Antibodies and Fab fragments protect Cu,Zn-SOD against methylglyoxal-induced inactivation

Biochimica et Biophysica Acta - General Subjects

Volumn 1760, Issue 8, 2006, Pages 1167-1174

  Jabeen, Rukhsana ^a,b   Mohammad, Amin A ^a   Elefano, Elizabeth C ^a   Petersen, John R ^a   Saleemuddin, Mohammed ^b  

^a University of Texas Medical Branch School of Medicine   (United States)

^b ALIGARH MUSLIM UNIVERSITY   (India)

Author keywords

Glycation; Methyl glyoxal; Polyclonal antibodies; SOD

Indexed keywords

COPPER ZINC SUPEROXIDE DISMUTASE; ENZYME ANTIBODY; IMMUNOGLOBULIN F(AB) FRAGMENT; METHYLGLYOXAL;

ARTICLE; CONCENTRATION RESPONSE; CONTROLLED STUDY; CROSS LINKING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME INACTIVATION; ERYTHROCYTE; INCUBATION TIME; MOLECULAR WEIGHT; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN AGGREGATION; RABBIT; SURFACE ENHANCED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY;

ANIMALS; ANTIBODIES; CATTLE; ENZYME INHIBITORS; IMMUNOGLOBULIN FAB FRAGMENTS; MASS SPECTROMETRY; PYRUVALDEHYDE; SUPEROXIDE DISMUTASE;

BOS TAURUS; ORYCTOLAGUS CUNICULUS;

EID: 33745288178     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2006.04.002     Document Type: Article

References (65)

1. Sell D.R., Lane M.A., Johnson W.A., Masoro E.J., Mock O.B., Reiser K.M., Fogarty J.F., Cutler R.G., Ingram D.K., Roth G.S., and Monnier V.M. Longevity and the genetic determination of collagen glycoxidation kinetics in mammalian senescence. Proc. Natl. Acad. Sci. U. S. A. 93 (1996) 485-490
2. Furth A.J. Glycated proteins in diabetes. Br. J. Biomed. Sci. 54 (1997) 192-200
3. Baynes J.W., Watkins N.G., Fisher C.I., Hull C.J., Patrick J.S., Ahmed M.U., Dunn J.A., and Thorpe S.R. The Amadori product on protein: structure and reactions. Prog. Clin. Biol. Res. 304 (1989) 43-67
4. Thornalley P.J., Langborg A., and Minhas H.S. Formation of glyoxal, methylglyoxal and 3-deoxyglucosone in the glycation of proteins by glucose. Biochem. J. 344 (1999) 109-116
5. Thornalley P.J. Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification-A role in pathogenesis and antiproliferative chemotherapy. Gen. Pharmacol. 4 (1996) 565-573
6. Thornalley P.J., Westwood M., Lo T.W., and McLellan A.C. Formation of methylglyoxal modified proteins in vitro and in vivo and their involvement in AGE related processes. Contrib. Nephrol. 112 (1995) 24-31
7. Wolff S.P., and Dean R.T. Aldehydes and dicarbonyls in non-enzymic glycosylation of proteins. Biochem. J. 249 (1988) 618-619
8. Thornalley P.J. Glyoxalase I-Structure, function and a critical role in the enzymatic defence against glycation. Biochem. Soc. Trans. 31 (2003) 1343-1348
9. Phillips S.A., Mirrlees D., and Thornalley P.J. Modification of the glyoxalase system in streptozotocin-induced diabetic rats. Effect of the aldose reductase inhibitor Statil. Biochem. Pharmacol. 46 (1993) 805-811
10. McLellan A.C., Thornalley P.J., Benn J., and Sonksen P.H. Glyoxalase system in clinical diabetes mellitus and correlation with diabetic complications. Clin. Sci. (Lond.) 87 (1994) 21-29
11. Thornalley P.J. Glycation in diabetic neuropathy: characteristics, consequences, causes, and therapeutic options. Int. Rev. Neurobiol. 50 (2002) 37-57
12. Kalapos M.P. Methylglyoxal in living organisms: chemistry, biochemistry, toxicology and biological implication. Toxicol. Lett. 110 (1999) 145-175
13. Shinohara M., Giardino I., and Brownlee M. Diabetes 45 (1996) 126
14. Ahmed N., Thornalley P.J., Dawczynski J., Franke S., Strobel J., Stein G., and Haik G.M. Methylglyoxal-derived hydroimidazolone advanced glycation end-products of human lens proteins. Investig. Ophthalmol. Vis. Sci. 44 (2003) 5287-5292
15. Oya T., Hattori N., Mizuno Y., Miyata S., Maeda S., Osawa T., and Uchida K. Methylglyoxal modification of protein. Chemical and immunochemical characterization of methylglyoxal-arginine adducts. J. Biol. Chem. 274 (1999) 18492-18502
16. Riley M.L., and Harding J.J. The reaction of methylglyoxal with human and bovine lens proteins. Biochim. Biophys. Acta 1270 (1995) 36-43
17. Lo T.W., Westwood M.E., McLellan A.C., Selwood T., and Thornalley P.J. Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin. J. Biol. Chem. 269 (1994) 32299-32305
18. Booth A.A., Khalifah R.G., Todd P., and Hudson B.G. In vitro kinetic studies of formation of antigenic advanced glycation end products (AGEs). Novel inhibition of post-Amadori glycation pathways. J. Biol. Chem. 272 (1997) 5430-5437
19. Thornalley P.J. Clinical significance of glycation. Clin. Lab. 45 (1999) 263-273
20. j{cyrillic, ukrainian}-(carboxyethyl) lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem. J. 324 (1997) 565-570
21. Brinkmann E.F., Degenhardt T.P., Thorpe S.R., and Baynes J.W. Role of the Maillard reaction in aging of tissue proteins: advanced glycation end product-dependent increase in imidazolium cross-links in human lens proteins. J. Biol. Chem. 273 (1998) 18714-18719
22. Shipanova N.I., Glomb M.A., and Nagaraj R.H. Protein modification by methylglyoxal: chemical nature and synthetic mechanism of a major fluorescent adduct. Arch. Biochem. Biophys. 344 (1997) 29-36
23. Westwood M.E., and Thornalley P.J. In: Colaco C. (Ed). Glycation and advanced glycation endproducts. In: the glycation hypothesis of atherosclerosis (1997), RG Landes, Georgetown, USA 57-87
24. j{cyrillic, ukrainian}-(1-carboxyethyl)lysine-modified albumin. Biochem. J. 364 (2002) 1-14
25. Ahmed N., and Thornalley P.J. Chromatographic assay of glycation adducts in human serum albumin glycated in vitro by derivatisation with aminoquinolyl-N-hydroxysuccimidyl-carbamate and intrinsic fluorescence. Biochem. J. 364 (2002) 15-24
26. Padival A.K., Crabb J.W., and Nagaraj R.H. Methylglyoxal modifies heat shock protein 27 in glomerular mesangial cells. FEBS Lett. 551 (2003) 113-118
27. Sakamoto H., Mashima T., Yamamoto K., and Tsuruo T. Modulation of heat-shock protein 27 (Hsp27) anti-apoptotic activity by methylglyoxal modification. J. Biol. Chem. 277 (2002) 45770-45775
28. Kumar M.S., Reddy P.Y., Kumar P.A., Surolia I., and Reddy G.B. Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: physiological significance and caveats of in vitro aggregation assays. Biochem. J. 379 (2004) 273-282
29. Amicarelli F., Colafarina S., Cesare P., Aimola P., Di Ilio C., Miranda M., and Ragnelli A.M. Morphofunctional mitochondrial response to methylglyoxal toxicity in Bufo bufo embryos. Int. J. Biochem. Cell Biol. 33 (2001) 1129-1139
30. Okado A., Kawasaki Y., Hasuike Y., Takahashi M., Teshima T., Fujii J., and Taniguchi N. Induction of apoptotic cell death by methylglyoxal and 3-deoxyglucosone in macrophage-derived cell lines. Biochem. Biophys. Res. Commun. 225 (1996) 219-224
31. Akhand A.A., Hossain K., Mitsui H., Kato M., Miyata T., Inagi R., Du J., Takeda K., Kawamoto Y., Suzuki H., Kurokawa K., and Nakashima I. Glyoxal and methylglyoxal trigger distinct signals for MAP family kinases and caspase activation in human endothelial cells. Free Radical Biol. Med. 31 (2001) 20-30
32. Halliwell B., and Gutteridge J.M. Oxygen toxicity, oxygen radicals, transition metals and disease. Biochem. J. 219 (1984) 1-14
33. Choudhary D., Chandra D., and Kale R.K. Influence of methylglyoxal on antioxidant enzymes and oxidative damage. Toxicol. Lett. 93 (1997) 141-152
34. Kang J.H. Modification and inactivation of human Cu,Zn-superoxide dismutase by methylglyoxal. Mol. Cells 15 (2003) 194-199
35. Jabeen R., and Saleemuddin M. Polyclonal antibodies inhibit the glycation-induced inactivation of bovine Cu, Zn-superoxide dismutase. Biotechnol. Appl. Biochem. 43 (2006) 49-53
36. Stults N.L., Asta L.M., and Lee Y.C. Immobilization of proteins on oxidized crosslinked Sepharose preparations by reductive amination. Anal. Biochem. 180 (1989) 114-119
37. Nishikimi M., Appaji N., and Yagi K. The occurrence of superoxide anion in the reaction of reduced phenazine methosulfate and molecular oxygen. Biochem. Biophys. Res. Commun. 46 (1972) 849-854
38. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
39. Vaca C.E., Fang J.L., Conradi M., and Hou S.M. Development of a 32P-postlabelling method for the analysis of 2′-deoxyguanosine-3′-monophosphate and DNA adducts of methylglyoxal. Carcinogenesis 15 (1994) 1887-1894
40. Papoulis A., al-Abed Y., and Bucala R. Identification of N2-(1-carboxyethyl) guanine (CEG) as a guanine advanced glycosylation end product. Biochemistry 34 (1995) 648-655
41. Westwood M.E., Argirov O.K., Bordo E.A., and Thornalley P.J. Methylglyoxal modified arginine residues-A signal for receptor-mediated endocytosis and degradation of proteins by monocytic THP-1 cells. Biochim. Biophys. Acta 1356 (1997) 84-94
42. Beswick H.T., and Harding J.J. Conformational changes induced in lens α- and γ-crystallins by modification with glucose 6-phosphate. Implications for cataract. Biochem. J. 246 (1987) 761-769
43. Liang J.N., and Rossi M. In vitro non-enzymatic glycation and formation of browning products in the bovine lens α-crystallin. Exp. Eye Res. 50 (1990) 367-371
44. Stitt A.W. The role of advanced glycation in the pathogenesis of diabetic retinopathy. Exp. Mol. Pathol. 75 (2003) 95-108
45. Reiser K.M. Nonenzymatic glycation of collagen in aging and diabetes. Proc. Soc. Exp. Biol. Med. 218 (1998) 23-37
46. Harding J.J. Nonenzymatic covalent posttranslational modification of proteins in vivo. Adv. Protein Chem. 37 (1985) 247-334
47. Hirsch J., Petrakova E., Feather M.S., and Barnes C.L. The reaction of d-glucose with aminoguanidine. Carbohydr. Res. 267 (1995) 17-25
48. Khalifah R.G., Baynes J.W., and Hudson B.G. Amadorins: novel post-Amadori inhibitors of advanced glycation reactions. Biochem. Biophys. Res. Commun. 257 (1999) 251-258
49. Voziyan P.A., Metz T.O., Baynes J.W., and Hudson B.G. A post-Amadori inhibitor pyridoxamine also inhibits chemical modification of proteins by scavenging carbonyl intermediates of carbohydrate and lipid degradation. J. Biol. Chem. 277 (2002) 3397-3403
50. Heath M.M., Rixon K.C., and Harding J.J. Glycation-induced inactivation of malate dehydrogenase protection by aspirin and a lens molecular chaperone, alpha-crystallin. Biochim. Biophys. Acta 1315 (1996) 176-184
51. Yan H., and Harding J.J. The molecular chaperone, alpha-crystallin, protects against loss of antigenicity and activity of esterase caused by sugars, sugar phosphate and a steroid. Biol. Chem. 384 (2003) 1185-1194
52. Ganea E., and Harding J.J. Molecular chaperones protect against glycation-induced inactivation of glucose-6-phosphate dehydrogenase. Eur. J. Biochem. 231 (1995) 181-185
53. Hendrick J.P., and Hartl F.U. Molecular chaperone functions of heat-shock proteins. Annu. Rev. Biochem. 62 (1993) 349-384
54. Becker J., and Craig E.A. Heat shock proteins as a molecular chaperones. Eur. J. Biochem. 219 (1994) 11-23
55. McLaughlin J.A., Pethig R., and Szent-Györgyi A. Spectroscopic studies of the protein-methylglyoxal adduct. Proc. Natl. Acad. Sci. U. S. A. 77 (1980) 949-951
56. Tainer J.A., Getzoff E.D., Richardson J.S., and Richardson D.C. Structure and mechanism of copper, zinc superoxide dismutase. Nature 306 (1983) 284-287
57. Ermolenko D.N., Zherdev A.V., and Dzantiev B.B. Antibodies as specific chaperones. Biochemistry 69 (2004) 1233-1238
58. Derham B.K., Ellory J.C., Bron A.J., and Harding J.J. The molecular chaperone alpha crystallin incorporated into red cell ghosts protects membrane Na/K-ATPase against glycation and oxidative stress. Eur. J. Biochem. 270 (2003) 2605-2611
59. Ulbrich-Hofman R., Golbik R., and Damerau W. In: Vander Tweel W.J.J., Harder A., and Buitelar R.M. (Eds). Stability sand stabilization of enzymes (1993), Elsevier, Amsterdam 497-504
60. Younus H., Owais M., Rao D.N., and Saleemuddin M. Stabilization of pancreatic ribonuclease A by immobilization on Sepharose-linked antibodies that recognize the labile region of the enzyme. Biochim. Biophys. Acta 36454 (2001) 1-7
61. Younus H., Koeditz J., Saleemuddin M., and Ulbrich-Hofman R. Selective stabilization of a labile mutant from bovine pancreatic ribonuclease A by antibodies. Biotechnol. Lett. 24 (2002) 1821-1826
62. Gupta P., Khan R.H., and Saleemuddin M. Binding of antibromelain monomeric Fab' improves the stability of stem bromelain against inactivation. Biochim. Biophys. Acta 1646 (2003) 131-135
63. Holliger P., and Hudson P.J. Engineered antibody fragments and the rise of single domains. Nat. Biotechnol. 23 (2005) 1126-1136
64. Clements Jr. R.S., Robison Jr. W.G., and Cohen M.P. Anti-glycated albumin therapy ameliorates early retinal microvascular pathology in db/db mice. J. Diabetes its Complicat. 12 (1998) 28-33
65. Cohen M.P., and Ziyadeh F.N. Role of Amadori modified non-enzymatically glycated serum proteins in the pathogenesis of diabetic retinopathy. J. Am. Soc. Nephrol. 7 (1996) 183-190