Reactive oxygen species cause direct damage of Engelbreth-Holm-Swarm matrix

American Journal of Pathology

Volumn 151, Issue 1, 1997, Pages 215-231

  Riedle, Barbara ^a   Kerjaschki, Dontscho ^a  

^a UNIVERSITY OF VIENNA   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

REACTIVE OXYGEN METABOLITE; XANTHINE OXIDASE;

ANIMAL CELL; ARTICLE; BASEMENT MEMBRANE; CELL DAMAGE; CELL MIGRATION; COVALENT BOND; CROSS LINKING; DOSE RESPONSE; EXTRACELLULAR MATRIX; EXTRACELLULAR SPACE; GLOMERULUS BASEMENT MEMBRANE; NONHUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEINURIA; RAT;

ANIMALS; BIOPOLYMERS; COLLAGEN; CROSS-LINKING REAGENTS; DIMERIZATION; DOSE-RESPONSE RELATIONSHIP, DRUG; EXTRACELLULAR MATRIX; EXTRACELLULAR MATRIX PROTEINS; HYDROGEN PEROXIDE; HYDROXYL RADICAL; IRON; LAMININ; MEMBRANE GLYCOPROTEINS; METALLOENDOPEPTIDASES; MICE; MICE, INBRED C57BL; NEOPLASMS, EXPERIMENTAL; OXIDATION-REDUCTION; REACTIVE OXYGEN SPECIES; TYROSINE; XANTHINE OXIDASE;

EID: 0030844478     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (55)

1. Yurchenco PD, Schittny JC: Molecular architecture of basement membranes. FASEB J 1990, 4:1577-1590
2. Schnaper HW, Kleinman HK, Grant DS: Role of laminin in endothelial cell recognition and differentiation. Kidney Int 1993, 43:20-25
3. Aumailley M: Structure and supramolecular organization of basement membranes. Kidney Int Suppl 1995, 49:S4-S7
4. Farquhar MG: The glomerular basement membrane: a selective macromolecular filter. Cell Biology of Extracellular Matrix, ed 2. Edited by ED Hay. New York, Plenum Press, 1991, pp 365-418
5. Abrahamson DR, Vanden Heuvel GB, Clapp WL: Nephritogenic antigens in the glomerular basement membrane. Immunologie Renal Diseases. Edited by EG Neilson, WG Couser. Philadelphia, Lippincott-Raven, 1997, pp 217-234
6. Tryggvason K: Mutations in type IV collagen genes and Alport phenotypes. Contrib Nephrol 1996, 117:154171
7. Turner N, Mason PJ, Brown R, Fox M, Povey S, Rees A, Pusey CD: Molecular cloning of the human Goodpasture antigen demonstrates it to be the o3 chain of type IV collagen. J Clin Invest 1992, 89:592-601
8. Noakes PG, Gautam M, Mudd J, Sanes JR, Merlie JP: Aberrant differentiation of neuromuscular junctions in mice lacking s-laminin/laminin-/32. Nature 1995, 374: 258-262
9. Kerjaschki D, Neale TJ: Molecular mechanisms of glomerular injury in rat experimental membranous nephropathy (Heymann nephritis). J Am Soc Nephrol 1996, 7:2518-2526
10. Britton RS: Metal-induced hepatotoxicity. Semin Liver Dis 1996, 16:3-12
11. Lonn E, Factor SM, Van Hoeven KH, Wen WH, Zhao M, Dawood F, Liu P: Effects of oxygen free radicals and scavengers on the cardiac extracellular collagen matrix during ischemia-reperfusion. Can J Cardiol 1994, 10:203-213
12. Orkin RW, Gehron P, McGoodwin EB, Martin GR, Valentine T, Swarm R: A murine tumor producing a matrix of basement membrane. J Exp Med 1977, 145:204220
13. Gutteridge JM: Ferrous-salt-promoted damage to deoxyribose and benzoate: the increased effectiveness of hydroxyl-radical scavengers in the presence of EDTA. Biochem J 1987, 243:709-714
14. Davies KJ: Protein damage and degradation by oxy-gen radicals. I. General aspects. J Biol Chem 1987, 262:9895-9901
15. Richmond R, Halliwell B, Chauhan J, Darbre A: Superoxide-dependent formation of hydroxyl radicals: detection of hydroxyl radicals by the hydroxylation of aromatic compounds. Anal Biochem 1981, 118:328-335
16. Greenwald RA, Moy WW: Inhibition of collagen gelation by action of the Superoxide radical. Arthritis Rheum 1979, 22:251-259
17. Girotti AW, Thomas JP, Jordan JE: Xanthine oxidasecatalyzed crosslinking of cell membrane proteins. Arch Biochem Biophys 1986, 251:639-653
18. Bull C, Fee JA, O'Neill P, Fielden EM: Iron-ethylenediaminetetraacetic acid (EDTA)-catalyzed Superoxide dismutation revisited: an explanation of why the dismutase activity of Fe-EDTA cannot be detected in the cytochrome c/xanthine oxidase assay system. Arch Biochem Biophys 1982, 215:551-555
19. Kleinman HK, McGarvey ML, Liotta LA, Robey PG, Tryggvason K, Martin GR: Isolation and characterization of type IV procollagen, laminin, and heparan sulfate proteoglycan from the EHS sarcoma. Biochemistry 1982, 21:6188-6193
20. Thomas CE, Jackson RL: Lipid hydroperoxide involvement in copper-dependent and independent oxidation of low density lipoproteins. J Pharmacol Exp Ther 1991, 256:1182-1188
21. Yurchenco PD, Cheng YS: Laminin self-assembly: a three-arm interaction hypothesis for the formation of a network in basement membranes. Contrib Nephrol 1994, 107:47-56
22. Yurchenco PD, Cheng YS, Colognato H: Laminin forms an independent network in basement membranes [published erratum appears in J Cell Biol 1992 18:493]. J Cell Biol 1992, 117:1119-1133
23. Engel J: Electron microscopy of extracellular matrix components. Methods Enzymol 1994, 245:469-88
24. Riley DP, Rivers WJ, Weiss RH: Stopped-flow kinetic analysis for monitoring Superoxide decay in aqueous systems. Anal Biochem 1991, 196:344-349
25. Mackay AR, Gomez DE, Cottam DW, Rees RC, Nason AM, Thorgeirsson UP: Identification of the 72-kDa (MMP-2) and 92-kDa (MMP-9) gelatinase/type IV collagenase in preparations of laminin and Matrigel. Biotechniques 1993, 15:1048-1051
26. Birkedal Hansen H: Proteolytic remodeling of extracellular matrix. Curr Opin Cell Biol 1995, 7:728-735
27. Meier B, Radeke HH, Selle S, Younes M, Sies H, Resch K, Habermehl GG: Human fibroblasts release reactive oxygen species in response to interleukin-1 or tumour necrosis factor-α. Biochem J 1989, 263:539-545
28. Radeke HH, Cross AR, Hancock JT, Jones OT, Nakamura M, Kaever V, Resch K: Functional expression of NADPH oxidase components (α- and β-subunits of cytochrome b558 and 45-kDa flavoprotein) by intrinsic human glomerular mesangial cells. J Biol Chem 1991, 266:21025-21029
29. Szatrowski TP, Nathan CF: Production of large amounts of hydrogen peroxide by human tumor cells. Cancer Res 1991.51:794-798
30. Rosen GM, Pou S, Ramos CL, Cohen MS, Britigan BE: Free radicals and phagocytic cells. FASEB J 1995, 9:200-209
31. Kaushal GP, Shah SV: Proteases and oxidants in glomerular injury. Immunologie Renal Diseases. Edited by EG Neilson, WG Couser. Philadelphia, LippincottRaven, 1997, pp 397-415
32. Davies KJ, Lin SW, Pacific! RE: Protein damage and degradation by oxygen radicals. IV. Degradation of denatured protein. J Biol Chem 1987, 262:9914-9920
33. Stadtman ER: Oxidation of free amino acids and amino acid residues in proteins by radiolysis and by metalcatalyzed reactions. Annu Rev Biochem 1993, 62:797821
34. Jarasch ED, Bruder G, Heid HW: Significance of xanthine oxidase in capillary endothelial cells. Acta Physiol Scand Suppl 1986, 548:39-46
35. Parks DA, Granger DN: Xanthine oxidase: biochemistry, distribution and physiology. Acta Physiol Scand Suppl 1986, 548:87-99
36. Weiss SJ: Oxygen, ischemia, and inflammation. Acta Physiol Scand Suppl 1986, 548:9-37
37. Halliwell B, Cross CE: Oxygen-derived species: their relation to human disease and environmental stress. Environ Health Perspect 1994, 102(Suppl 10):5-12
38. Charonis AS, Reger LA, Dege JE, Kouzi Koliakos K, Furcht LT, Wohlhueter RM, Tsilibary EC: Laminin alterations after in vitro nonenzymatic glycosylation. Diabetes 1990, 39:807-814
39. Weiner L, Kreimer D, Roth E, Silman I: Oxidative stress transforms acetylcholinesterase to a molten-globulelike state. Biochem Biophys Res Commun 1994, 198: 915-922
40. 2: conversion of proline residue to 2-pyrrolidone. J Biol Chem 1992, 267:23646-23651
41. Kashihara N, Watanabe Y, Makino H, Wallner E, Kanwar YS: Selective decreased de novo synthesis of glomerular proteoglycans under the influence of reactive oxygen species. Cell Biol 1992, 89:6309-6313
42. Panasyuk A, Frati E, Ribault D, Mitrovic D: Effect of reactive oxygen species on the biosynthesis and structure of newly synthesized proteoglycans. Free Radie Biol Med 1994, 16:157-167
43. Moseley R, Waddington R, Evans P, Halliwell B, Em-bery G: The chemical modification of glycosaminoglycan structure by oxygen-derived species in vitro. Biochim Biophys Acta 1995, 1244:245-252
44. Thakur V, Walker PD, Shah SV: Evidence suggesting a role for hydroxyl radical in puromycin aminonucleoside-induced proteinuria. Kidney Int 1988, 34:494-499
45. Miesel R, Kroger H, Kurpisz M, Weser U: Induction of arthritis in mice and rats by potassium peroxochromate and assessment of disease activity by whole blood chemiluminescence and 99mpertechnetate-imaging. Free Radie Res 1995, 23:213-227
46. Nonaka Y, Iwagaki H, Kimura T, Fuchimoto S, Orita K: Effect of reactive oxygen intermediates on the in vitro invasive capacity of tumor cells and liver metastasis in mice. Int J Cancer 1993, 54:983-6
47. Mignatti P: Extracellular matrix remodeling by metalloproteinases and plasminogen activators. Kidney Int Suppl 1995,49:512-814
48. Briggs RT, Drath DB, Karnovsky ML, Karnovsky MJ: Localization of NADH oxidase on the surface of human polymorphonuclear leukocytes by a new cytochemical technique. J Cell Biol 1975, 67:566-586
49. Winrow VR, Winyard PG, Morris CJ, Blake DR: Free radicals in inflammation: second messengers and mediators of tissue destruction. Br Med Bull 1993, 49: 506-522
50. Diamond JR, Bonventre JV, Karnovsky MJ: A role for oxygen free radicals in aminonucleoside nephrosis. Kidney Int 1986, 29:478-483
51. Shah SV: Evidence suggesting a role for hydroxyl radical in passive Heymann's nephritis. Am J Physiol 1988, 245:F337-F344
52. Price RG, Taylor SA, Crutcher E, Bergamaschi E, Franchini I, Mackie AD: The assay of laminin fragments in serum and urine as an indicator of renal damage induced by toxins. Toxicol Lett 1995, 77:313-318
53. Lin JJ, Partin J, Kaskel FJ: Changes in laminin during recovery from postischemic acute failure in rats. Exp Nephrol 1996, 4:279-285
54. Wallon HA, Byrne J, Robinson GB: Studies of the permeation properties of glomerular basement membrane: cross-linking renders glomerular basement membrane permeable to protein. Biochim Biophys Acta 1992, 1138:173-183
55. Boyd White J, Williams JC Jr: Effect of cross-linking on matrix permeability: a model for AGE-modified basement membranes. Diabetes 1996, 45:348-353