Microperoxidases catalytically degrade reactive oxygen species and may be anti-cataract agents

Experimental Eye Research

Volumn 65, Issue 4, 1997, Pages 457-470

  Spector, Abraham ^a   Ma, Wanchao ^a   Wang, Ren Rong ^a   Kleiman, Norman J ^a  

^a Coll Phys Surgs of Columbia Univ ^*  (United States)

Author keywords

Ascorbic acid; GSH; Hydrogen peroxide; Hydroxyl radical; Lens; Superoxide

Indexed keywords

CYTOCHROME C; HYDROXYL RADICAL; PEROXIDASE; SUPEROXIDE;

ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; CATARACT; LENS; NONHUMAN; OXIDATIVE STRESS; PRIORITY JOURNAL; PROTEIN DEGRADATION; RAT;

EID: 0030722939     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1997.0336     Document Type: Article

References (32)

1. Aron, J., Baldwin, D. A., Marques, H. M., Pratt, J. M. and Adams, P. A. (1986). Hemes and hemoproteins. 1: Preparation and analysis of the heme-containing octapeptide (microperoxidase-8) and identification of the monomeric form in aqueous solution. J. Inorg. Biochem. 27, 227-43.
2. Baba, Y., Mizushima, H. and Watanabe, H. (1969). Catalytic properties of cytochrome C heme peptides. Chem. Pharm. Bull. 17, 82-8.
3. Baldwin, D. A., Marques, H. M. and Pratt, J. M. (1987). Hemes and hemoproteins 5. Kinetics of the peroxidatic activity of microperoxidase-8: Model for peroxidase enzymes. J. Inorg. Biochem. 30, 203-17.
4. 2O- mediated nonphotodynamic crosslinking of lens crystallins generated by the heme-undecapeptide from cytochrome C: implications in man. Biochem. Biophys. Res. Commun. 113, 592-7.
5. Chance, B., Sies, H. and Boveris, A. (1979). Hydroperoxide metabolism in mammalian organs. Physiol. Rev. 59, 527-605.
6. Ehrenberg, A. and Theorell, H. (1955). On the stereo-chemical structure of cytochrome C. Acta Chem. Scand. 9, Part II, 1193-205.
7. Feder, N. (1970). A heme-peptide as an ultrastructural tracer. J. Histochem. Cytochem. 18, 911-3.
8. Flohé, L. and Otting, G. (1984). Superoxide dismutase assays. Meth. Enzymol. 105, 101-4.
9. Halliwell, B. and Gutteridge, J. M. C. (1984). Role of iron in oxygen radical reactions. Meth. Enzymol. 105, 47-56.
10. Harbury, H. A. and Loach, P. A. (1960a). Oxidation-linked proton functions in heme octa- and undecapeptides from mammalian cytochrome C. J. Biol. Chem. 235, 3640-5.
11. Harbury, H. A. and Loach, P. A. (1960b). Interaction of nitrogenous ligands with heme peptides from mammalian cytochrome C. J. Biol. Chem. 235, 3646-53.
12. 2 in hepatic microsomes. Meth. Enzymol. L11, 342-50.
13. Kleiman, N.J., Wang, R.-R. and Spector, A. (1990). Hydrogen peroxide-induced DNA damage in bovine lens epithelial cells. Mutation Res. 240, 35-45.
14. Kohn, K. W., Erickson, L. C., Ewig, R. A. G. and Friedman, C. A. (1976). Fractionation of DNA from mammalian cells by alkaline elution. Biochemistry 15, 4629-37.
15. Kraehenbuhl, J. P., Galardy, R. E. and Jamieson, J. D. (1974). Preparation and characterization of an immunoelectron microscope tracer consisting of a heme-octapeptide coupled to Fab. J. Exp. Med. 139, 208-23.
16. Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-5.
17. Massey, V. (1959). The microestimation of succinate and the extinction coefficient of cytochrome c. Biochim. Biophys. Acta 34, 255-6.
18. Paléus, S., Ehrenberg, A. and Tuppy, H. (1955). Study of a peptic degradation product of cytochrome C. II. Investigation of the linkage between peptide moiety and prosthetic group. Acta Chem. Scand. 9, 365-74.
19. Spector, A. (1995). Oxidative stress induced cataract: Mechanism of action. FASEB J. 9, 1173-82.
20. 2 induced DNA damage in bovine lens epithelial cell cultures. Exp. Eye Res. 49, 685-98.
21. 2 and photochemically induced cataract. Curr. Eye Res. 12, 163-79.
22. Spector, A., Wang, G.-M. and Wang, R.-R. (1993b). The prevention of cataract caused by oxidative stress in cultured rat lenses. II. Early effects of photochemical stress and recovery. Exp. Eye Res. 57, 659-67.
23. 2 stress. Exp. Eye Res. 62, 521-39.
24. Takano, T., Kallai, O. B., Swanson, R. and Dickerson, R. E. (1973). The structure of ferrocytochrome c at 2.45 A resolution. J. Biol. Chem. 248, 5234-55.
25. Theorell, H. (1956). Nature and mode of action of oxidation enzymes. Science 124, 467-72.
26. Tsou, C. L. (1951). Cytochrome C modified by digestion with proteolytic enzymes. Biochem. J. 49, 367-74.
27. Tuppy, H. and Paléus, S. (1955). Study of a peptic degradation product of cytochrome C. I. Purification and chemical composition. Acta Chem. Scand. 9, 353-64.
28. Vodnyánsky, L., Marton, A., Venekei, I., Végh, M., Blázovits, A., Kittel, A. and Horváth, I. (1985). Inhibition of lipid peroxidation by heme-nonapeptide derived from cytochrome C. Biochim. Biophys. Acta 835, 411-14.
29. Wang, K. and Spector, A. (1994). The chaperone activity of bovine a crystallin: Interaction with other lens crystallins in native and denatured states. J. Biol. Chem. 269, 13601-8.
30. Wendel, A. (1985). European Patent 0-165-534.
31. Wilson, S. R., Zucker, P. A., Huang, R.-R. C. and Spector, A. (1989). A development of synthetic compounds with glutathione peroxidase activity. J. Am. Chem. Soc. 111, 5936-9.
32. Yang, Y., Spector, A., Wang, R.-R. and Ma, W. (1997). Investigation of rat catalase gene enrichment in mouse cell and lens systems. (Submitted).