Enhanced recognition of reactive oxygen species damaged human serum albumin by circulating systemic lupus erythematosus autoantibodies

References

• Scofield RH, Kurien BT, Granick S, McClain MJ, Pye Q, James JA, Schneider RI, Broyles RH, Bachmann M, Hensley K. Modification of lupus-associated 60-kDa Ro protein with the lipid oxidation product 4-hydroxy-2-nonenal increases antigenicity and facilitates epitopes spreading. Free Radic Biol Med 2005; 38: 719–728
   PubMed Web of Science ®Google Scholar
• Greidinger EL, Hoffman RW. The appearance of U1 RNP antibody specificities in sequential autoimmune human antisera follows a characteristic order that implicates the U1-70 kd and B′/B proteins as predominant U1 RNP immunogens. Arthritis Rheum 2001; 44: 368–375
   PubMed Web of Science ®Google Scholar
• Lehmann PV, Sercarz EE, Forsthuker T, Doyan CM, Gammon G. Determinant spreading and the dynamics of the autoimmune T-cell repertoire. Immunol Today 1993; 14: 203–208
   PubMedGoogle Scholar
• James JA, Harley JB. B-cell epitope spreading in autoimmunity. Immunol Rev 1998; 164: 85–200
   Google Scholar
• Arbuckle MR, McClain MT, Rubertone MV, Scofied RH, Dennis GJ, James JA, Harley JB. Development of autoantibodies before the clinical onset of systemin lupus erythematosus. N Engl J Med 2003; 349: 1526–1533
   PubMed Web of Science ®Google Scholar
• Perl A. Pathogenesis and spectrum of autoimmunity. Autoimmunity, methods and protocols, A Perl. Humana Press, Totowa, NJ 2004; 1–8
   Google Scholar
• Ahsan H, Ali A, Ali R. Oxygen free radicals and systemic autoimmunity. Clin Exp Immunol 2003; 131: 398–404
   PubMed Web of Science ®Google Scholar
• Shacter E. Quantification and significance of protein oxidation in biological samples. Drug Met Rev 2000; 32: 307–326
   PubMed Web of Science ®Google Scholar
• Poon HF, Vaishnav RA, Gelchell TV, Getchell ML, Butterfield DA. Quantitative proteomics analysis of differential protein expression and oxidative modification of specific proteins in the brains of old mice. Neurobiol Aging 2006; 27: 1010–1019
   PubMedGoogle Scholar
• Tabner BJ, Turnbull S, El-Agnaf O, Allsop D. Production of reaction oxygen species from aggregating proteins implicated in Alzheimer's disease. Parkinson's disease and other neurodegenerative disease. Curr Top Med Chem 2001; 1: 507–517
   PubMedGoogle Scholar
• Arutyunova EI, Danshina PV, Domnina LV, Pleten AP, Muronetz VI. Oxidation of glyceraldehydes-3-phosphate dehydrogenase enhances its binding to nucleic acids. Biochem Biophys Res Commun 2003; 307: 547–552
   PubMed Web of Science ®Google Scholar
• Shacter E, Williams JA, Levine RL. Oxidative modification of fibrinogen inhibits thrombin-catalyzed clot formation. Free Radic Biol Med 1995; 18: 815–821
   PubMed Web of Science ®Google Scholar
• Chou C. Binding of rheumatoid and lupus synovial fluids and sera-derived human IgG rheumatoid factor to degalactosylated IgG. Arch Med Res 2002; 33: 541–544
   PubMedGoogle Scholar
• Dixit K, Ali R. Role of nitric oxide modified DNA in the etiopathogenesis of systemic lupus erythematosus. Lupus 2004; 13: 95–100
   PubMedGoogle Scholar
• Mansoor F, Ali A, Ali R. Binding of circulating SLE autoantibodies to oxygen free radical damaged chromatin. Autoimmunity 2005; 38: 431–438
   PubMed Web of Science ®Google Scholar
• Habib S, Moinuddin, Ali R. Acquired antigenicity of DNA after modification with peroxynitrite. Int J Biol Macromol 2005; 35: 221–225
   PubMedGoogle Scholar
• Dixit K, Moinuddin, Ali A. Immunological studies on peroxynitrite modifies human DNA. Life Sci 2005; 77: 2626–2642
   PubMed Web of Science ®Google Scholar
• Dixit K, Ali R. Antigen binding characteristics of antibodies induced against nitric oxide modified plasmid DNA. Biochim Biophys Acta 2001; 1528: 1–8
   PubMed Web of Science ®Google Scholar
• Carballal S, Radi R, Kirk MC, Barnes S, Freeman BA, Alvarez B. Sulfenic acid formation in human serum albumin by hydrogen peroxide and peroxynitrite. Biochemistry 2003; 42: 9906–9914
   PubMed Web of Science ®Google Scholar
• Rigamonti C, Mottaran E, Reale E, Rolla R, Cipriani V, Capelli F, Boldarini R, Vidali M, Sartori M, Albano E. Moderate alcohol consumption increases oxidative stress in patients with chronic hepatitis C. Hepatology 2003; 38: 42–49
   PubMedGoogle Scholar
• Rasheed Z, Ali R. Reactive oxygen species damaged human serum albumin in patients with type 1 diabetes mellitus: Biochemical and immunological studies. Life Sci 2006; 79: 2320–2328
   PubMed Web of Science ®Google Scholar
• Rasheed Z, Khan MWA, Ali R. Hydroxyl radical modification of human serum albumin generated cross reactive antibodies. Autoimmunity 2006; 39: 479–488
   PubMed Web of Science ®Google Scholar
• Lowry OH, Rosebrough NJ, Farr AL, Randall RJ. Protein measurement with the folin phenol reagent. J Biol Chem 1951; 193: 265–275
   PubMed Web of Science ®Google Scholar
• Bradford MM. A rapid and sensitive method for the quantitation microgram quantity of protein utilizing the principle of protein dye binding. Anal Biochem 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Wallevik K. Reversible denaturation of human serum albumin by pH, temperature and guanidine hydrochloride. J Biol Chem 1973; 245: 2650–2655
   Google Scholar
• Arnett FC, Edworthy SM, Bloch DA, et al. The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis. Arthritis Rheum 1998; 31: 315–324
   Web of Science ®Google Scholar
• Levine RL, Williams J, Stadtman ER, Shacter E. Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol 1994; 233: 346–357
   PubMed Web of Science ®Google Scholar
• Ali R, Alam K. Evaluation of antibodies against free radical modified DNA by ELISA. Methods in molecular biology: Oxidative stress biomarkers and antioxidants protocols1st ed., D Armstrong. Humana Press, New Jersey 2002; vol. 186: 171–181
   Google Scholar
• Langmuir I. The adsorption of gases on plane surface of glass, mica and platinum. J Am Chem Soc 1918; 40: 1361–1403
   Web of Science ®Google Scholar
• Tayyab S, Qasim MA. Purification and properties of buffalo serum albumin. Biochem Int 1990; 20: 405–415
   PubMedGoogle Scholar
• Chen RF. Removal of fatty acids from serum albumin by charcoal treatment. J Biol Chem 1967; 242: 173–181
   PubMed Web of Science ®Google Scholar
• Stryer L. The interaction of a naphthalene dye with apomyoglobin and apohemoglobin. A fluorescence probe of non-polar binding sites. J Mol Biol 1965; 13: 482–495
   PubMedGoogle Scholar
• Ravirajan CT, Rowse L, MacGowan JR, Isenberg DA. An analysis of clinical disease activity and nephritis-associated serum autoantibody profiles in patients with systemic lupus erythematosus: A cross-section study. Rheumatology 2001; 40: 1405–1412
   PubMedGoogle Scholar
• Domeiko JP, Nompleggi DL. Role of albumin in human physiology and pathophysiology. J Parenter Enteral Nutr 1991; 15: 207–211
   PubMedGoogle Scholar
• Witko-Sarsat V, Friedlander M, Khoa TN, Capeillere-Blandin C, Nguyen AT, Canteloup S, Dayer JM, Jungers P, Drueke T, Descamps-Latscha B. Advanced oxidation protein products as novel mediators of inflammation and monocytes activation in chronic renal failure. J Immunol 1998; 161: 2524–2532
   PubMed Web of Science ®Google Scholar
• Himmelfarb J, Mcmonagle E. Albumin is the major plasma protein target of oxidant stress in uremia. Kidney Int 2001; 60: 358–363
   PubMed Web of Science ®Google Scholar
• Dalle-Dome I, Rossi R, Giustarini D, Milzani A, Colombo R. Protein carbonyl groups as biomarkers of oxidative stress. Clin Chim Acta 2003; 29: 23–38
   Google Scholar
• Halliwell B, Gutteridge JM. The antioxidants of human extracellular fluids. Arch Biochem Biophys 1990; 280: 1–8
   PubMed Web of Science ®Google Scholar