메뉴 건너뛰기




Volumn 66, Issue 6, 1998, Pages 687-697

The effect of ascorbic acid and ferric ammonium citrate on iron uptake and storage in lens epithelial cells

Author keywords

Ascorbic acid; Ferric ammonium citrate; Ferritin; Iron; Lens; Transferrin

Indexed keywords

ASCORBIC ACID; FERRIC AMMONIUM CITRATE; FERRIC CHLORIDE; FERRITIN; IRON;

EID: 0032100224     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1997.0466     Document Type: Article
Times cited : (23)

References (48)
  • 1
    • 0028247159 scopus 로고
    • Ascorbic acid-mediated iron release from cellular ferritin and its relation to the formation of DNA strand breaks in neuroblastoma cells
    • Baader S. L., Bruchelt G., Carmine T. C., Lode H. N., Rieth A. G., Niethammer D. Ascorbic acid-mediated iron release from cellular ferritin and its relation to the formation of DNA strand breaks in neuroblastoma cells. J. Cancer Res. Clin. Oncol. 120:1994;415-421.
    • (1994) J. Cancer Res. Clin. Oncol. , vol.120 , pp. 415-421
    • Baader, S.L.1    Bruchelt, G.2    Carmine, T.C.3    Lode, H.N.4    Rieth, A.G.5    Niethammer, D.6
  • 2
    • 0030032753 scopus 로고    scopus 로고
    • Mobilization of iron from cellular ferritin by ascorbic acid in neuroblastoma SK-N-SH cells: An EPR study
    • Baader S. L., Bill E., Trautwein A. X., Bruchelt G., Matzanke B. F. Mobilization of iron from cellular ferritin by ascorbic acid in neuroblastoma SK-N-SH cells: an EPR study. FEBS Lett. 381:1996;131-134.
    • (1996) FEBS Lett. , vol.381 , pp. 131-134
    • Baader, S.L.1    Bill, E.2    Trautwein, A.X.3    Bruchelt, G.4    Matzanke, B.F.5
  • 4
    • 0010243026 scopus 로고
    • The kinetics and mechanism of iron (III) exchange between chelates and transferrin. IV. The reaction of transferrin with iron (III) nitrilotriacetate
    • Bates G. W., Wernicke J. The kinetics and mechanism of iron (III) exchange between chelates and transferrin. IV. The reaction of transferrin with iron (III) nitrilotriacetate. J. Biol. Chem. 246:1971;444-446.
    • (1971) J. Biol. Chem. , vol.246 , pp. 444-446
    • Bates, G.W.1    Wernicke, J.2
  • 6
    • 0018959185 scopus 로고
    • Rapid mobilization of ferritin iron by ascorbate in the presence of oxygen
    • Bienfait H. F., van den Briel M. L. Rapid mobilization of ferritin iron by ascorbate in the presence of oxygen. Biochim. Biophys. Acta. 631:1980;507-510.
    • (1980) Biochim. Biophys. Acta. , vol.631 , pp. 507-510
    • Bienfait, H.F.1    Van Den Briel, M.L.2
  • 7
    • 0027406739 scopus 로고
    • Decay of superoxide catalysed by ferritin
    • Bolann B. J., Ulvik R. J. Decay of superoxide catalysed by ferritin. FEBS Lett. 318:1993;149-152.
    • (1993) FEBS Lett. , vol.318 , pp. 149-152
    • Bolann, B.J.1    Ulvik, R.J.2
  • 8
    • 0022256894 scopus 로고
    • Iron metabolism in K562 erythroleukemic cells
    • Bottomley S. S., Wolfe L. C., Bridges K. R. Iron metabolism in K562 erythroleukemic cells. J. Biol. Chem. 260:1985;6811-6815.
    • (1985) J. Biol. Chem. , vol.260 , pp. 6811-6815
    • Bottomley, S.S.1    Wolfe, L.C.2    Bridges, K.R.3
  • 9
    • 0023162026 scopus 로고
    • Ascorbic acid inhibits lysosomal autophagy of ferritin
    • Bridges K. R. Ascorbic acid inhibits lysosomal autophagy of ferritin. J. Biol. Chem. 262:1987;14773-14778.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14773-14778
    • Bridges, K.R.1
  • 10
    • 0022973969 scopus 로고
    • The effects of ascorbic acid on the intracellular metabolism of iron and ferritin
    • Bridges K. R., Hoffman K. E. The effects of ascorbic acid on the intracellular metabolism of iron and ferritin. J. Biol. Chem. 261:1986;14273-14277.
    • (1986) J. Biol. Chem. , vol.261 , pp. 14273-14277
    • Bridges, K.R.1    Hoffman, K.E.2
  • 11
    • 0030811101 scopus 로고    scopus 로고
    • Hereditary hyperferritinemia-cataract syndrome: Relationship between phenotypes and specific mutations in the iron-responsive element of ferritin light-chain mRNA
    • Cazzola M., Bergamaschi G., Tonon L., Arbustini E., Grasso M., Vercesi E., Barosi G., Bianchi P. E., Cairo G., Arosio P. Hereditary hyperferritinemia-cataract syndrome: relationship between phenotypes and specific mutations in the iron-responsive element of ferritin light-chain mRNA. Blood. 90:1997;814-821.
    • (1997) Blood , vol.90 , pp. 814-821
    • Cazzola, M.1    Bergamaschi, G.2    Tonon, L.3    Arbustini, E.4    Grasso, M.5    Vercesi, E.6    Barosi, G.7    Bianchi, P.E.8    Cairo, G.9    Arosio, P.10
  • 13
    • 0025612310 scopus 로고
    • Iron detoxifying activity of ferritin. Effects of H and L human apoferritins on lipid peroxidation in vitro
    • Cozzi A., Santambrogio P., Levi S., Arosio P. Iron detoxifying activity of ferritin. Effects of H and L human apoferritins on lipid peroxidation in vitro. FEBS. 277:1990;119-122.
    • (1990) FEBS , vol.277 , pp. 119-122
    • Cozzi, A.1    Santambrogio, P.2    Levi, S.3    Arosio, P.4
  • 15
    • 0025365741 scopus 로고
    • Role of site-specific, metal-catalyzed oxidation in lens aging and cataract: A hypothesis
    • Garland D. Role of site-specific, metal-catalyzed oxidation in lens aging and cataract: a hypothesis. Exp. Eye Res. 50:1990;677-682.
    • (1990) Exp. Eye Res. , vol.50 , pp. 677-682
    • Garland, D.1
  • 16
    • 0022860324 scopus 로고
    • Structural changes in bovine lens crystallins induced by ascorbate, metal and oxygen
    • Garland D., Zigler J. S Jr, Kinoshita J. Structural changes in bovine lens crystallins induced by ascorbate, metal and oxygen. Arch. Biochem. Biophys. 251:1986;771-776.
    • (1986) Arch. Biochem. Biophys. , vol.251 , pp. 771-776
    • Garland, D.1    Zigler J.S., Jr.2    Kinoshita, J.3
  • 17
    • 0028788201 scopus 로고
    • Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: A mutation in the iron-responsive element of ferritinL
    • Girelli D., Corrocher R., Bisceglia L., Olivieri O., De Franceschi L., Zelante L., Gasparini P. Molecular basis for the recently described hereditary hyperferritinemia-cataract syndrome: a mutation in the iron-responsive element of ferritinL. Blood. 86:1995;4050-4053.
    • (1995) Blood , vol.86 , pp. 4050-4053
    • Girelli, D.1    Corrocher, R.2    Bisceglia, L.3    Olivieri, O.4    De Franceschi, L.5    Zelante, L.6    Gasparini, P.7
  • 18
    • 0030921671 scopus 로고    scopus 로고
    • Hereditary hyperferritinemia-cataract syndrome caused by a 29 bp deletion in the iron responsive element of ferritinL
    • Girelli D., Corrocher R., Bisceglia L., Olivieri O., Zelante L., Panozzo G., Gasparini P. Hereditary hyperferritinemia-cataract syndrome caused by a 29 bp deletion in the iron responsive element of ferritinL. Blood. 90:1997;2084-2088.
    • (1997) Blood , vol.90 , pp. 2084-2088
    • Girelli, D.1    Corrocher, R.2    Bisceglia, L.3    Olivieri, O.4    Zelante, L.5    Panozzo, G.6    Gasparini, P.7
  • 19
    • 0031105416 scopus 로고    scopus 로고
    • Mechanisms by which ascorbic acid increases ferritin levels in cultured lens epithelial cells
    • Goralska M., Harned J., Grimes A. M., Fleisher L. N., McGahan M. C. Mechanisms by which ascorbic acid increases ferritin levels in cultured lens epithelial cells. Exp. Eye Res. 64:1997;413-421.
    • (1997) Exp. Eye Res. , vol.64 , pp. 413-421
    • Goralska, M.1    Harned, J.2    Grimes, A.M.3    Fleisher, L.N.4    McGahan, M.C.5
  • 20
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: Molecular properties, iron storage function and cellular regulation
    • Harrison P. M., Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochim. Biophys. Acta. 1275:1996;161-203.
    • (1996) Biochim. Biophys. Acta. , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 21
    • 0029758487 scopus 로고    scopus 로고
    • Molecular control of vertebrate iron metabolism: MRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress
    • Hentze M. W., Kuhn L. C. Molecular control of vertebrate iron metabolism: mRNA-based regulatory circuits operated by iron, nitric oxide and oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 93:1996;8175-8182.
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 8175-8182
    • Hentze, M.W.1    Kuhn, L.C.2
  • 23
    • 0025774978 scopus 로고
    • Regulation of the transferrin-independent iron system in cultured cells
    • Kaplan J., Jordan I., Sturrock A. Regulation of the transferrin-independent iron system in cultured cells. J. Biol. Chem. 266:1991;2997-3004.
    • (1991) J. Biol. Chem. , vol.266 , pp. 2997-3004
    • Kaplan, J.1    Jordan, I.2    Sturrock, A.3
  • 25
    • 0025298553 scopus 로고
    • Photoreduction and incorporation of iron into ferritins
    • Laulhere J.-P., Laboure A.-M., Briat J.-F. Photoreduction and incorporation of iron into ferritins. Biochem. J. 269:1990;79-84.
    • (1990) Biochem. J. , vol.269 , pp. 79-84
    • Laulhere, J.-P.1    Laboure, A.-M.2    Briat, J.-F.3
  • 26
    • 0019837628 scopus 로고
    • Iron uptake by rabbit intestinal mucosal membrane vesicles
    • Marx J. J. M., Aisen P. Iron uptake by rabbit intestinal mucosal membrane vesicles. Biochim. Biophys. Acta. 649:1981;297-304.
    • (1981) Biochim. Biophys. Acta. , vol.649 , pp. 297-304
    • Marx, J.J.M.1    Aisen, P.2
  • 27
    • 0023902907 scopus 로고
    • Inflammation-induced changes in the iron concentration and total iron-binding capacity of the intraocular fluids of rabbits
    • McGahan M. C., Fleisher L. N. Inflammation-induced changes in the iron concentration and total iron-binding capacity of the intraocular fluids of rabbits. Graefe's Arch. Clin. Exp. Ophthalmol. 226:1988;27-30.
    • (1988) Graefe's Arch. Clin. Exp. Ophthalmol. , vol.226 , pp. 27-30
    • McGahan, M.C.1    Fleisher, L.N.2
  • 28
    • 0028035109 scopus 로고
    • Regulation of ferritin levels in cultured lens epithelial cells
    • McGahan M. C., Harned J., Grimes A. M., Fleisher L. N. Regulation of ferritin levels in cultured lens epithelial cells. Exp. Eye Res. 59:1994;551-556.
    • (1994) Exp. Eye Res. , vol.59 , pp. 551-556
    • McGahan, M.C.1    Harned, J.2    Grimes, A.M.3    Fleisher, L.N.4
  • 32
    • 0023694365 scopus 로고
    • Membrane transport of non-transferrin-bound iron by reticulocytes
    • Morgan E. H. Membrane transport of non-transferrin-bound iron by reticulocytes. Biochim. Biophys. Acta. 943:1988;428-439.
    • (1988) Biochim. Biophys. Acta. , vol.943 , pp. 428-439
    • Morgan, E.H.1
  • 33
    • 0022332414 scopus 로고
    • Preventive effect of ascorbic acid against glucocorticoid-induced cataract formation of developing chick embryos
    • Nishigori H., Hayashi R., Lee J. W., Maruyama K., Iwatsuru M. Preventive effect of ascorbic acid against glucocorticoid-induced cataract formation of developing chick embryos. Exp. Eye Res. 40:1985;445-451.
    • (1985) Exp. Eye Res. , vol.40 , pp. 445-451
    • Nishigori, H.1    Hayashi, R.2    Lee, J.W.3    Maruyama, K.4    Iwatsuru, M.5
  • 35
    • 0026516293 scopus 로고
    • Changes in the uptake of transferrin-free and transferrin-bound iron during reticulocyte maturation in vivo and in vitro
    • Qian Z. M., Morgan E. H. Changes in the uptake of transferrin-free and transferrin-bound iron during reticulocyte maturation in vivo and in vitro. Biochim. Biophys. Acta. 1135:1992;35-43.
    • (1992) Biochim. Biophys. Acta. , vol.1135 , pp. 35-43
    • Qian, Z.M.1    Morgan, E.H.2
  • 37
    • 0019570250 scopus 로고
    • Role of glycosylation and protein synthesis in insulin receptor metabolism by 3T3-L1 mouse adipocytes
    • Reed B. C., Ronnett G. V., Lane M. D. Role of glycosylation and protein synthesis in insulin receptor metabolism by 3T3-L1 mouse adipocytes. Proc. Natl. Acad. Sci. U.S.A. 78:1981;2908-2912.
    • (1981) Proc. Natl. Acad. Sci. U.S.A. , vol.78 , pp. 2908-2912
    • Reed, B.C.1    Ronnett, G.V.2    Lane, M.D.3
  • 38
    • 0028875152 scopus 로고
    • Identification of a mechanism of iron uptake by cells which is stimulated by hydroxyl radicals generated via the iron-catalysed Haber-Weiss reaction
    • Richardson D. R., Ponka P. Identification of a mechanism of iron uptake by cells which is stimulated by hydroxyl radicals generated via the iron-catalysed Haber-Weiss reaction. Biochim. Biophys. Acta. 1269:1995;105-114.
    • (1995) Biochim. Biophys. Acta. , vol.1269 , pp. 105-114
    • Richardson, D.R.1    Ponka, P.2
  • 40
    • 0029151027 scopus 로고
    • Oxidative stress-induced cataract: Mechanism of action
    • Spector A. Oxidative stress-induced cataract: mechanism of action. FASEB J. 9:1995;1173-1182.
    • (1995) FASEB J. , vol.9 , pp. 1173-1182
    • Spector, A.1
  • 41
    • 0028879018 scopus 로고
    • Relations among aging, antioxidant status and cataract
    • Taylor, A., Jacques, P. F. and Epstein, E. M. (1995). Relations among aging, antioxidant status and cataract. Am. J. Clin. Nutr. 62, 1439S-47.
    • (1995) Am. J. Clin. Nutr. , vol.62
    • Taylor, A.1    Jacques, P.F.2    Epstein, E.M.3
  • 42
    • 0023949731 scopus 로고
    • Uptake of Fe from transferrin by isolated hepatocytes. A redox-mediated plasma membrane process
    • Thorstensen, K. and Romslo, I. (1990). Uptake of Fe from transferrin by isolated hepatocytes. A redox-mediated plasma membrane process. J. Biol. Chem. 263, 8844- 50.
    • (1990) J. Biol. Chem. , vol.263 , pp. 8844-8850
    • Thorstensen, K.1    Romslo, I.2
  • 43
    • 0020037206 scopus 로고
    • Photoperoxidation in lens and cataract formation: Preventive role of superoxide dismutase, catalase and vitamin C
    • Varma S. D., Srivastava V. K., Richards R. D. Photoperoxidation in lens and cataract formation: preventive role of superoxide dismutase, catalase and vitamin C. Ophthal. Res. 14:1982;167-175.
    • (1982) Ophthal. Res. , vol.14 , pp. 167-175
    • Varma, S.D.1    Srivastava, V.K.2    Richards, R.D.3
  • 44
    • 0026752331 scopus 로고
    • Desferoxamine effect on selenite-induced cataract formation in rats
    • Wang Z., Hess J. L., Bunce G. E. Desferoxamine effect on selenite-induced cataract formation in rats. Invest. Ophthalmol. Vis. Sci. 33:1992;2511-2519.
    • (1992) Invest. Ophthalmol. Vis. Sci. , vol.33 , pp. 2511-2519
    • Wang, Z.1    Hess, J.L.2    Bunce, G.E.3
  • 45
    • 0345349786 scopus 로고
    • Morphologic characterization of the pathway of transferrin endocytosis and recycling in human KB cells
    • Willingham M. C., Hanover J. A., Pastan I. Morphologic characterization of the pathway of transferrin endocytosis and recycling in human KB cells. Proc. Natl. Acad. Sic. U.S.A. 81:1984;175-179.
    • (1984) Proc. Natl. Acad. Sic. U.S.A. , vol.81 , pp. 175-179
    • Willingham, M.C.1    Hanover, J.A.2    Pastan, I.3
  • 46
    • 0028289072 scopus 로고
    • A physiological level of ascorbate inhibits galactose cataract in guinea pigs by decreasing polyol accumulation in the lens epithelium: A dehydroascorbate-linked mechanism
    • Yokoyama T., Sasaki H., Giblin F., Reddy V. A physiological level of ascorbate inhibits galactose cataract in guinea pigs by decreasing polyol accumulation in the lens epithelium: a dehydroascorbate-linked mechanism. Exp. Eye Res. 58:1994;207-218.
    • (1994) Exp. Eye Res. , vol.58 , pp. 207-218
    • Yokoyama, T.1    Sasaki, H.2    Giblin, F.3    Reddy, V.4
  • 47
    • 0022338318 scopus 로고
    • Cataracts in the Royal College of Surgeons rat: Evidence for initiation by lipid peroxidation products
    • Zigler J. S., Hess H. H. Cataracts in the Royal College of Surgeons rat: evidence for initiation by lipid peroxidation products. Exp. Eye Res. 41:1985;67-76.
    • (1985) Exp. Eye Res. , vol.41 , pp. 67-76
    • Zigler, J.S.1    Hess, H.H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.