes JW. Role of glycation in modification of lens crystallins in diabetic and non-diabetic senile cataracts. iDiabetesi 1991;40:1010–1015.
   Google Scholar
• Nagaraj RH, Sell DR, Prabhakaram M, Ortwerth BJ, Monnier VM. High correlation between pentosidine pro-tein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis. iProc Natl Acad Sci USA.i 1991;88: 10257–10261.
   Google Scholar
• Reddy S, Bichler J, Wells-Knecht KJ, Thorpe SR, Baynes JW. NE-(carboxymethyl) lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. iBiochemistryi 1995;34:10872–10878.
   Google Scholar
• Ikeda K, Higash T, Sano H, Jinnouchi Y, Yoshida M, Araki T, Ueda S, Horiuchi S. NE-(carboxymethyplysine protein adduct is a major immunological epitope in pro-teins modified with advanced glycation end products of the Maillard reaction. iBiochemistryi 1996;35:8075–8083.
   PubMed Web of Science ®Google Scholar
• Stevens VJ, Rouzer CA, Monnier VM, Cerami A. Dia-betic cataract formation: potential role of glycosylation of lens crystallins. iProc Natl Acad Sci USAi 1978;75: 2918–2922.
   PubMed Web of Science ®Google Scholar
• Brownlee M, Cerami A, Vlassara H. Advanced glyco-sylation end products in tissue and the biochemical ba-sis of diabetic complications. iN Engl J Med.i 1988;318: 1315–1321.
   Google Scholar
• Bucala R, Cerami A. Advanced glycosylation: chemis-try, biology, and implications for diabetes and aging. iAdv Pharmacol.i 1992;23:1–34.
   Google Scholar
• Beswick HT, Harding JJ. Conformational changes in-duced in lens alpha- and gamma-crystallins by modifi-cation with glucose 6-phosphate. Implications for cata-ract. iBiochem J.i 1987;246:761–769.
   Google Scholar
• Santini SA, Mordente A, Meucci E, Miggiano GA, Martorana GE. Conformational stability of bovine a-crystallin. Evidence for a destabilizing effect of ascor-bate. iBiochem J.i 1992;287:107–112.
   Google Scholar
• Luthra M, Balasubramanian D. Nonenzymatic glyca-tion alters protein structure and stability. A study of two eye lens crystallins. iJ Biol Chem.i 1993;268:18119–18127.
   PubMed Web of Science ®Google Scholar
• Sun TX, Das BK, Liang JJN. Conformational and func-tional differences between recombinant human lens aA- and aB-crystallin. iJ Biol Chem.i 1997;272:6220–6225.
   Google Scholar
• Sun TX, Liang JJN. Intermolecular exchange and sta-bilization of human lens recombinant aA- and aB-crys-tallins. iJ Biol Chem.i 1998;273:286–290.
   Google Scholar
• Sun TX, Akhtar NJ, Liang UN. Subunit exchange of lens a-crystallin: A fluorescence energy transfer study with the fluorescent labeled aA-crystallin mutant W9F as a probe. iFEBS Lett.i 1998;430: 401–404.
   Google Scholar
• Habeeb AFSA. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. iAnal Biochem.i 1966;14:328–336.
   Google Scholar
• Mach H, Middaugh CR, Lewis RV. Statistical determi-nation of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. iAnal Bio-chem.i 1992;200:74–80.
   Google Scholar
• Laemmli UK. Cleavage of structural protein during as-sembly of the head of bacteriophage T4. iNaturei 1970; 227:680–685.
   PubMed Web of Science ®Google Scholar
• Liang JN, Li XY. Interaction and aggregation of lens crystallins. iExp Eye Res.i 1991;53:61–66.
   Google Scholar
• Sharma KK, Kaur H, Kumar GS, Kester K. Interaction of 1,11-bis(4-anilino)naphthalene-5,5'-disulfonic acid with a-crystallin. iJ Biol Chem.i 1998;273:8965–8970.
   Google Scholar
• Sun TX, Akhtar NJ, Liang UN. Conformational change of human lens insoluble a-crystallin. iJ Protein Chem.i 1998;17:685–690.
   Google Scholar
• Farahbakhsh ZT, Huang QL, Ding LL, Altenbach C, Steinhoff HJ, Horwitz J, Hubbell WL. Interaction of a-crystallin with spin-labeled peptides. iBiochemistryi 1995;34:509–516.
   Google Scholar
• Lakowicz JR. iPrinciples of fluorescence spectroscopy.iNew York, NY. Plenum Press. 1983:342–381.
   Google Scholar
• Musci G, Berliner U. Probing different conformation-al states of bovine a-lactalbumin: fluorescence studies with 4,4'-bis[1-(phenylamino)-8-naphthalenesulfonate]. iBiochemistryi 1985;24:3852–3856.
   PubMedGoogle Scholar
• Das KP, Surewicz WK. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of a-crystallin. iFEBS Lett.i 1995;369:321–325.
   PubMed Web of Science ®Google Scholar
• Das BK, Liang JJN, Chakrabarti B. Heat-induced con-formational change and increased chaperone activity of lens a-crystallin. iCurr Eye Res.i 1997;16:303–309.
   Google Scholar
• Cantor CR, Timasheff SN. Optical spectroscopy of pro-teins. In iThe Proteins,i Vol V. New York, NY: Academic Press. 1982:145–306.
   Google Scholar
• Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klent DC. Measurement of protein using bicinchon-inic acid. iAnal Biochem.i 1986;150:76–80.
   Google Scholar
• Horwitz J, Huang QL, Ding L, Bova MP. Lens a-crys-tallin: chaperone-like properties. iMethods Enzymol.i 1998;290:365–383.
   PubMed Web of Science ®Google Scholar
• Horwitz J, Bova M, Huang QL, Ding L, Yaron 0, Low-man S. Mutation of aB-crystallin: effects on chaperone-like activity. iInt J Biol Macromol.i 1998;22: 263–269.
   Google Scholar
• Ikeda K, Nagai R, Sakamoto T, Sano H, Araki T, Saka-ta N, Nakayama H, Yoshida M, Ueda S, Horiuchi S. Immunochemical approaches to AGE-structures: char-acterization of anti-AGE antibodies. iJ Immunol Meth-odsi 1998;215:95–104.
   Google Scholar
• Liang JN, Pelletier MR. Destabilization of lens protein conformation by glutathione mixed disulfide. iExp Eye Res.i 1988;47:17–25.
   PubMedGoogle Scholar
• Kono M, Sen AC, Chakrabarti B. Thermodynamics of thermal and athermal denaturation of y-crystallins: chang-es in conformational stability upon glutathione reaction. iBiochemistryi 1990;29:464–470.
   Google Scholar
• Raman B, Rao CM. Chaperone-like activity and tem-perature-induced structural changes of a-crystallin. iJ Biol Chem.i 1997;272:23559–23564.
   Google Scholar
• Das BK, Liang JJN. Detection and characterization of a-crystallin intermediate with maximal chaperone-likeactivity. iBiochem Biophys Res Commun.i 1997;236:370–374.
   Google Scholar
• Phipps BM, Typke D, Hegerl R, Volker S, Hoffmann A, Stetter KO, Baumeister W. Structure of a molecular chaperone from a thermophilic archaebacterium. iNaturei 1993;361:475–477.
   Google Scholar
• Smulders RH, van Boekel MA, de Jong WW. Mutations and modifications support a `pitted-flexiball' model for a-crystallin. iInt J Riol Macromol.i 1998;22:187–196.
   Google Scholar
• Cherian M, Abraham EC. Decreased molecular chaper-one property of a-crystallins due to posttranslational modifications. iBiochem Biophys Res Commun.i 1995;208: 675–967.
   PubMed Web of Science ®Google Scholar
• van Boekel MA, Hoogakker SE, Harding JJ, de Jong WW. The influence of some post-translational modifi-cations on the chaperone-like activity of a-crystallin. iOphthalmic Res.i 1996;28 (Suppl 1):32–38.
   Google Scholar
• Sharma KK, Kumar GS, Murphy AS, Kester K. Identi-fication of 1,1'-bi (4-anilino)naphthalene-5, 5 '-di sulfonic acid binding sequences in alpha-crystallin. iJ Riol Chem.i 1998;273:15474–15478.
   PubMed Web of Science ®Google Scholar
• Das BK, Sun TX, Akhtar NJ, Chylack Jr LT, Liang JJN. Fluorescence and Immunochemical Studies of Advanced Glycation Related Lens Pigments. iInvest Ophthalmol Vis Sci.i 1998;39:2058–2066.
   Google Scholar
• Ahmed MU, Brinkmann Frye E, Degenhardt TP, Thor-pe SR, Baynes JW. NE-(carboxyethyplysine, a product of the chemical modification of proteins by methylgly-oxal, increases with age in human lens proteins. iBio-chem J.i 1997;324:565–570.
   Google Scholar