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Volumn 26, Issue 9-10, 1999, Pages 1172-1180

Ascorbic acid maintenance in HaCaT cells prevents radical formation and apoptosis by UV-B

Author keywords

Apoptosis; Ascorbic acid 2 phosphate; Ascorbyl free radical reductase; Dehydroascorbate reductase; Free radicals; HaCaT cells; Keratinocytes

Indexed keywords

ASCORBATE OXIDASE; ASCORBIC ACID;

EID: 0032982685     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0891-5849(98)00311-6     Document Type: Article
Times cited : (59)

References (46)
  • 1
    • 0026043824 scopus 로고
    • Mechanism of lipid radical formation following exposure of epidermal homogenate to ultraviolet light
    • Ogura R., Sugiyama M., Nishi J., Haramaki N. Mechanism of lipid radical formation following exposure of epidermal homogenate to ultraviolet light. J. Invest. Dermatol. 97:1991;1044-1047.
    • (1991) J. Invest. Dermatol. , vol.97 , pp. 1044-1047
    • Ogura, R.1    Sugiyama, M.2    Nishi, J.3    Haramaki, N.4
  • 2
    • 0026636441 scopus 로고
    • Free radicals, antioxidant, and human disease: Where are we now?
    • Halliwell B., Gutteridge J.M.C., Cross C.E. Free radicals, antioxidant, and human disease where are we now? J. Lab. Med. 119:1992;598-620.
    • (1992) J. Lab. Med. , vol.119 , pp. 598-620
    • Halliwell, B.1    Gutteridge, J.M.C.2    Cross, C.E.3
  • 4
    • 0027327373 scopus 로고
    • Biology of free radical scavengers: An evaluation of ascorbate
    • Rose R.C., Bode A.M. Biology of free radical scavengers an evaluation of ascorbate . FASEB J. 7:1993;1035-1042.
    • (1993) FASEB J , vol.7 , pp. 1035-1042
    • Rose, R.C.1    Bode, A.M.2
  • 5
    • 0030874407 scopus 로고    scopus 로고
    • Vitamin C abrogates the deleterious effects of UVB radiation on cutaneous immunity by a mechanism that does not depend on TNF-α
    • Nakamura T., Pinnel R.S., Darr D., Kurimoto I., Itami S., Yoshikawa K., Streilein J.W. Vitamin C abrogates the deleterious effects of UVB radiation on cutaneous immunity by a mechanism that does not depend on TNF-α J. Invest. Dermatol. 109:1997;20-24.
    • (1997) J. Invest. Dermatol. , vol.109 , pp. 20-24
    • Nakamura, T.1    Pinnel, R.S.2    Darr, D.3    Kurimoto, I.4    Itami, S.5    Yoshikawa, K.6    Streilein, J.W.7
  • 6
    • 0029898054 scopus 로고    scopus 로고
    • Antioxidant nutrients protect against UVB-induced oxidative damage to DNA of mouse keratinocytes in culture
    • Stewart M.S., Cameron G.S., Pence B.C. Antioxidant nutrients protect against UVB-induced oxidative damage to DNA of mouse keratinocytes in culture. J. Invest. Dermatol. 106:1996;1086-1089.
    • (1996) J. Invest. Dermatol. , vol.106 , pp. 1086-1089
    • Stewart, M.S.1    Cameron, G.S.2    Pence, B.C.3
  • 7
    • 0031059601 scopus 로고    scopus 로고
    • L-Ascorbic acid inhibits UVA-induced lipid peroxidation and secretion of IL-1α and IL-6 in cultured human keratinocytes in vitro
    • Tebbe B., Wu S., Geilen C.C., Eberle J., Kodelja V., Orfanos C.E. L-Ascorbic acid inhibits UVA-induced lipid peroxidation and secretion of IL-1α and IL-6 in cultured human keratinocytes in vitro. J. Invest. Dermatol. 108:1997;302-306.
    • (1997) J. Invest. Dermatol. , vol.108 , pp. 302-306
    • Tebbe, B.1    Wu, S.2    Geilen, C.C.3    Eberle, J.4    Kodelja, V.5    Orfanos, C.E.6
  • 8
    • 0020200648 scopus 로고
    • The reversibility of the vitamin C redox system: Electrochemical reasons and biological aspects
    • Sapper H., Kang S.O., Paul H.H., Lohmann W. The reversibility of the vitamin C redox system electrochemical reasons and biological aspects . Z. Naturforsch. 37:1982;942-946.
    • (1982) Z. Naturforsch. , vol.37 , pp. 942-946
    • Sapper, H.1    Kang, S.O.2    Paul, H.H.3    Lohmann, W.4
  • 9
    • 33947292106 scopus 로고
    • Ascorbic acid free radicals. I. Pulse radiolysis study of optical absorption and kinetic properties
    • Bielski B.H.J., Comstock D.A., Bowen R.A. Ascorbic acid free radicals. I. Pulse radiolysis study of optical absorption and kinetic properties. J. Am. Chem. Soc. 93:1971;5624-5629.
    • (1971) J. Am. Chem. Soc. , vol.93 , pp. 5624-5629
    • Bielski, B.H.J.1    Comstock, D.A.2    Bowen, R.A.3
  • 10
    • 0025066396 scopus 로고
    • Spontaneous decay of oxidized ascorbic acid (dehydro-L-ascorbic acid) evaluated by high pressure liquid chromatography
    • Bode A.M., Cunningham L., Rose R.C. Spontaneous decay of oxidized ascorbic acid (dehydro-L-ascorbic acid) evaluated by high pressure liquid chromatography. Clin. Chem. 36:1990;1807-1809.
    • (1990) Clin. Chem. , vol.36 , pp. 1807-1809
    • Bode, A.M.1    Cunningham, L.2    Rose, R.C.3
  • 11
    • 0029858883 scopus 로고    scopus 로고
    • Enhancement of radical intensity and cytotoxic activity of ascorbate by PSK and lignins
    • Satoh K., Sakagami H., Nakamura K. Enhancement of radical intensity and cytotoxic activity of ascorbate by PSK and lignins. Anticancer Res. 16:1996;2981-2986.
    • (1996) Anticancer Res , vol.16 , pp. 2981-2986
    • Satoh, K.1    Sakagami, H.2    Nakamura, K.3
  • 12
    • 0027202468 scopus 로고
    • Enzymatic basis for altered ascorbic acid and dehydroascorbic acid levels in diabetes
    • Bode A.M., Yavarow R.C., Fry D.A., Vargas T. Enzymatic basis for altered ascorbic acid and dehydroascorbic acid levels in diabetes. Biochem. Biophys. Res. Commun. 191:1993;1347-1353.
    • (1993) Biochem. Biophys. Res. Commun. , vol.191 , pp. 1347-1353
    • Bode, A.M.1    Yavarow, R.C.2    Fry, D.A.3    Vargas, T.4
  • 13
    • 0001662170 scopus 로고
    • Ascorbate free radical reductase, a key enzyme of the ascorbic acid system
    • Arrigoni O., Dipierro S., Borraccino G. Ascorbate free radical reductase, a key enzyme of the ascorbic acid system. FEBS Lett. 125:1981;242-244.
    • (1981) FEBS Lett , vol.125 , pp. 242-244
    • Arrigoni, O.1    Dipierro, S.2    Borraccino, G.3
  • 14
    • 0030009362 scopus 로고    scopus 로고
    • Ascorbate recycling in human erythrocytes: Role of GSH in reducing dehydroascorbate
    • May M.J., Qu Z.C., Whitesell R.R., Cobb C.E. Ascorbate recycling in human erythrocytes role of GSH in reducing dehydroascorbate . Free Radic. Biol. Med. 20:1996;543-551.
    • (1996) Free Radic. Biol. Med. , vol.20 , pp. 543-551
    • May, M.J.1    Qu, Z.C.2    Whitesell, R.R.3    Cobb, C.E.4
  • 15
    • 0029197970 scopus 로고
    • Glutathione: Dehydroascorbate oxide reductases (E.C. 1.8.5.1)
    • Wells W.W., Xu D.P., Washburn M.P. Glutathione dehydroascorbate oxide reductases (E.C. 1.8.5.1) . Methods Enzymol. 252:1995;30-38.
    • (1995) Methods Enzymol , vol.252 , pp. 30-38
    • Wells, W.W.1    Xu, D.P.2    Washburn, M.P.3
  • 17
    • 0026911120 scopus 로고
    • Isolation of plasma membranes from keratinocytes: A newly developed methods allows the sensitive detection of the membrane antigen pattern in normal and psoriatic skin
    • Licht A., Bauer C., Stadler R. Isolation of plasma membranes from keratinocytes a newly developed methods allows the sensitive detection of the membrane antigen pattern in normal and psoriatic skin . Exp. Dermatol. 1:1992;67-75.
    • (1992) Exp. Dermatol. , vol.1 , pp. 67-75
    • Licht, A.1    Bauer, C.2    Stadler, R.3
  • 18
    • 84961031476 scopus 로고
    • Biochemistry of dystrophic muscle
    • Pennington R.J. Biochemistry of dystrophic muscle. Biochem. J. 80:1961;649-654.
    • (1961) Biochem. J. , vol.80 , pp. 649-654
    • Pennington, R.J.1
  • 19
    • 77956985845 scopus 로고
    • DPNH cytochrome c reductase (animal)
    • Mahler H.R. DPNH cytochrome c reductase (animal). Methods Enzymol. 2:1955;688-693.
    • (1955) Methods Enzymol , vol.2 , pp. 688-693
    • Mahler, H.R.1
  • 21
    • 0020626279 scopus 로고
    • A spectrophotometric assay for dehydroascorbate reductase
    • Stahl, R. L.; Liebes, L. F.; Farber, C. M.; Silber, R. A spectrophotometric assay for dehydroascorbate reductase. Anal. Biochem. 131:341-344; 1983.
    • (1983) Anal. Biochem. , vol.131 , pp. 341-344
    • Stahl, R.L.1    Liebes, L.F.2    Farber, C.M.3    Silber, R.4
  • 22
    • 0028151023 scopus 로고
    • Molecular cloning and characterization of cDNA encoding pea Monodehydroascorbate reductase
    • Murthy S.S., Zilinskas A.B. Molecular cloning and characterization of cDNA encoding pea Monodehydroascorbate reductase. J. Biol. Chem. 269:1994;31129-31133.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31129-31133
    • Murthy, S.S.1    Zilinskas, A.B.2
  • 23
    • 2642666080 scopus 로고
    • Cell shape controls terminal differentiation of human epidermal keratinocytes
    • Watt M.F., Jordan P.W., O'Neill C.H. Cell shape controls terminal differentiation of human epidermal keratinocytes. Proc. Natl. Acad. Sci. USA. 85:1988;5576-5580.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5576-5580
    • Watt, M.F.1    Jordan, P.W.2    O'Neill, C.H.3
  • 24
    • 0017184389 scopus 로고
    • Protein determination
    • Bradford S. Protein determination. Anal. Biochem. 72:1976;248-252.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-252
    • Bradford, S.1
  • 25
    • 0030732696 scopus 로고    scopus 로고
    • 2′,7′-Dihydrodichlorofluorescein diacetate as a fluorescent marker for peroxynitrite formation
    • Possel H., Noack H., Augustin W., Keilhoff G., Wolf G. 2′,7′-Dihydrodichlorofluorescein diacetate as a fluorescent marker for peroxynitrite formation. FEBS Lett. 416:1997;175-178.
    • (1997) FEBS Lett , vol.416 , pp. 175-178
    • Possel, H.1    Noack, H.2    Augustin, W.3    Keilhoff, G.4    Wolf, G.5
  • 26
    • 0014912570 scopus 로고
    • Preparation and characterization of Golgi membranes from rat liver
    • Fleischer B., Fleischer S. Preparation and characterization of Golgi membranes from rat liver. Biochim. Biophys. Acta. 219:1970;301-319.
    • (1970) Biochim. Biophys. Acta. , vol.219 , pp. 301-319
    • Fleischer, B.1    Fleischer, S.2
  • 27
    • 0027406835 scopus 로고
    • High-performance liquid chromatographic determination of plasma ascorbic acid in relationship to health care
    • Tanishima K., Kita M. High-performance liquid chromatographic determination of plasma ascorbic acid in relationship to health care. J. Chromatogr. 613:1993;275-280.
    • (1993) J. Chromatogr. , vol.613 , pp. 275-280
    • Tanishima, K.1    Kita, M.2
  • 28
    • 0028837221 scopus 로고
    • The early intracellular production of a reactive oxygen intermediate mediates apoptosis in dexamethasone-treated thymocytes
    • Torres-Roca J.F., Lecoeur H., Amatore C., Gougeon M.L. The early intracellular production of a reactive oxygen intermediate mediates apoptosis in dexamethasone-treated thymocytes. Cell Death Differ. 2:1995;309-319.
    • (1995) Cell Death Differ , vol.2 , pp. 309-319
    • Torres-Roca, J.F.1    Lecoeur, H.2    Amatore, C.3    Gougeon, M.L.4
  • 29
    • 0022372087 scopus 로고
    • Monodehidroascorbate reductase from cucumber is a flavine adenine dinucleotide enzyme
    • Hossain M.A., Asada K. Monodehidroascorbate reductase from cucumber is a flavine adenine dinucleotide enzyme. J. Biol. Chem. 260:1985;12920-12926.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12920-12926
    • Hossain, M.A.1    Asada, K.2
  • 30
    • 0000594637 scopus 로고
    • Purification and properties of ascorbate free-radical reductase from potato tubers
    • Borraccino G., Dipierro S., Arrigoni O. Purification and properties of ascorbate free-radical reductase from potato tubers. Planta. 167:1986;521-526.
    • (1986) Planta , vol.167 , pp. 521-526
    • Borraccino, G.1    Dipierro, S.2    Arrigoni, O.3
  • 31
    • 0026530853 scopus 로고
    • Purification and characterization of monodehydroascorbate reductase from soybean root nodules
    • Dalton D.A., Langeberg L., Robbins M. Purification and characterization of monodehydroascorbate reductase from soybean root nodules. Arch. Biochem. Biophys. 292:1992;281-286.
    • (1992) Arch. Biochem. Biophys. , vol.292 , pp. 281-286
    • Dalton, D.A.1    Langeberg, L.2    Robbins, M.3
  • 32
    • 0015455720 scopus 로고
    • Isolierung und charakterisierung einer NADH: Semidehydroascorbinsaure-oxidoreduktase aus Neurospora crassa
    • Schulze U., Schott H., Staudinger H. Isolierung und charakterisierung einer NADH Semidehydroascorbinsaure-oxidoreduktase aus Neurospora crassa . Hoppe-Seyler's Z. Physiol. Chem. 353:1972;1931-1942.
    • (1972) Hoppe-Seyler's Z. Physiol. Chem. , vol.353 , pp. 1931-1942
    • Schulze, U.1    Schott, H.2    Staudinger, H.3
  • 34
    • 0025947937 scopus 로고
    • Kinetic behaviour of the monodehydroascorbate radical studied by pulse radiolysis
    • Kobayashi K., Harada Y., Hayashi K. Kinetic behaviour of the monodehydroascorbate radical studied by pulse radiolysis. Biochemistry. 30:1991;8310-8315.
    • (1991) Biochemistry , vol.30 , pp. 8310-8315
    • Kobayashi, K.1    Harada, Y.2    Hayashi, K.3
  • 36
    • 0027131323 scopus 로고
    • Monodehydroascorbate reductase activity in the surface membrane of leukemic cells
    • Schweinzer E., Goldenberg H. Monodehydroascorbate reductase activity in the surface membrane of leukemic cells. Eur. J. Biochem. 218:1993;1057-1062.
    • (1993) Eur. J. Biochem. , vol.218 , pp. 1057-1062
    • Schweinzer, E.1    Goldenberg, H.2
  • 39
    • 0032031568 scopus 로고    scopus 로고
    • Absorption, transport, and disposition of ascorbic acid in humans
    • Rumsey S.C., Levine M. Absorption, transport, and disposition of ascorbic acid in humans. Nutr. Biochem. 9:1998;116-130.
    • (1998) Nutr. Biochem. , vol.9 , pp. 116-130
    • Rumsey, S.C.1    Levine, M.2
  • 40
    • 0029945450 scopus 로고    scopus 로고
    • Synthesis of novel vitamin C phosphodiesters: Stability and antioxidant activity
    • Morisaki K., Ozaki S. Synthesis of novel vitamin C phosphodiesters stability and antioxidant activity . Carbohyd. Res. 289:1996;123-138.
    • (1996) Carbohyd. Res. , vol.289 , pp. 123-138
    • Morisaki, K.1    Ozaki, S.2
  • 41
    • 0027029575 scopus 로고
    • Increase in the activity of alkaline phosphatase by L-ascorbic acid 2-phosphate in a human osteoblast cell line, HuO-3N1
    • Hitomi K., Torii Y., Tsukagoshi N. Increase in the activity of alkaline phosphatase by L-ascorbic acid 2-phosphate in a human osteoblast cell line, HuO-3N1. J. Nutr. Sci. Vitaminol. 38:1992;535-544.
    • (1992) J. Nutr. Sci. Vitaminol. , vol.38 , pp. 535-544
    • Hitomi, K.1    Torii, Y.2    Tsukagoshi, N.3
  • 42
    • 15044356704 scopus 로고
    • Friedrich, L. Ascorbic acid derivatives increase collagen synthesis by living dermal equivalents
    • Green G.D., Muthukumaran N., Kemp P.D. Friedrich, L. Ascorbic acid derivatives increase collagen synthesis by living dermal equivalents. J. Cell. Biol. 111:1990;21a.
    • (1990) J. Cell. Biol. , vol.111
    • Green, G.D.1    Muthukumaran, N.2    Kemp, P.D.3
  • 43
    • 0024557841 scopus 로고
    • L-Ascorbic acid 2-phosphate stimulates collagen accumulation, cell proliferation, and formation of a three-dimensional tissue-like substance by skin fibroblasts
    • Hata, R. I.; Senoo, H. L-Ascorbic acid 2-phosphate stimulates collagen accumulation, cell proliferation, and formation of a three-dimensional tissue-like substance by skin fibroblasts. J. Cell. Physiol. 138:8-16; 1989.
    • (1989) J. Cell. Physiol. , vol.138 , pp. 8-16
    • Hata, R.I.1    Senoo, H.2
  • 44
    • 0029552921 scopus 로고
    • Differential susceptibility of epidermal keratinocytes and neuroblastoma cells to cytotoxicity of ultraviolet-B light irradiation prevented by the oxygen radical-scavenger ascorbate 2-phosphate but not by ascorbate
    • Kanatate T., Nagao N., Sugimoto M., Kageyama K., Fujimoto T., Miwa N. Differential susceptibility of epidermal keratinocytes and neuroblastoma cells to cytotoxicity of ultraviolet-B light irradiation prevented by the oxygen radical-scavenger ascorbate 2-phosphate but not by ascorbate. Cell. Mol. Biol. Res. 41:1995;561-567.
    • (1995) Cell. Mol. Biol. Res. , vol.41 , pp. 561-567
    • Kanatate, T.1    Nagao, N.2    Sugimoto, M.3    Kageyama, K.4    Fujimoto, T.5    Miwa, N.6
  • 45
    • 0028105617 scopus 로고
    • Apoptosis, the skin from a new perspective
    • Polakowska R.R., Haake A.R. Apoptosis, the skin from a new perspective. Cell Death Differ. 1:1994;19-31.
    • (1994) Cell Death Differ , vol.1 , pp. 19-31
    • Polakowska, R.R.1    Haake, A.R.2


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