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Volumn 33, Issue 4, 2003, Pages 257-266

Intracellular Ca2+ regulates the cellular iron uptake in K562 cells

Author keywords

Actin polymerization; Endocytosis; Intracellular calcium; Iron uptake; Recycling; Transferrin receptor

Indexed keywords

2 [1 (3 DIMETHYLAMINOPROPYL) 3 INDOLYL] 3 (3 INDOLYL)MALEIMIDE; ACTIN; CALCIUM ION; CALMODULIN INHIBITOR; ENZYME ACTIVATOR; IRON; N (6 AMINOHEXYL) 5 CHLORO 1 NAPHTHALENESULFONAMIDE; PHORBOL 13 ACETATE 12 MYRISTATE; PROTEIN KINASE C; PROTEIN KINASE C INHIBITOR; THAPSIGARGIN; TRANSFERRIN RECEPTOR;

EID: 0037379003     PISSN: 01434160     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0143-4160(02)00240-3     Document Type: Review
Times cited : (21)

References (38)
  • 1
    • 0021259518 scopus 로고
    • Desferoxamine: A reversible S-phase inhibitor of human lymphocyte proliferation
    • H.M. Lederman, A. Cohen, J.W. Lee, M.H. Freedman, E.W. Gelfand, Desferoxamine: a reversible S-phase inhibitor of human lymphocyte proliferation, Blood 64 (1980) 748-753.
    • (1980) Blood , vol.64 , pp. 748-753
    • Lederman, H.M.1    Cohen, A.2    Lee, J.W.3    Freedman, M.H.4    Gelfand, E.W.5
  • 2
    • 0000622023 scopus 로고
    • Iron-transferrin requirements and transferrin receptor expression in proliferating cell
    • CRC Press, Boca Raton, FL
    • L.C. Kühn, H.M. Schulman, P. Ponka, Iron-transferrin requirements and transferrin receptor expression in proliferating cell, in: Iron Transport and Storage, CRC Press, Boca Raton, FL, 1990, pp. 149-191.
    • (1990) Iron Transport and Storage , pp. 149-191
    • Kühn, L.C.1    Schulman, H.M.2    Ponka, P.3
  • 3
    • 0021298328 scopus 로고
    • The activity of tissue enzymes in iron-deficient rat and man: An overview
    • P. Galan, S. Hercberg, Y. Touitou, The activity of tissue enzymes in iron-deficient rat and man: an overview, Comp. Biochem. Physiol. B 77 (1984) 647-653.
    • (1984) Comp. Biochem. Physiol. B , vol.77 , pp. 647-653
    • Galan, P.1    Hercberg, S.2    Touitou, Y.3
  • 4
    • 0025126555 scopus 로고
    • Role of free radicals and catalytic metal ions in human diseases: An overview
    • B. Halliwell, J.M.C. Gutteridge, Role of free radicals and catalytic metal ions in human diseases: an overview, Methods Enzymol. 186 (1990) 1-85.
    • (1990) Methods Enzymol. , vol.186 , pp. 1-85
    • Halliwell, B.1    Gutteridge, J.M.C.2
  • 6
    • 0032975570 scopus 로고    scopus 로고
    • The role of iron in neurodegeneration
    • K.A. Jellinger, The role of iron in neurodegeneration, Drugs Aging 14 (1999) 115-140.
    • (1999) Drugs Aging , vol.14 , pp. 115-140
    • Jellinger, K.A.1
  • 7
    • 0010487727 scopus 로고    scopus 로고
    • Expression of iron transport proteins and excessive iron accumulation of iron in the brain in neurodegenerative disorders
    • Z.M. Qian, Q. Wang, Expression of iron transport proteins and excessive iron accumulation of iron in the brain in neurodegenerative disorders, Brain Res. Rev. 27 (1998) 257-267.
    • (1998) Brain Res. Rev. , vol.27 , pp. 257-267
    • Qian, Z.M.1    Wang, Q.2
  • 8
    • 0026317374 scopus 로고
    • Hallervorden-Spatz and brain iron metabolism
    • K.F. Swaiman, Hallervorden-Spatz and brain iron metabolism, Arch. Neurol. 48 (1991) 1285-1293.
    • (1991) Arch. Neurol. , vol.48 , pp. 1285-1293
    • Swaiman, K.F.1
  • 9
    • 0030058299 scopus 로고    scopus 로고
    • Molecular mechanisms of iron uptake in eukaryotes
    • D.M.D. Silva, C. Askwith, J. Kaplan, Molecular mechanisms of iron uptake in eukaryotes, Physiol. Rev. 76 (1996) 31-47.
    • (1996) Physiol. Rev. , vol.76 , pp. 31-47
    • Silva, D.M.D.1    Askwith, C.2    Kaplan, J.3
  • 10
    • 0028832288 scopus 로고
    • Mechanism of iron uptake by mammalian cells
    • Z.M. Qian, P.L. Tang, Mechanism of iron uptake by mammalian cells, Biochim. Biophys. Acta 1269 (1995) 205-214.
    • (1995) Biochim. Biophys. Acta , vol.1269 , pp. 205-214
    • Qian, Z.M.1    Tang, P.L.2
  • 11
    • 0031018874 scopus 로고    scopus 로고
    • Regulation of cellular iron metabolism by erythropoietin: Activation of iron-regulatory protein and up regulation of transferrin receptor expression in erythroid cells
    • G. Weiss, T. Houston, S. Kastner, K. Johrer, K. Grunewald, J.H. Brock, Regulation of cellular iron metabolism by erythropoietin: activation of iron-regulatory protein and up regulation of transferrin receptor expression in erythroid cells, Blood 89 (1997) 680-687.
    • (1997) Blood , vol.89 , pp. 680-687
    • Weiss, G.1    Houston, T.2    Kastner, S.3    Johrer, K.4    Grunewald, K.5    Brock, J.H.6
  • 12
    • 0029034338 scopus 로고
    • Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels
    • B. Guo, F.M. Brown, J.D. Phillips, Y. Yu, E.A. Leibold, Characterization and expression of iron regulatory protein 2 (IRP2). Presence of multiple IRP2 transcripts regulated by intracellular iron levels, J. Biol. Chem. 270 (1995) 16529-16535.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16529-16535
    • Guo, B.1    Brown, F.M.2    Phillips, J.D.3    Yu, Y.4    Leibold, E.A.5
  • 13
    • 0034644715 scopus 로고    scopus 로고
    • Thyrotropin-releasing hormone and epidermal growth factor regulate iron-regulatory protein binding in pituitary cells via protein kinase C-dependent and-independent signaling pathways
    • A.M. Thomson, J.T. Rogers, P.J. Leedman, Thyrotropin-releasing hormone and epidermal growth factor regulate iron-regulatory protein binding in pituitary cells via protein kinase C-dependent and-independent signaling pathways, J. Biol. Chem. 275 (2000) 31609-31615.
    • (2000) J. Biol. Chem. , vol.275 , pp. 31609-31615
    • Thomson, A.M.1    Rogers, J.T.2    Leedman, P.J.3
  • 15
    • 0026472376 scopus 로고
    • Iron metabolism-new perspectives in view
    • R.R. Crichton, R.J. Ward, Iron metabolism-new perspectives in view, Biochemistry 31 (1992) 11255-11264.
    • (1992) Biochemistry , vol.31 , pp. 11255-11264
    • Crichton, R.R.1    Ward, R.J.2
  • 16
    • 0026569505 scopus 로고
    • Receptor-mediated iron uptake and intracellular iron transport
    • S. Pollack, Receptor-mediated iron uptake and intracellular iron transport, Am. J. Hematol. 39 (1992) 113-118.
    • (1992) Am. J. Hematol. , vol.39 , pp. 113-118
    • Pollack, S.1
  • 17
    • 0027080934 scopus 로고
    • Cellular pool of transient ferric iron, chelatable by desferoxamine and distinct from ferritin
    • R.J. Rothman, A. Serroni, J.H. Farer, Cellular pool of transient ferric iron, chelatable by desferoxamine and distinct from ferritin, Mol. Pharmacol. 42 (1992) 703-710.
    • (1992) Mol. Pharmacol. , vol.42 , pp. 703-710
    • Rothman, R.J.1    Serroni, A.2    Farer, J.H.3
  • 18
    • 0028834446 scopus 로고
    • Iron acquired from transferrin by k562 cells is delivered into a cytoplasmic pool of chelatable iron(II)
    • W. Breuer, S. Epsztezn, Z.I. Cabantchik, Iron acquired from transferrin by k562 cells is delivered into a cytoplasmic pool of chelatable iron(II), J. Biol. Chem. 70 (1995) 24209-24215.
    • (1995) J. Biol. Chem. , vol.70 , pp. 24209-24215
    • Breuer, W.1    Epsztezn, S.2    Cabantchik, Z.I.3
  • 19
    • 0023095571 scopus 로고
    • The calcium mobilizing and tumor-promoting agent, thapsigargin elevates the platelet cytoplasmic free calcium concentration to a higher steady state level. A possible mechanism of action for the tumor promotion
    • O. Thastrup, B. Foder, O. Scharff, The calcium mobilizing and tumor-promoting agent, thapsigargin elevates the platelet cytoplasmic free calcium concentration to a higher steady state level. A possible mechanism of action for the tumor promotion, Biochem. Biophys. Res. Commun. 142 (1987) 654-660.
    • (1987) Biochem. Biophys. Res. Commun. , vol.142 , pp. 654-660
    • Thastrup, O.1    Foder, B.2    Scharff, O.3
  • 21
    • 0028912190 scopus 로고
    • A fluorescent probe study of plasminogen activator inhibitor-1: Evidence for reactive center loop insertion and its role in the inhibitory mechanism
    • J.D. Shore, D.E. Day, A.M. Francis-Chmura, I. Verhamme, J. Kvassman, D.A. Lawrence, D. Ginsburg, A fluorescent probe study of plasminogen activator inhibitor-1: evidence for reactive center loop insertion and its role in the inhibitory mechanism, J. Biol. Chem. 270 (1995) 5395-5398.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5395-5398
    • Shore, J.D.1    Day, D.E.2    Francis-Chmura, A.M.3    Verhamme, I.4    Kvassman, J.5    Lawrence, D.A.6    Ginsburg, D.7
  • 22
    • 0021998316 scopus 로고
    • 2+ in individual small cells using fluorescence microscopy with dual excitation wavelengths
    • 2+ in individual small cells using fluorescence microscopy with dual excitation wavelengths, Cell Calcium 6 (1985) 145-157.
    • (1985) Cell Calcium , vol.6 , pp. 145-157
    • Tsien, R.Y.1    Rink, T.J.2    Poenie, M.3
  • 23
    • 0028985124 scopus 로고
    • Shape oscillations: A fundamental response of human neutrophils stimulated by chemotactic peptides?
    • M.U. Ehrengruber, T.D. Coates, D.A. Deranleau, Shape oscillations: a fundamental response of human neutrophils stimulated by chemotactic peptides? FEBS Lett. 359 (1995) 229-232.
    • (1995) FEBS Lett. , vol.359 , pp. 229-232
    • Ehrengruber, M.U.1    Coates, T.D.2    Deranleau, D.A.3
  • 24
    • 0018906488 scopus 로고
    • Calcium-regulated modulator protein interacting agents inhibit smooth muscle calcium-stimulated protein kinase and ATPase
    • H. Hidaka, T. Yamaki, M. Naka, T. Tanaka, H. Hayashi, R. Kobayashi, Calcium-regulated modulator protein interacting agents inhibit smooth muscle calcium-stimulated protein kinase and ATPase, Mol. Pharmacol. 17 (1980) 66-72.
    • (1980) Mol. Pharmacol. , vol.17 , pp. 66-72
    • Hidaka, H.1    Yamaki, T.2    Naka, M.3    Tanaka, T.4    Hayashi, H.5    Kobayashi, R.6
  • 25
    • 0030025794 scopus 로고    scopus 로고
    • Augmentation by calmodulin of ADP ribosylation factor-stimulated phospholipase D activity in permeabilized rabbit peritoneal neutrophils
    • K. Takahashi, K. Tago, H. Okano, Y. Ohya, T. Katada, Y. Kanaho, Augmentation by calmodulin of ADP ribosylation factor-stimulated phospholipase D activity in permeabilized rabbit peritoneal neutrophils, J. Immunol. 156 (1996) 1229-1234.
    • (1996) J. Immunol. , vol.156 , pp. 1229-1234
    • Takahashi, K.1    Tago, K.2    Okano, H.3    Ohya, Y.4    Katada, T.5    Kanaho, Y.6
  • 26
    • 0031002365 scopus 로고    scopus 로고
    • Effects of calmodulin antagonists on calcium pump and cytosolic calcium level in human neutrophils
    • 1357
    • E. Capuozzo, D. Verginelli, C. Crifo, C. Salerno, Effects of calmodulin antagonists on calcium pump and cytosolic calcium level in human neutrophils, Biochim. Biophys. Acta 1357 (1997) 124-127.
    • (1997) Biochim. Biophys. Acta , pp. 124-127
    • Capuozzo, E.1    Verginelli, D.2    Crifo, C.3    Salerno, C.4
  • 27
    • 0032705583 scopus 로고    scopus 로고
    • The protein kinase C inhibitors bisindolylmaleimide I (GF 109203x) and IX (Ro 31-8220) are potent inhibitors of glycogen synthase kinase-3 activity
    • I. Hers, J.M. Tavare, R.M. Denton, The protein kinase C inhibitors bisindolylmaleimide I (GF 109203x) and IX (Ro 31-8220) are potent inhibitors of glycogen synthase kinase-3 activity, FEBS Lett. 460 (1999) 433-436.
    • (1999) FEBS Lett. , vol.460 , pp. 433-436
    • Hers, I.1    Tavare, J.M.2    Denton, R.M.3
  • 28
    • 0036124412 scopus 로고    scopus 로고
    • Effects of reactive oxygen species on actin filament polymerization and amylase secretion in mouse pancreatic acinar cells
    • J.A. Rosado, A. Gonzalez, G.M. Salido, J.A. Pariente, Effects of reactive oxygen species on actin filament polymerization and amylase secretion in mouse pancreatic acinar cells, Cell Signal. 14 (2002) 547-556.
    • (2002) Cell Signal. , vol.14 , pp. 547-556
    • Rosado, J.A.1    Gonzalez, A.2    Salido, G.M.3    Pariente, J.A.4
  • 29
    • 0035971163 scopus 로고    scopus 로고
    • Receptor and membrane recycling can occur with unaltered efficiency despite dramatic Rab5 (Q79L)-induced changes in endosome geometry
    • B.P. Ceresa, M. Lotscher, S.L. Schmid, Receptor and membrane recycling can occur with unaltered efficiency despite dramatic Rab5 (Q79L)-induced changes in endosome geometry, J. Biol. Chem. 276 (2001) 9649-9654.
    • (2001) J. Biol. Chem. , vol.276 , pp. 9649-9654
    • Ceresa, B.P.1    Lotscher, M.2    Schmid, S.L.3
  • 30
    • 0034054183 scopus 로고    scopus 로고
    • The role of the membrane-bound tumor antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell
    • D.R. Richardson, The role of the membrane-bound tumor antigen, melanotransferrin (p97), in iron uptake by the human malignant melanoma cell, Eur. J. Biochem. 267 (2000) 1290-1298.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 1290-1298
    • Richardson, D.R.1
  • 31
    • 0032007849 scopus 로고    scopus 로고
    • Binding of iron and inhibition of iron-dependent oxidative cell injury by the calcium chelator 1,2-bis(2-aminophenoxy) ethane N,N,N′,N′-tetraacitic acid (BAPTA)
    • B.E. Britigan, G.T. Rasmussen, C.D. Cox, Binding of iron and inhibition of iron-dependent oxidative cell injury by the calcium chelator 1,2-bis(2-aminophenoxy) ethane N,N,N′,N′-tetraacitic acid (BAPTA), Biochem. Pharmacol. 55 (1998) 287-295.
    • (1998) Biochem. Pharmacol. , vol.55 , pp. 287-295
    • Britigan, B.E.1    Rasmussen, G.T.2    Cox, C.D.3
  • 32
    • 0035806991 scopus 로고    scopus 로고
    • Cytoskeleton: Actin and endocytosis - No longer the weakest link
    • R.L. Jeng, M.D. Welch, Cytoskeleton: actin and endocytosis - no longer the weakest link, Curr. Biol. 11 (2001) R691-R694.
    • (2001) Curr. Biol. , vol.11
    • Jeng, R.L.1    Welch, M.D.2
  • 33
    • 0034605038 scopus 로고    scopus 로고
    • Molecular links between endocytosis and actin cytoskeleton
    • B. Qualmann, M.M. Kessel, R.B. Kelly, Molecular links between endocytosis and actin cytoskeleton, J. Cell Biol. 150 (2000) F111-F116.
    • (2000) J. Cell Biol. , vol.150
    • Qualmann, B.1    Kessel, M.M.2    Kelly, R.B.3
  • 34
    • 0035952983 scopus 로고    scopus 로고
    • Molecular requirements for the internalization step of endocytosis: Insights from yeast
    • 1535
    • A.L. Munn, Molecular requirements for the internalization step of endocytosis: insights from yeast, Biochim. Biophys. Acta 1535 (2001) 236-257.
    • (2001) Biochim. Biophys. Acta , pp. 236-257
    • Munn, A.L.1
  • 35
    • 0031901141 scopus 로고    scopus 로고
    • Protein kinase C and the cytoskeleton
    • C. Keenan, D. Kelleher, Protein kinase C and the cytoskeleton, Cell Signal. 10 (1998) 225-232.
    • (1998) Cell Signal. , vol.10 , pp. 225-232
    • Keenan, C.1    Kelleher, D.2
  • 36
    • 0027162398 scopus 로고
    • Actin polymerization and pseudopod reorganization accompany anti-CD3-induced growth arrest in Jurkat T cells
    • M.V. Parsey, G.K. Lewis, Actin polymerization and pseudopod reorganization accompany anti-CD3-induced growth arrest in Jurkat T cells, J. Immunol. 151 (1993) 1881-1893.
    • (1993) J. Immunol. , vol.151 , pp. 1881-1893
    • Parsey, M.V.1    Lewis, G.K.2
  • 37
    • 0026527780 scopus 로고
    • Phorbol ester-induced actin assembly in neutrophils: Role of protein kinase C
    • G.P. Downey, C.K. Chan, P. Lea, A. Takai, S. Grinstein, Phorbol ester-induced actin assembly in neutrophils: role of protein kinase C, J. Cell Biol. 116 (1992) 695-706.
    • (1992) J. Cell Biol. , vol.116 , pp. 695-706
    • Downey, G.P.1    Chan, C.K.2    Lea, P.3    Takai, A.4    Grinstein, S.5
  • 38
    • 0032517822 scopus 로고    scopus 로고
    • Calcium and protein kinase regulate the actin cytoskeleton in the synaptic terminal of retinal bipolar cells
    • C. Job, L. Lagnado, Calcium and protein kinase regulate the actin cytoskeleton in the synaptic terminal of retinal bipolar cells, J. Cell Biol. 143 (1998) 1661-1672.
    • (1998) J. Cell Biol. , vol.143 , pp. 1661-1672
    • Job, C.1    Lagnado, L.2


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