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Volumn 26, Issue 6, 2012, Pages 2394-2400

Ferritin couples iron and fatty acid metabolism

Author keywords

Arachidonic acid; Calorimetry; Ferrihydrite; X ray crystallography

Indexed keywords

APOFERRITIN; ARACHIDONIC ACID; FATTY ACID; FERRIC HYDROXIDE; FERRITIN; FREE RADICAL; IRON; OCTANOIC ACID; SOLVENT;

EID: 84861788364     PISSN: 08926638     EISSN: 15306860     Source Type: Journal    
DOI: 10.1096/fj.11-198853     Document Type: Article
Times cited : (40)

References (34)
  • 2
    • 32544436435 scopus 로고    scopus 로고
    • The multigene family of fatty acid-binding proteins (FABPs): Function, structure and polymorphism
    • Chmurzynska, A. (2006) The multigene family of fatty acid-binding proteins (FABPs): function, structure and polymorphism. J. Appl. Genet. 47, 39-48
    • (2006) J. Appl. Genet. , vol.47 , pp. 39-48
    • Chmurzynska, A.1
  • 3
    • 0026736804 scopus 로고
    • Three-dimensional structure of recombinant human muscle fatty acid-binding protein
    • Zanotti, G., Scapin, G., Spadon, P., Veerkamp, J. H., and Sacchettini, J. C. (1992) Three-dimensional structure of recombinant human muscle fatty acid-binding protein. J. Biol. Chem. 267, 18541-18550
    • (1992) J. Biol. Chem. , vol.267 , pp. 18541-18550
    • Zanotti, G.1    Scapin, G.2    Spadon, P.3    Veerkamp, J.H.4    Sacchettini, J.C.5
  • 4
    • 70350455500 scopus 로고    scopus 로고
    • Lessons from the crystallographic analysis of small molecule binding to human serum albumin
    • Curry, S. (2009) Lessons from the crystallographic analysis of small molecule binding to human serum albumin. Drug Metab. Pharmacokinet. 24, 342-357
    • (2009) Drug Metab. Pharmacokinet. , vol.24 , pp. 342-357
    • Curry, S.1
  • 5
    • 66349090778 scopus 로고    scopus 로고
    • 2 structure/ function, mechanism, and signaling
    • 2 structure/ function, mechanism, and signaling. J. Lipid Res. 50(Suppl), S237-S242
    • (2009) J. Lipid Res. , vol.50 , Issue.SUPPL.
    • Burke, J.E.1    Dennis, E.A.2
  • 6
    • 78649444888 scopus 로고    scopus 로고
    • Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson's, Huntington's, Alzheimer's, prions, bactericides, chemical toxicology and others as examples
    • Kell, D. B. (2010) Towards a unifying, systems biology understanding of large-scale cellular death and destruction caused by poorly liganded iron: Parkinson's, Huntington's, Alzheimer's, prions, bactericides, chemical toxicology and others as examples. Arch. Toxicol. 84, 825-889
    • (2010) Arch. Toxicol. , vol.84 , pp. 825-889
    • Kell, D.B.1
  • 7
    • 0034983085 scopus 로고    scopus 로고
    • Arachidonic acid as a bioactive molecule
    • Brash, A. R. (2001) Arachidonic acid as a bioactive molecule. J. Clin. Invest. 107, 1339-1345
    • (2001) J. Clin. Invest. , vol.107 , pp. 1339-1345
    • Brash, A.R.1
  • 8
    • 0033568442 scopus 로고    scopus 로고
    • 1in human monocytes. Evidence for transcriptional and post-transcriptional regulation
    • 1 in human monocytes. Evidence for transcriptional and post-transcriptional regulation. Eur. J. Biochem. 264, 736-745
    • (1999) Eur. J. Biochem. , vol.264 , pp. 736-745
    • Elia, G.1    Polla, B.2    Rossi, A.3    Santoro, M.G.4
  • 10
    • 0034002559 scopus 로고    scopus 로고
    • Contrasting effects of excess ferritin expression on the iron-mediated oxidative stress induced by tert-butyl hydroperoxide or ultraviolet-A in human fibroblasts and keratinocytes
    • DOI 10.1016/S1011-1344(99)00154-2
    • Giordani, A., Haigle, J., Leflon, P., Risler, A., Salmon, S., Aubailly, M., Maziere, J. C., Santus, R., and Morliere, P. (2000) Contrasting effects of excess ferritin expression on the iron-mediated oxidative stress induced by tert-butyl hydroperoxide or ultraviolet-A in human fibroblasts and keratinocytes. J. Photochem. Photobiol. B 54, 43-54 (Pubitemid 30124227)
    • (2000) Journal of Photochemistry and Photobiology B: Biology , vol.54 , Issue.1 , pp. 43-54
    • Giordani, A.1    Haigle, J.2    Leflon, P.3    Risler, A.4    Salmon, S.5    Aubailly, M.6    Maziere, J.-C.7    Santus, R.8    Morliere, P.9
  • 11
    • 0035003922 scopus 로고    scopus 로고
    • Association of serum ferritin and indices of body fat distribution and obesity in Mexican American men-the Third National Health and Nutrition Examination Survey
    • Gillum, R. F. (2001) Association of serum ferritin and indices of body fat distribution and obesity in Mexican American men-the Third National Health and Nutrition Examination Survey. Int. J. Obes. Relat. Metab. Disord. 25, 639-645
    • (2001) Int. J. Obes. Relat. Metab. Disord. , vol.25 , pp. 639-645
    • Gillum, R.F.1
  • 13
    • 16344374288 scopus 로고    scopus 로고
    • Structural basis for high-affinity volatile anesthetic binding in a natural 4-helix bundle protein
    • DOI 10.1096/fj.04-3171com
    • Liu, R., Loll, P. J., and Eckenhoff, R. G. (2005) Structural basis for high-affinity volatile anesthetic binding in a natural 4-helix bundle protein. FASEB J. 19, 567-576 (Pubitemid 40471248)
    • (2005) FASEB Journal , vol.19 , Issue.6 , pp. 567-576
    • Liu, R.1    Loll, P.J.2    Eckenhoff, R.G.3
  • 16
    • 0029040871 scopus 로고
    • High resolution crystal structures of amphibian red-cell L ferritin: Potential roles for structural plasticity and solvation in function
    • Trikha, J., Theil, E. C., and Allewell, N. M. (1995) High resolution crystal structures of amphibian red-cell L ferritin: potential roles for structural plasticity and solvation in function. J. Mol. Biol. 248, 949-967
    • (1995) J. Mol. Biol. , vol.248 , pp. 949-967
    • Trikha, J.1    Theil, E.C.2    Allewell, N.M.3
  • 18
    • 0027522012 scopus 로고
    • Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin, and site-directed mutants
    • Sun, S., Arosio, P., Levi, S., and Chasteen, N. D. (1993) Ferroxidase kinetics of human liver apoferritin, recombinant H-chain apoferritin, and site-directed mutants. Biochemistry 32, 9362-9369 (Pubitemid 23292055)
    • (1993) Biochemistry , vol.32 , Issue.36 , pp. 9362-9369
    • Sun, S.1    Arosio, P.2    Levi, S.3    Chasteen, N.D.4
  • 19
    • 0026469339 scopus 로고
    • Ferroxidase kinetics of horse spleen apoferritin
    • Sun, S., and Chasteen, N. D. (1992) Ferroxidase kinetics of horse spleen apoferritin. J. Biol. Chem. 267, 25160-25166
    • (1992) J. Biol. Chem. , vol.267 , pp. 25160-25166
    • Sun, S.1    Chasteen, N.D.2
  • 21
    • 0028067272 scopus 로고
    • Direct observation of the iron binding sites in a ferritin
    • DOI 10.1016/0014-5793(94)00781-0
    • Hempstead, P. D., Hudson, A. J., Artymiuk, P. J., Andrews, S. C., Banfield, M. J., Guest, J. R., and Harrison, P. M. (1994) Direct observation of the iron binding sites in a ferritin. FEBS Lett. 350, 258-262 (Pubitemid 24268033)
    • (1994) FEBS Letters , vol.350 , Issue.2-3 , pp. 258-262
    • Hempstead, P.D.1
  • 22
    • 79960411403 scopus 로고    scopus 로고
    • Moving iron through ferritin protein nanocages depends on residues throughout each four α-helix bundle subunit
    • Haldar, S., Bevers, L. E., Tosha, T., and Theil, E. C. (2011) Moving iron through ferritin protein nanocages depends on residues throughout each four α-helix bundle subunit. J. Biol. Chem. 286, 25620-25627
    • (2011) J. Biol. Chem. , vol.286 , pp. 25620-25627
    • Haldar, S.1    Bevers, L.E.2    Tosha, T.3    Theil, E.C.4
  • 25
    • 1842583828 scopus 로고    scopus 로고
    • The Putative "Nucleation Site" in Human H-Chain Ferritin Is Not Required for Mineralization of the Iron Core
    • DOI 10.1021/bi0498813
    • Bou-Abdallah, F., Biasiotto, G., Arosio, P., and Chasteen, N. D. (2004) The putative "nucleation site" in human H-chain ferritin is not required for mineralization of the iron core. Biochemistry 43, 4332-4337 (Pubitemid 38445654)
    • (2004) Biochemistry , vol.43 , Issue.14 , pp. 4332-4337
    • Bou-Abdallah, F.1    Biasiotto, G.2    Arosio, P.3    Chasteen, N.D.4
  • 26
    • 77953812371 scopus 로고    scopus 로고
    • X-ray structures of ferritins and related proteins
    • Crichton, R. R., and Declercq, J. P. (2010) X-ray structures of ferritins and related proteins. Biochim. Biophys. Acta 1800, 706-718
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 706-718
    • Crichton, R.R.1    Declercq, J.P.2
  • 27
    • 41649090143 scopus 로고    scopus 로고
    • Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization
    • DOI 10.1042/BJ20071544
    • MacKenzie, E. L., and Tsuji, Y. (2008) Elevated intracellular calcium increases ferritin H expression through an NFAT-independent post-transcriptional mechanism involving mRNA stabilization. Biochem. J. 411, 107-113 (Pubitemid 351482352)
    • (2008) Biochemical Journal , vol.411 , Issue.1 , pp. 107-113
    • MacKenzie, E.L.1    Tsuji, Y.2
  • 28
    • 27844572844 scopus 로고    scopus 로고
    • JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress
    • Tsuji, Y. (2005) JunD activates transcription of the human ferritin H gene through an antioxidant response element during oxidative stress. Oncogene 24, 7567-7578
    • (2005) Oncogene , vol.24 , pp. 7567-7578
    • Tsuji, Y.1
  • 29
    • 0034711295 scopus 로고    scopus 로고
    • Overexpression of H ferritin and up-regulation of iron regulatory protein genes during differentiation of 3T3-L1 pre-adipocytes
    • DOI 10.1074/jbc.M004988200
    • Festa, M., Ricciardelli, G., Mele, G., Pietropaolo, C., Ruffo, A., and Colonna, A. (2000) Overexpression of H ferritin and up-regulation of iron regulatory protein genes during differentiation of 3T3-L1 pre-adipocytes. J. Biol. Chem. 275, 36708-36712 (Pubitemid 32002076)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.47 , pp. 36708-36712
    • Festa, M.1    Ricciardelli, G.2    Mele, G.3    Pietropaolo, C.4    Ruffo, A.5    Colonna, A.6
  • 31
    • 77950644284 scopus 로고    scopus 로고
    • Do high ferritin levels confer lower cardiovascular risk in men with type 2 diabetes?
    • Hermans, M. P., Ahn, S. A., Amoussou-Guenou, K. D., Balde, N. M., and Rousseau, M. F. (2010) Do high ferritin levels confer lower cardiovascular risk in men with type 2 diabetes? Diabet. Med. 27, 417-422
    • (2010) Diabet. Med. , vol.27 , pp. 417-422
    • Hermans, M.P.1    Ahn, S.A.2    Amoussou-Guenou, K.D.3    Balde, N.M.4    Rousseau, M.F.5
  • 32
    • 4444273210 scopus 로고    scopus 로고
    • Effect of manipulation of iron storage, transport, or availability on myelin composition and brain iron content in three different animal models
    • DOI 10.1002/jnr.20207
    • Ortiz, E., Pasquini, J. M., Thompson, K., Felt, B., Butkus, G., Beard, J., and Connor, J. R. (2004) Effect of manipulation of iron storage, transport, or availability on myelin composition and brain iron content in three different animal models. J. Neurosci. Res. 77, 681-689 (Pubitemid 39194609)
    • (2004) Journal of Neuroscience Research , vol.77 , Issue.5 , pp. 681-689
    • Ortiz, E.1    Pasquini, J.M.2    Thompson, K.3    Felt, B.4    Butkus, G.5    Beard, J.6    Connor, J.R.7
  • 33
    • 33846964515 scopus 로고    scopus 로고
    • Reduction of iron stores and cardiovascular outcomes in patients with peripheral arterial disease: A randomized controlled trial
    • Zacharski, L. R., Chow, B. K., Howes, P. S., Shamayeva, G., Baron, J. A., Dalman, R. L., Malenka, D. J., Ozaki, C. K., and Lavori, P. W. (2007) Reduction of iron stores and cardiovascular outcomes in patients with peripheral arterial disease: a randomized controlled trial. JAMA 297, 603-610
    • (2007) JAMA , vol.297 , pp. 603-610
    • Zacharski, L.R.1    Chow, B.K.2    Howes, P.S.3    Shamayeva, G.4    Baron, J.A.5    Dalman, R.L.6    Malenka, D.J.7    Ozaki, C.K.8    Lavori, P.W.9
  • 34
    • 0037481178 scopus 로고    scopus 로고
    • Serum ferritin and cardiovascular disease: A 17-year follow-up study in Busselton, Western Australia
    • DOI 10.1093/aje/kwg121
    • Knuiman, M. W., Divitini, M. L., Olynyk, J. K., Cullen, D. J., and Bartholomew, H. C. (2003) Serum ferritin and cardiovascular disease: a 17-year follow-up study in Busselton, Western Australia. Am. J. Epidemiol. 158, 144-149 (Pubitemid 36841946)
    • (2003) American Journal of Epidemiology , vol.158 , Issue.2 , pp. 144-149
    • Knuiman, M.W.1    Divitini, M.L.2    Olynyk, J.K.3    Cullen, D.J.4    Bartholomew, H.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.