Spatial distribution of protein damage by singlet oxygen in keratinocytes

Photochemistry and Photobiology

Volumn 84, Issue 1, 2008, Pages 69-74

  He, Yu Ying ^a   Council, Sarah E ^a   Feng, Li ^a   Bonini, Marcelo G ^a   Chignell, Colin F ^a  

^a NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN; ROSE BENGAL; SINGLET OXYGEN;

CELL LINE; CHEMICAL STRUCTURE; CHEMISTRY; CONFERENCE PAPER; HUMAN; KERATINOCYTE; METABOLISM;

CELL LINE; HUMANS; KERATINOCYTES; MOLECULAR STRUCTURE; PROTEINS; ROSE BENGAL; SINGLET OXYGEN;

ALEXA; CAPRA HIRCUS; ORYCTOLAGUS CUNICULUS;

EID: 37249087262     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1751-1097.2007.00199.x     Document Type: Conference Paper

References (25)

1. Davies, M. J. (2005) The oxidative environment and protein damage. Biochim. Biophys. Acta 1703, 93 109.
2. Hall, R. D., W. Chamulitrat, N. Takahashi, C. F. Chignell R. P. Mason (1989) Detection of singlet (1O2) oxygen phosphorescence during chloroperoxidase-catalyzed decomposition of ethyl hydroperoxide. J. Biol. Chem. 264, 7900 7906.
3. Redmond, R. W. I. E. Kochevar (2006) Spatially-resolved cellular responses to singlet oxygen. Photochem. Photobiol. 82, 1178 1186.
4. Skovsen, E., J. W. Snyder, J. D. C. Lambert P. R. Ogilby (2005) Lifetime and diffusion of singlet oxygen in a cell. J. Phys. Chem. B 109, 8570 8573.
5. Snyder, J. W., E. Skovsen, J. D. Lambert P. R. Ogilby (2005) Subcellular, time-resolved studies of singlet oxygen in single cells. J. Am. Chem. Soc. 127, 14558 14559.
6. Davies, M. J. (2004) Reactive species formed on proteins exposed to singlet oxygen. Photochem. Photobiol. Sci. 3, 17 25.
7. Mason, R. P. (2004) Using anti-5,5-dimethyl-1-pyrroline N-oxide (anti-DMPO) to detect protein radicals in time and space with immuno-spin trapping. Free Radic. Biol. Med. 36, 1214 1223.
8. Ramirez, D. C., Y. R. Chen R. P. Mason (2003) Immunochemical detection of hemoglobin-derived radicals formed by reaction with hydrogen peroxide: Involvement of a protein-tyrosyl radical. Free Radic. Biol. Med. 34, 830 839.
9. Bilski, P., B. M. Kukielczak C. F. Chignell (1998) Photoproduction and direct spectral detection of singlet molecular oxygen (1O2) in keratinocytes stained with rose bengal. Photochem. Photobiol. 68, 675 678.
10. Bonini, M. G., A. G. Siraki, B. S. Atanassov R. P. Mason (2007) Immunolocalization of hypochlorite-induced, catalase-bound free radical formation in mouse hepatocytes. Free Radic. Biol. Med. 42, 530 540.
11. Boukamp, P., R. T. Petrussevska, D. Breitkreutz, J. Hornung, A. Markham N. E. Fusenig (1988) Normal keratinization in a spontaneously immortalized aneuploid human keratinocyte cell line. J. Cell Biol. 106, 761 771.
12. Detweiler, C. D., L. J. Deterding, K. B. Tomer, C. F. Chignell, D. Germolec R. P. Mason (2002) Immunological identification of the heart myoglobin radical formed by hydrogen peroxide. Free Radic. Biol. Med. 33, 364 369.
13. Kato, N., M. Nakamura T. Uchiyama (1999) H-1 NMR studies of the reactions of copper(I) and copper(II) with D-penicillamine and glutathione. J. Inorg. Biochem. 75, 117 121.
14. He, Y. Y., J. L. Huang, D. C. Ramirez C. F. Chignell (2003) Role of reduced glutathione efflux in apoptosis of immortalized human keratinocytes induced by UVA. J. Biol. Chem. 278, 8058 8064.
15. Wright, A., C. L. Hawkins M. J. Davies (2003) Photo-oxidation of cells generates long-lived intracellular protein peroxides. Free Radic. Biol. Med. 34, 637 647.
16. Ramirez, D. C., S. E. Mejiba R. P. Mason (2005) Copper-catalyzed protein oxidation and its modulation by carbon dioxide: Enhancement of protein radicals in cells. J. Biol. Chem. 280, 27402 27411.
17. Hall, R. D. C. F. Chignell (1987) Steady-state near-infrared detection of singlet molecular oxygen: A Stern-Volmer quenching experiment with sodium azide. Photochem. Photobiol. 45, 459 464.
18. Kochevar, I. E., J. Bouvier, M. Lynch C. W. Lin (1994) Influence of dye and protein location on photosensitization of the plasma membrane. Biochim. Biophys. Acta 1196, 172 180.
19. Bottone, M. G., C. Soldani, A. Fraschini, C. Alpini, A. C. Croce, G. Bottiroli C. Pellicciari (2007) Enzyme-assisted photosensitization with rose bengal acetate induces structural and functional alteration of mitochondria in HeLa cells. Histochem. Cell Biol. 127, 263 271.
20. Panzarini, E., B. Tenuzzo, F. Palazzo, A. Chionna L. Dini (2006) Apoptosis induction and mitochondria alteration in human HeLa tumour cells by photoproducts of rose bengal acetate. J. Photochem. Photobiol. B, Biol. 83, 39 47.
21. Soldani, C., M. G. Bottone, A. C. Croce, A. Fraschini, G. Bottiroli C. Pellicciari (2004) The Golgi apparatus is a primary site of intracellular damage after photosensitization with rose bengal acetate. Eur. J. Histochem. 48, 443 448.
22. Inbaraj, J. J., B. M. Kukielczak, P. Bilski, S. L. Sandvik C. F. Chignell (2001) Photochemistry and photocytotoxicity of alkaloids from Goldenseal (Hydrastis canadensis L.) 1. Berberine. Chem. Res. Toxicol. 14, 1529 1534.
23. Davila, J. A. Harriman (1990) Photoreactions of macrocyclic dyes bound to human serum albumin. Photochem. Photobiol. 51, 9 19.
24. Afanas'ev, I. B. (1989) Superoxide Ion: Chemistry and Biological Implications, Vol. 1. CRC Press, Boca Raton, FL.
25. Palmer, B. M., S. Vogt, Z. Y. Chen, R. R. Lachapelle M. M. LeWinter (2006) Intracellular distributions of essential elements in cardiomyocytes. J. Struct. Biol. 155, 12 21.