The high concentration of Arg213 → Gly extracellular superoxide dismutase (EC-SOD) in plasma is caused by a reduction of both heparin and collagen affinities

Biochemical Journal

Volumn 385, Issue 2, 2005, Pages 427-432

  Petersen, Steen V ^a   Olsen, Dorte Aa ^a   Kenney, John M ^b   Oury, Tim D ^c   Valnickova, Zuzana ^a   Thøgersen, Ida B ^a   Crapos, James D ^d   Enghild, Jan J ^a  

^a AARHUS UNIVERSITY   (Denmark)

^b EAST CAROLINA UNIVERSITY   (United States)

^c UNIVERSITY OF PITTSBURGH MEDICAL CENTER   (United States)

^d NATIONAL JEWISH MEDICAL AND RESEARCH CENTER   (United States)

Author keywords

Arg213 Gly (R213G); Collagen; Extracellular superoxide dismutase (EC SOD); Oxidative damage; Reduced affinity; Structure

Indexed keywords

CARDIOVASCULAR SYSTEM; COLLAGEN; DISEASES; STRUCTURAL ANALYSIS;

COLLAGEN AFFINITIES; EXTRACELLULAR SUPEROXIDE DISMUTASE (EC-SOD); HEART DISEASE; HEPARIN AFFINITY;

ENZYME KINETICS;

ARGININE; COLLAGEN; GLYCINE; HEPARIN; SUPEROXIDE DISMUTASE; PEPTIDE; SOD3 PROTEIN, HUMAN;

AMINO ACID SUBSTITUTION; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; ENZYME ASSAY; ENZYME BINDING; EXTRACELLULAR MATRIX; HEART DISEASE; HOMOZYGOTE; HUMAN; PRIORITY JOURNAL; PROTEIN PROTEIN INTERACTION; PROTEIN SECONDARY STRUCTURE; PROTEIN STRUCTURE; AFFINITY CHROMATOGRAPHY; AMINO ACID SEQUENCE; AORTA; BLOOD; CHEMISTRY; CIRCULAR DICHROISM; ENZYME SPECIFICITY; ENZYMOLOGY; GEL CHROMATOGRAPHY; GENETICS; METABOLISM; METHODOLOGY; MOLECULAR GENETICS; PH;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AORTA; ARGININE; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, AGAROSE; CIRCULAR DICHROISM; COLLAGEN; EXTRACELLULAR MATRIX; GLYCINE; HEPARIN; HUMANS; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; PEPTIDES; SUBSTRATE SPECIFICITY; SUPEROXIDE DISMUTASE;

EID: 12844261649     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20041218     Document Type: Article

References (38)

1. Fattman, C. L., Schaefer, L. M. and Oury, T. D. (2003) Extracellular superoxide dismutase in biology and medicine. Free Radical Biol. Med. 35, 236-256
2. Marklund, S. L. (1982) Human copper-containing superoxide dismutase of high molecular weight. Proc. Natl. Acad. Sci. U.S.A. 79, 7634-7638
3. Oury, T. D., Crapo, J. D., Valnickova, Z. and Enghild, J. J. (1996) Human extracellular superoxide dismutase is a tetramer composed of two disulphide-linked dimers: a simplified, high-yield purification of extracellular superoxide dismutase. Biochem. J. 317, 51-57
4. Petersen, S. V., Oury, T. D., Valnickova, Z., Thogersen, I. B., Hojrup, P., Crapo, J. D. and Enghild, J. J. (2003) The dual nature of human extracellular superoxide dismutase: one sequence and two structures. Proc. Natl. Acad. Sci. U.S.A. 100, 13875-13880
5. Karlsson, K., Lindahl, U. and Marklund, S. L. (1988) Binding of human extracellular superoxide dismutase C to sulphated glycosaminoglycans. Biochem. J. 256, 29-33
6. Adachi, T. and Marklund, S. L. (1989) Interactions between human extracellular superoxide dismutase C and sulfated polysaccharides. J. Biol. Chem. 264, 8537-8541
7. Adachi, T., Kodera, T., Ohta, H., Hayashi, K. and Hirano, K. (1992) The heparin binding site of human extracellular-superoxide dismutase. Arch. Biochem. Biophys. 297, 155-161
8. Sandstrom, J., Carlsson, L., Marklund, S. L. and Edlund, T. (1992) The heparin-binding domain of extracellular superoxide dismutase C and formation of variants with reduced heparin affinity. J. Biol. Chem. 267, 18205-18209
9. Petersen, S. V., Oury, T., Oestergaard, L., Valnickova, Z., Wegrzyn, J., Thogersen, I. B., Jacobsen, C., Bowler, R. P., Fattman, C. L., Crapo, J. D. et al. (2004) Extracellular superoxide dismutase (EC-SOD) binds to type I collagen and protects against oxidative fragmentation. J. Biol. Chem. 279, 13705-13710
10. Fattman, C. L., Chang, L. Y., Termin, T. A., Petersen, L., Enghild, J. J. and Oury, T. D. (2003) Enhanced bleomycin-induced pulmonary damage in mice lacking extracellular superoxide dismutase. Free Radical Biol. Med. 35, 763-771
11. Enghild, J. J., Thogersen, I. B., Oury, T. D., Valnickova, Z., Hojrup, P. and Crapo, J. D. (1999) The heparin-binding domain of extracellular superoxide dismutase is proteolytically processed intracellularly during biosynthesis. J. Biol. Chem. 274, 14818-14822
12. Bowler, R. P., Nicks, M., Olsen, D. A., Thogersen, I. B., Valnickova, Z., Hojrup, P., Franzusoff, A., Enghild, J. J. and Crapo, J. D. (2002) Furin proteolytically processes the heparin-binding region of extracellular superoxide dismutase. J. Biol. Chem. 277, 16505-16511
13. Olsen, D. A., Petersen, S. V., Oury, T. D., Valnickova, Z., Thogersen, I. B., Kristensen, T., Bowler, R. P., Crapo, J. D. and Enghild, J. J. (2004) The intracellular proteolytic processing of extracellular superoxide dismutase (EC-SOD) is a two step event. J. Biol. Chem. 279, 22152-22157
14. Hjalmarsson, K., Marklund, S. L., Engstrom, A. and Edlund, T. (1987) Isolation and sequence of complementary DNA encoding human extracellular superoxide dismutase. Proc. Natl. Acad. Sci. U.S.A. 84, 6340-6344
15. Tibell, L. A., Sethson, I. and Buevich, A. V. (1997) Characterization of the heparin-binding domain of human extracellular superoxide dismutase. Biochim. Biophys. Acta 1340, 21-32
16. Lookene, A., Stenlund, P. and Tibell, L. A. (2000) Characterization of heparin binding of human extracellular superoxide dismutase. Biochemistry 39, 230-236
17. Stenlund, P., Lindberg, M. J. and Tibell, L. A. (2002) Structural requirements for high-affinity heparin binding: alanine scanning analysis of charged residues in the C-terminal domain of human extracellular superoxide dismutase. Biochemistry 41, 3168-3175
18. Sandstrom, J., Nilsson, P., Karlsson, K. and Marklund, S. L. (1994) 10-fold increase in human plasma extracellular superoxide dismutase content caused by a mutation in heparin-binding domain. J. Biol. Chem. 269, 19163-19166
19. Folz, R. J., Peno-Green, L. and Crapo, J. D. (1994) Identification of a homozygous missense mutation (Arg to Gly) in the critical binding region of the human EC-SOD gene (SOD3) and its association with dramatically increased serum enzyme levels. Hum. Mol. Genet. 3, 2251-2254
20. Yamada, H., Yamada, Y., Adachi, T., Goto, H., Ogasawara, N., Futenma, A., Kitano, M., Hirano, K. and Kato, K. (1995) Molecular analysis of extracellular-superoxide dismutase gene associated with high level in serum. Jpn. J. Hum. Genet. 40, 177-184
21. Marklund, S. L., Nilsson, P., Israelsson, K., Schampi, I., Peltonen, M. and Asplund, K. (1997) Two variants of extracellular-superoxide dismutase: relationship to cardiovascular risk factors in an unselected middle-aged population. J. Intern. Med. 242, 5-14
22. Wang, X. L., Adachi, T., Sim, A. S. and Wilcken, D. E. (1998) Plasma extracellular superoxide dismutase levels in an Australian population with coronary artery disease. Arterioscler. Thromb. Vasc. Biol. 18, 1915-1921
23. Juul, K., Tybjaerg-Hansen, A., Marklund, S., Heegaard, N. H., Steffensen, R., Sillesen, H., Jensen, G. and Nordestgaard, B. G. (2004) Genetically reduced antioxidative protection and increased ischaemic heart disease risk: the Copenhagen City Heart Study. Circulation 109, 59-65
24. Bury, A. F. (1981) Analysis of protein and peptide mixtures. Evaluation of three sodium dodecyl sulfate-polyacrylamide gel electrophoresis buffer systems. J. Chromatogr. 213, 491-500
25. Matsudaira, P. (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J. Biol. Chem. 262, 10035-10038
26. Meltzer, N. M., Tous, G. I., Gruber, S. and Stein, S. (1987) Gas-phase hydrolysis of proteins and peptides. Anal. Biochem. 160, 356-361
27. Luo, P. and Baldwin, R. L. (1997) Mechanism of helix induction by trifluoroethanol: a framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 36, 8413-8421
28. Adachi, T., Yamada, H., Yamada, Y., Morihara, N., Yamazaki, N., Murakami, T., Futenma, A., Kato, K. and Hirano, K. (1996) Substitution of glycine for arginine-213 in extracellular-superoxide dismutase impairs affinity for heparin and endothelial cell surface. Biochem. J. 313, 235-239
29. Adachi, T., Morihara, N., Yamazaki, N., Yamada, H., Futenma, A., Kato, K. and Hirano, K. (1996) An arginine-213 to glycine mutation in human extracellular-superoxide dismutase reduces susceptibility to trypsin-like proteinases. J. Biochem. (Tokyo) 120, 184-188
30. Oury, T. D., Chang, L. Y., Marklund, S. L., Day, B. J. and Crapo, J. D. (1994) Immunocytochemical localization of extracellular superoxide dismutase in human lung. Lab. Invest. 70, 889-898
31. Oury, T. D., Day, B. J. and Crapo, J. D. (1996) Extracellular superoxide dismutase in vessels and airways of humans and baboons. Free Radical Biol. Med. 20, 957-965
32. Stralin, P., Karlsson, K., Johansson, B. O. and Marklund, S. L. (1995) The interstitium of the human arterial wall contains very large amounts of extracellular superoxide dismutase. Arterioscler. Thromb. Vasc. Biol. 15, 2032-2036
33. Oury, T. D., Thakker, K., Menache, M., Chang, L. Y., Crapo, J. D. and Day, B. J. (2001) Attenuation of bleomycin-induced pulmonary fibrosis by a catalytic antioxidant metalloporphyrin. Am. J. Respir. Cell Mol. Biol. 25, 164-169
34. Rahman, I. (2002) Oxidative stress and gene transcription in asthma and chronic obstructive pulmonary disease: antioxidant therapeutic targets. Curr. Drug Targets Inflamm. Allergy 1, 291-315
35. Emsley, J., Knight, C. G., Farndale, R. W., Barnes, M. J. and Liddington, R. C. (2000) Structural basis of collagen recognition by integrin alpha2beta1. Cell (Cambridge, Mass.) 101, 47-56
36. Nishida, N., Sumikawa, H., Sakakura, M., Shimba, N., Takahashi, H., Terasawa, H., Suzuki, E. I. and Shimada, I. (2003) Collagen-binding mode of vWF-A3 domain determined by a transferred cross-saturation experiment. Nat. Struct. Biol. 10, 53-58
37. Yamada, H., Yamada, Y., Adachi, T., Fukatsu, A., Sakuma, M., Futenma, A. and Kakumu, S. (2000) Protective role of extracellular superoxide dismutase in hemodialysis patients. Nephron 84, 218-223
38. Carlsson, L. M., Jonsson, J., Edlund, T. and Marklund, S. L. (1995) Mice lacking extracellular superoxide dismutase are more sensitive to hyperoxia. Proc. Natl. Acad. Sci. U.S.A. 92, 6264-6268