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Volumn 56, Issue 20, 1996, Pages 4636-4643

Hyperresistance of leukemia cells to photodynamic inactivation after long-term exposure to hemin

Author keywords

[No Author keywords available]

Indexed keywords

HEMIN; MEROCYANINE;

EID: 0029838484     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (25)

References (37)
  • 1
    • 0023464537 scopus 로고
    • Merocyanine 540
    • Sieber, F. Merocyanine 540. Photochem. Photobiol , 46: 1035-1042, 1987
    • (1987) Photochem. Photobiol , vol.46 , pp. 1035-1042
    • Sieber, F.1
  • 3
    • 0001809611 scopus 로고
    • Extracorporeal purging of bone marrow grafts by dye-sensitized photoirradiation
    • J. Gee (ed.), Boca Raton, FL: CRC Press, Inc.
    • Sieber, F Extracorporeal purging of bone marrow grafts by dye-sensitized photoirradiation In: J. Gee (ed.), Bone Marrow Processing and Purging. A Practical Guide, pp. 263-280 Boca Raton, FL: CRC Press, Inc., 1991.
    • (1991) Bone Marrow Processing and Purging. A Practical Guide , pp. 263-280
    • Sieber, F.1
  • 4
    • 0011230888 scopus 로고
    • Photodynamic action of merocyanine 540 on artificial and natural cell membranes: Involvement of singlet molecular oxygen
    • Kalyanaraman, B., Feix, J. B., Sieber, F., Thomas, J. P., and Girotti, A. W. Photodynamic action of merocyanine 540 on artificial and natural cell membranes: involvement of singlet molecular oxygen. Proc. Natl Acad Sci. USA, 84: 2999-3003, 1987.
    • (1987) Proc. Natl Acad Sci. USA , vol.84 , pp. 2999-3003
    • Kalyanaraman, B.1    Feix, J.B.2    Sieber, F.3    Thomas, J.P.4    Girotti, A.W.5
  • 5
    • 0018905725 scopus 로고
    • Perturbations of membrane structure by optical probes. I. Location and structural sensitivity of merocyanine 540 bound to phospholipid membranes
    • Lelkes, P. I., and Miller, I. R Perturbations of membrane structure by optical probes. I. Location and structural sensitivity of merocyanine 540 bound to phospholipid membranes. J. Membr. Biol , 52: 1-15, 1980.
    • (1980) J. Membr. Biol , vol.52 , pp. 1-15
    • Lelkes, P.I.1    Miller, I.R.2
  • 6
    • 0025408177 scopus 로고
    • Photodynamic lipid peroxidation in biological systems
    • Girotti, A. W. Photodynamic lipid peroxidation in biological systems. Photochem. Photobiol., 51: 497-509, 1990.
    • (1990) Photochem. Photobiol. , vol.51 , pp. 497-509
    • Girotti, A.W.1
  • 7
    • 0027329036 scopus 로고
    • Photodynamic action of merocyanine 540 on leukemia cells, iron stimulated lipid peroxidation and cell killing
    • Lin, F., and Girotti, A. W. Photodynamic action of merocyanine 540 on leukemia cells, iron stimulated lipid peroxidation and cell killing. Arch Biochem. Biophys., 300: 714-723, 1993.
    • (1993) Arch Biochem. Biophys. , vol.300 , pp. 714-723
    • Lin, F.1    Girotti, A.W.2
  • 8
    • 0029360765 scopus 로고
    • Stimulatory and inhibitory effects of iron on photodynamic inactivation of leukemia cells
    • Lin, F., and Girotti, A. W. Stimulatory and inhibitory effects of iron on photodynamic inactivation of leukemia cells. Photochem. Photobiol., 62, 528-534, 1995
    • (1995) Photochem. Photobiol. , vol.62 , pp. 528-534
    • Lin, F.1    Girotti, A.W.2
  • 9
    • 0026644828 scopus 로고
    • Selenoperoxidase-mediated cytoprotection against merocyanine 540-sensitized photoperoxidation and photokilling of leukemia cells
    • Lin, F., Geiger, P. G , and Girotti, A. W. Selenoperoxidase-mediated cytoprotection against merocyanine 540-sensitized photoperoxidation and photokilling of leukemia cells. Cancer Res., 52: 5282-5290, 1992.
    • (1992) Cancer Res. , vol.52 , pp. 5282-5290
    • Lin, F.1    Geiger, P.G.2    Girotti, A.W.3
  • 11
    • 0020027081 scopus 로고
    • The role of heme biosynthetic and degradative enzymes in erythroid colony development: The effect of hemin
    • Ibrahim, N. G., Lutton, J. D., and Levere, R. D. The role of heme biosynthetic and degradative enzymes in erythroid colony development: the effect of hemin Br. J. Haematol , 50: 17-28, 1982.
    • (1982) Br. J. Haematol , vol.50 , pp. 17-28
    • Ibrahim, N.G.1    Lutton, J.D.2    Levere, R.D.3
  • 13
    • 85052774941 scopus 로고
    • Catalase activity
    • R. A. Greenwald (ed.), Boca Raton, FL: CRC Press, Inc.
    • Claiborne, A Catalase activity In: R. A. Greenwald (ed.), Handbook of Methods for Oxygen Free Radical Research, pp. 283-284. Boca Raton, FL: CRC Press, Inc., 1985.
    • (1985) Handbook of Methods for Oxygen Free Radical Research , pp. 283-284
    • Claiborne, A.1
  • 14
    • 0001422064 scopus 로고
    • Glucose-6-phosphate dehydrogenase
    • H U. Bergmeyer (ed.), Weinheim: Verlag Chemie
    • Deutsch, J Glucose-6-phosphate dehydrogenase In. H U. Bergmeyer (ed.), Methods of Enzymatic Analysis, Vol. 3, pp. 190-197. Weinheim: Verlag Chemie, 1983.
    • (1983) Methods of Enzymatic Analysis , vol.3 , pp. 190-197
    • Deutsch, J.1
  • 16
    • 0014481378 scopus 로고
    • Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione applications to mammalian blood and other tissues
    • Tietze, F Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione applications to mammalian blood and other tissues. Anal Biochem , 27: 502-522, 1969.
    • (1969) Anal Biochem , vol.27 , pp. 502-522
    • Tietze, F.1
  • 17
    • 0002219603 scopus 로고
    • Alpha, beta, gamma and omega - The roster of the plasma proteins
    • F. W. Putnam (ed.), New York: Academic Press
    • Putnam, F W , Alpha, beta, gamma and omega - the roster of the plasma proteins. In: F. W. Putnam (ed.), The Plasma Proteins, Vol. 1, pp. 57-131. New York: Academic Press, 1975
    • (1975) The Plasma Proteins , vol.1 , pp. 57-131
    • Putnam, F.W.1
  • 18
    • 0344041416 scopus 로고
    • Selective killing of leukemia cells by merocyanine 540-mediated photosensitization
    • Sieber, F , Spivak, J. C , and Sutcliffe, A M. Selective killing of leukemia cells by merocyanine 540-mediated photosensitization. Proc Natl Acad. Sci. USA, 18: 7584-7587, 1984.
    • (1984) Proc Natl Acad. Sci. USA , vol.18 , pp. 7584-7587
    • Sieber, F.1    Spivak, J.C.2    Sutcliffe, A.M.3
  • 19
    • 0002569886 scopus 로고
    • Dye exclusion tests for cell viability
    • P. F. Kruse Jr and M. K. Patterson (eds.), New York: Academic Press
    • Phillips, H. J. Dye exclusion tests for cell viability. In: P. F. Kruse Jr and M. K. Patterson (eds.), Tissue Culture, pp. 406-408. New York: Academic Press, 1973.
    • (1973) Tissue Culture , pp. 406-408
    • Phillips, H.J.1
  • 20
    • 0027306178 scopus 로고
    • Hyperexpression of catalase in selenium-deprived murine L1210 cells
    • Lin, F., Thomas, J. P., and Girotti, A. W. Hyperexpression of catalase in selenium-deprived murine L1210 cells. Arch. Biochem. Biophys., 305: 176-185, 1993.
    • (1993) Arch. Biochem. Biophys. , vol.305 , pp. 176-185
    • Lin, F.1    Thomas, J.P.2    Girotti, A.W.3
  • 21
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of the head of bacteriophage T4
    • Laemmli, U. K. Cleavage of structural proteins during assembly of the head of bacteriophage T4. Nature (Lond.), 227: 680-685, 1970.
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 0027533498 scopus 로고
    • Selenoperoxidase-mediated cytoprotection against the damaging effects of tert-butyl hydroperoxide on leukemia cells
    • Geiger, P. G., Lin, F., and Girotti, A. W. Selenoperoxidase-mediated cytoprotection against the damaging effects of tert-butyl hydroperoxide on leukemia cells. Free Radical Biol. & Med , 14: 251-266, 1993.
    • (1993) Free Radical Biol. & Med , vol.14 , pp. 251-266
    • Geiger, P.G.1    Lin, F.2    Girotti, A.W.3
  • 23
    • 0027520674 scopus 로고
    • Tumor cell heme uptake induces ferritin synthesis resulting in altered oxidant sensitivity: Possible role in chemotherapy efficacy
    • Cermak, J., Balla, J., Jacob, H. S., Balla, G., Enright, H., Nath, K , and Vercellotti, G. M. Tumor cell heme uptake induces ferritin synthesis resulting in altered oxidant sensitivity: possible role in chemotherapy efficacy. Cancer Res., 53: 5308-5313, 1993
    • (1993) Cancer Res. , vol.53 , pp. 5308-5313
    • Cermak, J.1    Balla, J.2    Jacob, H.S.3    Balla, G.4    Enright, H.5    Nath, K.6    Vercellotti, G.M.7
  • 24
    • 0025969686 scopus 로고
    • Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron
    • Eisenstein, R. S., Garcia-Mayol, D., Pettingell, W., and Munro, H. N. Regulation of ferritin and heme oxygenase synthesis in rat fibroblasts by different forms of iron. Proc. Natl. Acad. Sci. USA, 88: 688-692, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 688-692
    • Eisenstein, R.S.1    Garcia-Mayol, D.2    Pettingell, W.3    Munro, H.N.4
  • 25
    • 0023731036 scopus 로고
    • Heme oxygenase: Function, multiplicity, regulatory mechanisms, and clinical applications
    • Maines, M. D. Heme oxygenase: function, multiplicity, regulatory mechanisms, and clinical applications. FASEB J , 2: 2557-2568, 1988.
    • (1988) FASEB J , vol.2 , pp. 2557-2568
    • Maines, M.D.1
  • 26
    • 7444249085 scopus 로고
    • The biochemistry of desferrioxamine and its relationship to iron metabolism
    • Keberle, H. The biochemistry of desferrioxamine and its relationship to iron metabolism. Ann. NY Acad. Sci., 119: 758-768, 1964.
    • (1964) Ann. NY Acad. Sci. , vol.119 , pp. 758-768
    • Keberle, H.1
  • 27
    • 0027255106 scopus 로고
    • Oxidative stress resulting from ultraviolet a irradiation of human skin fibroblasts leads to a heme oxygenase-dependent increase in ferritin
    • Vile, G. F , and Tyrrell, R M. Oxidative stress resulting from ultraviolet A irradiation of human skin fibroblasts leads to a heme oxygenase-dependent increase in ferritin. J. Biol. Chem., 268: 14678-14681, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14678-14681
    • Vile, G.F.1    Tyrrell, R.M.2
  • 28
    • 0019961225 scopus 로고
    • Chemoprevention of neonatal jaundice: Potency of tin-protoporphyrin in an animal model
    • Washington DC
    • Drummond, G. S., and Kappas, A. Chemoprevention of neonatal jaundice: potency of tin-protoporphyrin in an animal model. Science (Washington DC), 217: 1250-1252, 1982.
    • (1982) Science , vol.217 , pp. 1250-1252
    • Drummond, G.S.1    Kappas, A.2
  • 29
    • 0025038744 scopus 로고
    • Iron loading of endothelial cells augments oxidant damage
    • Balla, G., Vercellotti, G. M., and Jacob, H S Iron loading of endothelial cells augments oxidant damage J. Lab. Clin. Med , 116: 546-554, 1990
    • (1990) J. Lab. Clin. Med , vol.116 , pp. 546-554
    • Balla, G.1    Vercellotti, G.M.2    Jacob, H.S.3
  • 30
    • 0028934323 scopus 로고
    • Endothelial cell heme oxygenase and ferritin induction in rat lung by hemoglobin in vivo
    • Balla, J., Nath, K. A., Balla, G., Juckett, M. B., Jacob, H. S , and Vercellotti, G. M. Endothelial cell heme oxygenase and ferritin induction in rat lung by hemoglobin in vivo. Am. J. Physiol., 268: L321-L327, 1995
    • (1995) Am. J. Physiol. , vol.268
    • Balla, J.1    Nath, K.A.2    Balla, G.3    Juckett, M.B.4    Jacob, H.S.5    Vercellotti, G.M.6
  • 31
    • 0028300334 scopus 로고
    • Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts
    • Vile, G. F., Basu-Modak, S., Waltner, C., and Tyrrell, R. M. Heme oxygenase 1 mediates an adaptive response to oxidative stress in human skin fibroblasts. Proc. Natl. Acad. Sci. USA, 91: 2607-2610, 1994.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 2607-2610
    • Vile, G.F.1    Basu-Modak, S.2    Waltner, C.3    Tyrrell, R.M.4
  • 32
    • 0026113376 scopus 로고
    • Increased transcription and translation of heme oxygenase in Chinese hamster fibroblasts following photodynamic stress or Photofrin II incubation
    • Gomer, C. J., Luna, M., Ferraro, A., and Rucker, N Increased transcription and translation of heme oxygenase in Chinese hamster fibroblasts following photodynamic stress or Photofrin II incubation Photochem. Photobiol., 53, 275-279, 1991.
    • (1991) Photochem. Photobiol. , vol.53 , pp. 275-279
    • Gomer, C.J.1    Luna, M.2    Ferraro, A.3    Rucker, N.4
  • 34
    • 0028589014 scopus 로고
    • Molecular regulation of iron proteins
    • Kuhn, L. C. Molecular regulation of iron proteins. Baillieres Clin. Haematol., 7: 763-785, 1994.
    • (1994) Baillieres Clin. Haematol. , vol.7 , pp. 763-785
    • Kuhn, L.C.1
  • 35
    • 0027751714 scopus 로고
    • Iron regulatory factor the conductor of cellular iron regulation
    • Melefors, O., and Hentze, M. W. Iron regulatory factor the conductor of cellular iron regulation. Blood Rev., 7: 251-258, 1993.
    • (1993) Blood Rev. , vol.7 , pp. 251-258
    • Melefors, O.1    Hentze, M.W.2
  • 36
    • 0348016662 scopus 로고
    • Ferritin in malignant cells
    • P. Ponka, H. M. Schulman, and R. C Woodsworth (eds.), Boca Raton, FL: CRC Press, Inc
    • Arosio, P , Levi, S., Cairo, G , Cazzolo, M , and Farigon, S. Ferritin in malignant cells. In: P. Ponka, H. M. Schulman, and R. C Woodsworth (eds.), Iron Transport and Storage, pp. 201-216. Boca Raton, FL: CRC Press, Inc , 1990.
    • (1990) Iron Transport and Storage , pp. 201-216
    • Arosio, P.1    Levi, S.2    Cairo, G.3    Cazzolo, M.4    Farigon, S.5
  • 37
    • 0027498438 scopus 로고
    • Biochemistry of heme and its containment
    • Muller-Eberhard, U., and Fraig, M Biochemistry of heme and its containment. Am. J. Hematol , 42 59-62, 1993.
    • (1993) Am. J. Hematol , vol.42 , pp. 59-62
    • Muller-Eberhard, U.1    Fraig, M.2


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