메뉴 건너뛰기




Volumn 45, Issue 5, 2009, Pages 972-979

Iron overload alters iron-regulatory genes and proteins, down-regulates osteoblastic phenotype, and is associated with apoptosis in fetal rat calvaria cultures

Author keywords

Bone nodules; Ferritin; Ferrous sulfate; Osteocalcin; Transferrin receptor

Indexed keywords

FERRITIN; FERROUS SULFATE; IRON; REGULATOR PROTEIN; TRANSFERRIN RECEPTOR;

EID: 70349282987     PISSN: 87563282     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bone.2009.07.073     Document Type: Article
Times cited : (78)

References (41)
  • 1
    • 0037173578 scopus 로고    scopus 로고
    • Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells
    • Crichton R.R., Wilmet S., Legssyer R., and Ward R. Molecular and cellular mechanisms of iron homeostasis and toxicity in mammalian cells. J. Inorg. Biochem. 91 (2002) 9-18
    • (2002) J. Inorg. Biochem. , vol.91 , pp. 9-18
    • Crichton, R.R.1    Wilmet, S.2    Legssyer, R.3    Ward, R.4
  • 2
    • 33745405978 scopus 로고    scopus 로고
    • Age-associated iron accumulation in bone: implications for postmenopausal osteoporosis and a new target for prevention and treatment by chelation
    • Liu G., Men P., Kenner G.H., and Miller S.C. Age-associated iron accumulation in bone: implications for postmenopausal osteoporosis and a new target for prevention and treatment by chelation. BioMetals 19 (2006) 245-251
    • (2006) BioMetals , vol.19 , pp. 245-251
    • Liu, G.1    Men, P.2    Kenner, G.H.3    Miller, S.C.4
  • 3
    • 0035087037 scopus 로고    scopus 로고
    • Disposition, accumulation and toxicity of iron fed as iron (II) sulfate or as sodium iron EDTA in rats
    • Appel M.J., Kuper C.F., and Woutersen R.A. Disposition, accumulation and toxicity of iron fed as iron (II) sulfate or as sodium iron EDTA in rats. Food Chem. Toxicol. 39 (2001) 261-269
    • (2001) Food Chem. Toxicol. , vol.39 , pp. 261-269
    • Appel, M.J.1    Kuper, C.F.2    Woutersen, R.A.3
  • 4
    • 0034006860 scopus 로고    scopus 로고
    • Genetic disorders affecting proteins of iron metabolism: clinical implications
    • Sheth S., and Brittenham G.M. Genetic disorders affecting proteins of iron metabolism: clinical implications. Annu. Rev. Med. 51 (2000) 443-464
    • (2000) Annu. Rev. Med. , vol.51 , pp. 443-464
    • Sheth, S.1    Brittenham, G.M.2
  • 5
    • 36849032903 scopus 로고    scopus 로고
    • Diagnosis and management of transfusion iron overload: the role of imaging
    • Wood J.C. Diagnosis and management of transfusion iron overload: the role of imaging. Am. J. Hematol. 82 (2007) 1132-1135
    • (2007) Am. J. Hematol. , vol.82 , pp. 1132-1135
    • Wood, J.C.1
  • 10
    • 0242637137 scopus 로고    scopus 로고
    • Iron lactate-induced osteomalacia in association with osteoblast dynamics
    • Matsushima S., Torii M., Ozaki K., and Narama I. Iron lactate-induced osteomalacia in association with osteoblast dynamics. Toxicol. Pathol. 31 (2003) 646-654
    • (2003) Toxicol. Pathol. , vol.31 , pp. 646-654
    • Matsushima, S.1    Torii, M.2    Ozaki, K.3    Narama, I.4
  • 11
    • 0025257154 scopus 로고
    • Characterization of the transferrin receptor in UMR-106-01 osteoblast-like cells
    • Kasai K., Hori M.T., and Goodman W.G. Characterization of the transferrin receptor in UMR-106-01 osteoblast-like cells. Endocrinology 126 3 (1990) 1742-1749
    • (1990) Endocrinology , vol.126 , Issue.3 , pp. 1742-1749
    • Kasai, K.1    Hori, M.T.2    Goodman, W.G.3
  • 12
    • 0029088699 scopus 로고
    • The iron-binding protein ferritin is expressed in cells of the osteoblastic lineage in vitro and in vivo
    • Spanner M., Weber K., Lanske B., Ihbe A., Siggelkow H., Schutze H., et al. The iron-binding protein ferritin is expressed in cells of the osteoblastic lineage in vitro and in vivo. Bone 17 2 (1995) 161-165
    • (1995) Bone , vol.17 , Issue.2 , pp. 161-165
    • Spanner, M.1    Weber, K.2    Lanske, B.3    Ihbe, A.4    Siggelkow, H.5    Schutze, H.6
  • 13
    • 84970822533 scopus 로고
    • Ferritin in the serum of normal subjects and patients with iron deficiency and iron overload
    • Jacobs A., Miller F., Worwood M., Beamish M.R., and Wardrop C.A. Ferritin in the serum of normal subjects and patients with iron deficiency and iron overload. BMJ 4 (1972) 206-208
    • (1972) BMJ , vol.4 , pp. 206-208
    • Jacobs, A.1    Miller, F.2    Worwood, M.3    Beamish, M.R.4    Wardrop, C.A.5
  • 14
    • 0033826764 scopus 로고    scopus 로고
    • Iron regulatory proteins and the molecular control of mammalian iron metabolism
    • Eisenstein R.S. Iron regulatory proteins and the molecular control of mammalian iron metabolism. Annu. Rev. Nutr. 20 (2000) 627-662
    • (2000) Annu. Rev. Nutr. , vol.20 , pp. 627-662
    • Eisenstein, R.S.1
  • 15
    • 0029855076 scopus 로고    scopus 로고
    • Histopathological evaluation of liver, pancreas, spleen, and heart from iron-overloaded Sprague-Dawley rats
    • Whittaker P., Hines F.A., Robl M.G., and Dunkel V.C. Histopathological evaluation of liver, pancreas, spleen, and heart from iron-overloaded Sprague-Dawley rats. Toxicol. Pathol. 24 5 (1996) 55-63
    • (1996) Toxicol. Pathol. , vol.24 , Issue.5 , pp. 55-63
    • Whittaker, P.1    Hines, F.A.2    Robl, M.G.3    Dunkel, V.C.4
  • 16
    • 9244230038 scopus 로고    scopus 로고
    • Oxidative stress, β-cell apoptosis, and decreased insulin secretory capacity in mouse models of hemochromatosis
    • Cooksey R.C., Jouihan H.A., Ajioka R.S., Hazel M.W., Jones D.L., Kushner J.P., and McClain D.A. Oxidative stress, β-cell apoptosis, and decreased insulin secretory capacity in mouse models of hemochromatosis. Endocrinology 145 11 (2004) 5305-5312
    • (2004) Endocrinology , vol.145 , Issue.11 , pp. 5305-5312
    • Cooksey, R.C.1    Jouihan, H.A.2    Ajioka, R.S.3    Hazel, M.W.4    Jones, D.L.5    Kushner, J.P.6    McClain, D.A.7
  • 17
  • 18
    • 0022569874 scopus 로고
    • Mineralized bone nodules formed in vitro from enzymatically released rat calvaria cell populations
    • Bellows C.G., Aubin J.E., Heersche J.N.M., and Antosz M.E. Mineralized bone nodules formed in vitro from enzymatically released rat calvaria cell populations. Calcif. Tissue Int. 38 (1986) 143-154
    • (1986) Calcif. Tissue Int. , vol.38 , pp. 143-154
    • Bellows, C.G.1    Aubin, J.E.2    Heersche, J.N.M.3    Antosz, M.E.4
  • 19
    • 0022707291 scopus 로고
    • Regulation of transferrin receptor expression at the cell surface by insulin-like growth factors, epidermal growth factor and platelet-derived growth factor
    • Davis R.J., and Czech M.P. Regulation of transferrin receptor expression at the cell surface by insulin-like growth factors, epidermal growth factor and platelet-derived growth factor. EMBO 5 4 (1986) 653-658
    • (1986) EMBO , vol.5 , Issue.4 , pp. 653-658
    • Davis, R.J.1    Czech, M.P.2
  • 20
    • 28544449476 scopus 로고    scopus 로고
    • Increased manganese uptake by primary astrocyte cultures with altered iron status is mediated primarily by divalent metal transporter
    • Erikson K.M., and Aschner M. Increased manganese uptake by primary astrocyte cultures with altered iron status is mediated primarily by divalent metal transporter. Neurotoxicology 27 (2006) 125-130
    • (2006) Neurotoxicology , vol.27 , pp. 125-130
    • Erikson, K.M.1    Aschner, M.2
  • 21
    • 0035947765 scopus 로고    scopus 로고
    • The orphan nuclear estrogen receptor-related receptor α (ERRα) is expressed throughout osteoblast differentiation and regulated bone formation in vitro
    • Bonnelye E., Merdad L., Kung V., and Aubin J.E. The orphan nuclear estrogen receptor-related receptor α (ERRα) is expressed throughout osteoblast differentiation and regulated bone formation in vitro. J. Cell Biol. 153 5 (2001) 971-983
    • (2001) J. Cell Biol. , vol.153 , Issue.5 , pp. 971-983
    • Bonnelye, E.1    Merdad, L.2    Kung, V.3    Aubin, J.E.4
  • 22
    • 0037623420 scopus 로고    scopus 로고
    • Differential accumulation of non-transferrin-bound iron by cardiac myocytes and fibroblasts
    • Liu Y., Parkes J.G., and Templeton D.M. Differential accumulation of non-transferrin-bound iron by cardiac myocytes and fibroblasts. J. Mol. Cell. Cardiol. 35 (2003) 505-514
    • (2003) J. Mol. Cell. Cardiol. , vol.35 , pp. 505-514
    • Liu, Y.1    Parkes, J.G.2    Templeton, D.M.3
  • 23
    • 37349123534 scopus 로고    scopus 로고
    • Dual effect of strontium ranelate: stimulation of osteoblast differentiation and inhibition of osteoclast formation and resorption in vitro
    • Bonnelye E., Chabadel A., Saltel F., and Jurdic P. Dual effect of strontium ranelate: stimulation of osteoblast differentiation and inhibition of osteoclast formation and resorption in vitro. Bone 42 1 (2008) 129-138
    • (2008) Bone , vol.42 , Issue.1 , pp. 129-138
    • Bonnelye, E.1    Chabadel, A.2    Saltel, F.3    Jurdic, P.4
  • 24
    • 26444485498 scopus 로고    scopus 로고
    • Role of mitogen-activated protein kinases in hydrogen peroxide-induced cell death in osteoblastic cells
    • Park B.G., Yoo C.I., Kim H.T., Kwon C.H., and Kim Y.K. Role of mitogen-activated protein kinases in hydrogen peroxide-induced cell death in osteoblastic cells. Toxicol 215 (2005) 115-125
    • (2005) Toxicol , vol.215 , pp. 115-125
    • Park, B.G.1    Yoo, C.I.2    Kim, H.T.3    Kwon, C.H.4    Kim, Y.K.5
  • 25
    • 0032323828 scopus 로고    scopus 로고
    • Advances in the osteoblast lineage
    • Aubin J.E. Advances in the osteoblast lineage. Biochem. Cell. Biol. 76 6 (1998) 899-910
    • (1998) Biochem. Cell. Biol. , vol.76 , Issue.6 , pp. 899-910
    • Aubin, J.E.1
  • 26
    • 0031911846 scopus 로고    scopus 로고
    • Accumulation of iron by primary rat hepatocytes in long-term culture: changes in nuclear shape mediated by non-transferrin-bound forms of iron
    • Cable E.E., Connor J.R., and Isom H.C. Accumulation of iron by primary rat hepatocytes in long-term culture: changes in nuclear shape mediated by non-transferrin-bound forms of iron. Am. J. Pathol. 152 3 (1998) 781-792
    • (1998) Am. J. Pathol. , vol.152 , Issue.3 , pp. 781-792
    • Cable, E.E.1    Connor, J.R.2    Isom, H.C.3
  • 27
    • 14244258216 scopus 로고    scopus 로고
    • Iron accumulation and iron-regulatory protein activity in human hepatoma (HepG2) cells
    • Popovic Z., and Templeton D.M. Iron accumulation and iron-regulatory protein activity in human hepatoma (HepG2) cells. Mol. Cell. Biochem. 265 (2004) 37-45
    • (2004) Mol. Cell. Biochem. , vol.265 , pp. 37-45
    • Popovic, Z.1    Templeton, D.M.2
  • 28
    • 1442323987 scopus 로고    scopus 로고
    • Iron accumulation, iron-mediated toxicity and altered levels of ferritin and transferrin receptor in cultured astrocytes during incubation with ferric ammonium citrate
    • Hoepken H.H., Korten T., Robinson S.R., and Dringen R. Iron accumulation, iron-mediated toxicity and altered levels of ferritin and transferrin receptor in cultured astrocytes during incubation with ferric ammonium citrate. J. Neurochem. 88 (2004) 1194-1202
    • (2004) J. Neurochem. , vol.88 , pp. 1194-1202
    • Hoepken, H.H.1    Korten, T.2    Robinson, S.R.3    Dringen, R.4
  • 29
    • 0028006812 scopus 로고
    • Regulation of transferrin receptor recycling by protein phosphorylation
    • Beauchamp J.R., and Woodman P.G. Regulation of transferrin receptor recycling by protein phosphorylation. Biochem. J. 303 Pt 2 (1994) 647-655
    • (1994) Biochem. J. , vol.303 , Issue.PART 2 , pp. 647-655
    • Beauchamp, J.R.1    Woodman, P.G.2
  • 30
    • 0022428440 scopus 로고
    • Heterogeneous glycosylation of murine transferrin receptor subunits
    • van Driel I.R., and Goding J.W. Heterogeneous glycosylation of murine transferrin receptor subunits. Eur. J. Biochem. 149 (1985) 543-548
    • (1985) Eur. J. Biochem. , vol.149 , pp. 543-548
    • van Driel, I.R.1    Goding, J.W.2
  • 31
    • 0037093202 scopus 로고    scopus 로고
    • Regulation of ferritin genes and protein
    • Torti F.M., and Torti S.V. Regulation of ferritin genes and protein. Blood 99 10 (2002) 3505-3516
    • (2002) Blood , vol.99 , Issue.10 , pp. 3505-3516
    • Torti, F.M.1    Torti, S.V.2
  • 32
    • 0029131505 scopus 로고
    • Ascorbic acid enhances ferritin mRNA translation by an IRP/aconitase switch
    • Toth I., and Bridges K.R. Ascorbic acid enhances ferritin mRNA translation by an IRP/aconitase switch. J. Biol. Chem. 270 33 (1995) 19540-19544
    • (1995) J. Biol. Chem. , vol.270 , Issue.33 , pp. 19540-19544
    • Toth, I.1    Bridges, K.R.2
  • 33
    • 0033080559 scopus 로고    scopus 로고
    • In vitro osteoblastic differentiation of human bone marrow cells in the presence of metal ions
    • Morais S., Dias N., Sousa J.P., Fernandes M.H., and Carvalho G.S. In vitro osteoblastic differentiation of human bone marrow cells in the presence of metal ions. J. Biomed. Mater. Res. 44 (1999) 176-190
    • (1999) J. Biomed. Mater. Res. , vol.44 , pp. 176-190
    • Morais, S.1    Dias, N.2    Sousa, J.P.3    Fernandes, M.H.4    Carvalho, G.S.5
  • 34
    • 33745871571 scopus 로고    scopus 로고
    • Nrf2 negatively regulates osteoblast differentiation via interfering with Runx2-dependent transcriptional activation
    • Hinoi E., Fujimori S., Wang L., Hojo H., Uno K., and Yoneda Y. Nrf2 negatively regulates osteoblast differentiation via interfering with Runx2-dependent transcriptional activation. J. Biol. Chem. 281 26 (2006) 18015-18024
    • (2006) J. Biol. Chem. , vol.281 , Issue.26 , pp. 18015-18024
    • Hinoi, E.1    Fujimori, S.2    Wang, L.3    Hojo, H.4    Uno, K.5    Yoneda, Y.6
  • 35
    • 0347356247 scopus 로고    scopus 로고
    • Oxidative stress inhibits osteoblastic differentiation of bone cells by ERK and NF-κB
    • Bai X., Lu D., Bai J., Zheng H., Ke Z., Li X., and Luo S. Oxidative stress inhibits osteoblastic differentiation of bone cells by ERK and NF-κB. Biochem. Biophys. Res. Comm. 314 (2004) 197-207
    • (2004) Biochem. Biophys. Res. Comm. , vol.314 , pp. 197-207
    • Bai, X.1    Lu, D.2    Bai, J.3    Zheng, H.4    Ke, Z.5    Li, X.6    Luo, S.7
  • 36
    • 34848814178 scopus 로고    scopus 로고
    • Oxidative stress antagonizes Wnt signaling in osteoblast precursors by diverting β-catenin from T-cell factor- to Forkhead box O-mediated transcription
    • Almeida M., Han L., Martin-Millan M., O'Brien C.A., and Manolagas S.C. Oxidative stress antagonizes Wnt signaling in osteoblast precursors by diverting β-catenin from T-cell factor- to Forkhead box O-mediated transcription. J. Biol. Chem. 282 37 (2007) 27298-27305
    • (2007) J. Biol. Chem. , vol.282 , Issue.37 , pp. 27298-27305
    • Almeida, M.1    Han, L.2    Martin-Millan, M.3    O'Brien, C.A.4    Manolagas, S.C.5
  • 37
    • 0025316785 scopus 로고
    • Progressive development of the rat osteoblast phenotype in vitro: reciprocal relationships in expression of genes associated with osteoblast proliferation and differentiation during formation of the bone extracellular matrix
    • Owen T.A., Aronow M., Shalhoub V., Barone L.M., Wilming L., Tassinari M.S., Kennedy M.B., Pockwinse S., Lian J.B., and Stein G.S. Progressive development of the rat osteoblast phenotype in vitro: reciprocal relationships in expression of genes associated with osteoblast proliferation and differentiation during formation of the bone extracellular matrix. J. Cell. Physiol. (1990) 420-430
    • (1990) J. Cell. Physiol. , pp. 420-430
    • Owen, T.A.1    Aronow, M.2    Shalhoub, V.3    Barone, L.M.4    Wilming, L.5    Tassinari, M.S.6    Kennedy, M.B.7    Pockwinse, S.8    Lian, J.B.9    Stein, G.S.10
  • 38
    • 0036775797 scopus 로고    scopus 로고
    • Effect of free iron on collagen synthesis, cell proliferation and MMP-2 expression in rat hepatic stellate cells
    • Gardi C., Arezzini B., Fortino V., and Comporti M. Effect of free iron on collagen synthesis, cell proliferation and MMP-2 expression in rat hepatic stellate cells. Biochem. Pharmacol. 64 (2002) 1139-1145
    • (2002) Biochem. Pharmacol. , vol.64 , pp. 1139-1145
    • Gardi, C.1    Arezzini, B.2    Fortino, V.3    Comporti, M.4
  • 39
    • 0037378611 scopus 로고    scopus 로고
    • Expression of E-cadherin and other paracellular junction genes is decreased in iron-loaded hepatocytes
    • Bilello J.P., Cable E.E., and Isom H.C. Expression of E-cadherin and other paracellular junction genes is decreased in iron-loaded hepatocytes. Am. J. Pathol. 162 4 (2003) 1323-1338
    • (2003) Am. J. Pathol. , vol.162 , Issue.4 , pp. 1323-1338
    • Bilello, J.P.1    Cable, E.E.2    Isom, H.C.3
  • 40
    • 0034008280 scopus 로고    scopus 로고
    • Iron-dependent generation of free radicals: plausible mechanisms in the progressive deterioration of the temporomandibular joint
    • Zardeneta G., Milam S.B., and Schimtz J.P. Iron-dependent generation of free radicals: plausible mechanisms in the progressive deterioration of the temporomandibular joint. J. Oral. Maxillofac. Surg. 58 (2000) 302-308
    • (2000) J. Oral. Maxillofac. Surg. , vol.58 , pp. 302-308
    • Zardeneta, G.1    Milam, S.B.2    Schimtz, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.