메뉴 건너뛰기




Volumn 84, Issue 6, 2013, Pages 888-898

The iron-binding protein lactoferrin protects vulnerable dopamine neurons from degeneration by preserving mitochondrial calcium homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

1 METHYL 4 PHENYLPYRIDINIUM; CALCIUM ION; DOPAMINE; FOCAL ADHESION KINASE; GLIAL CELL LINE DERIVED NEUROTROPHIC FACTOR; LACTOFERRIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOROTRITHIOIC ACID TRIBUTYL ESTER; PROTEIN KINASE B; PROTEOHEPARAN SULFATE; REACTIVE OXYGEN METABOLITE;

EID: 84888878250     PISSN: 0026895X     EISSN: 15210111     Source Type: Journal    
DOI: 10.1124/mol.113.087965     Document Type: Article
Times cited : (69)

References (51)
  • 1
    • 0036191387 scopus 로고    scopus 로고
    • The physiology of lactoferrin
    • Brock JH (2002) The physiology of lactoferrin. Biochem Cell Biol 80 :1-6.
    • (2002) Biochem Cell Biol , vol.80 , pp. 1-6
    • Brock, J.H.1
  • 3
    • 84861554724 scopus 로고    scopus 로고
    • α-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions
    • Calì T, Ottolini D, Negro A, and Brini M (2012) α-Synuclein controls mitochondrial calcium homeostasis by enhancing endoplasmic reticulum-mitochondria interactions. J Biol Chem 287:17914-17929.
    • (2012) J Biol Chem , vol.287 , pp. 17914-17929
    • Calì, T.1    Ottolini, D.2    Negro, A.3    Brini, M.4
  • 4
    • 0141741347 scopus 로고    scopus 로고
    • Parkinson' s disease: Mechanisms and models
    • Dauer W and Przedborski S (2003) Parkinson' s disease: mechanisms and models. Neuron 39:889-909.
    • (2003) Neuron , vol.39 , pp. 889-909
    • Dauer, W.1    Przedborski, S.2
  • 7
    • 0034668833 scopus 로고    scopus 로고
    • Mitochondria and calcium: From cell signalling to cell death
    • Duchen MR (2000) Mitochondria and calcium: from cell signalling to cell death. J Physiol 529:57-68.
    • (2000) J Physiol , vol.529 , pp. 57-68
    • Duchen, M.R.1
  • 9
    • 0035976727 scopus 로고    scopus 로고
    • Lactoferrin is synthesized by activated microglia in the human substantia nigra and its synthesis by the human microglial CHME cell line is upregulated by tumor necrosis factor alpha or 1-methyl-4-phenylpyridinium treatment
    • Fillebeen C, Ruchoux MM, Mitchell V, Vincent S, Benaïssa M, and Pierce A (2001) Lactoferrin is synthesized by activated microglia in the human substantia nigra and its synthesis by the human microglial CHME cell line is upregulated by tumor necrosis factor alpha or 1-methyl-4-phenylpyridinium treatment. Brain Res Mol Brain Res 96 :103-113.
    • (2001) Brain Res Mol Brain Res , vol.96 , pp. 103-113
    • Fillebeen, C.1    Ruchoux, M.M.2    Mitchell, V.3    Vincent, S.4    Benaïssa, M.5    Pierce, A.6
  • 11
    • 0035241262 scopus 로고    scopus 로고
    • Assessment of plasma lactoferrin in Parkinson's disease
    • Grau AJ, Willig V, Fogel W, and Werle E (2001) Assessment of plasma lactoferrin in Parkinson's disease. Mov Disord 16:131-134.
    • (2001) Mov Disord , vol.16 , pp. 131-134
    • Grau, A.J.1    Willig, V.2    Fogel, W.3    Werle, E.4
  • 12
    • 52949091483 scopus 로고    scopus 로고
    • Paraxanthine, the primary metabolite of caffeine, provides protection against dopaminergic cell death via stimulation of ryanodine receptor channels
    • Guerreiro S, Toulorge D, Hirsch E, Marien M, Sokoloff P, and Michel PP (2008) Paraxanthine, the primary metabolite of caffeine, provides protection against dopaminergic cell death via stimulation of ryanodine receptor channels. Mol Pharmacol 74:980-989.
    • (2008) Mol Pharmacol , vol.74 , pp. 980-989
    • Guerreiro, S.1    Toulorge, D.2    Hirsch, E.3    Marien, M.4    Sokoloff, P.5    Michel, P.P.6
  • 13
    • 65649126049 scopus 로고    scopus 로고
    • Protection of midbrain dopaminergic neurons by the end-product of purine metabolism uric acid: Potentiation by low-level depolarization
    • Guerreiro S, Ponceau A, Toulorge D, Martin E, Alvarez-Fischer D, Hirsch EC, and Michel PP (2009) Protection of midbrain dopaminergic neurons by the end-product of purine metabolism uric acid: potentiation by low-level depolarization. J Neurochem 109:1118-1128.
    • (2009) J Neurochem , vol.109 , pp. 1118-1128
    • Guerreiro, S.1    Ponceau, A.2    Toulorge, D.3    Martin, E.4    Alvarez-Fischer, D.5    Hirsch, E.C.6    Michel, P.P.7
  • 14
    • 80054951619 scopus 로고    scopus 로고
    • Prolonged membrane depolarization enhances midbrain dopamine neuron differentiation via epigenetic histone modifications
    • He XB, Yi SH, Rhee YH, Kim H, Han YM, Lee SH, Lee H, Park CH, Lee YS, and Richardson E et al. (2011) Prolonged membrane depolarization enhances midbrain dopamine neuron differentiation via epigenetic histone modifications. Stem Cells 29:1861-1873.
    • (2011) Stem Cells , vol.29 , pp. 1861-1873
    • He, X.B.1    Yi, S.H.2    Rhee, Y.H.3    Kim, H.4    Han, Y.M.5    Lee, S.H.6    Lee, H.7    Park, C.H.8    Lee, Y.S.9    Richardson, E.10
  • 15
    • 33845329178 scopus 로고    scopus 로고
    • Signalling via integrins: Implications for cell survival and anticancer strategies
    • Hehlgans S, Haase M, and Cordes N (2007) Signalling via integrins: implications for cell survival and anticancer strategies. Biochim Biophys Acta 1775:163-180.
    • (2007) Biochim Biophys Acta , vol.1775 , pp. 163-180
    • Hehlgans, S.1    Haase, M.2    Cordes, N.3
  • 16
    • 0026034279 scopus 로고
    • Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: An X-ray microanalysis
    • Hirsch EC, Brandel JP, Galle P, Javoy-Agid F, and Agid Y (1991) Iron and aluminum increase in the substantia nigra of patients with Parkinson's disease: an X-ray microanalysis. J Neurochem 56:446-451.
    • (1991) J Neurochem , vol.56 , pp. 446-451
    • Hirsch, E.C.1    Brandel, J.P.2    Galle, P.3    Javoy-Agid, F.4    Agid, Y.5
  • 17
    • 62549133546 scopus 로고    scopus 로고
    • Neuroinflammation in Parkinson's disease: A target for neuroprotection?
    • Hirsch EC and Hunot S (2009) Neuroinflammation in Parkinson's disease: a target for neuroprotection? Lancet Neurol 8:382-397.
    • (2009) Lancet Neurol , vol.8 , pp. 382-397
    • Hirsch, E.C.1    Hunot, S.2
  • 19
    • 0041430614 scopus 로고    scopus 로고
    • Dysfunction of mitochondrial complex I and the proteasome: Interactions between two biochemical deficits in a cellular model of Parkinson's disease
    • Höglinger GU, Carrard G, Michel PP, Medja F, Lombès A, Ruberg M, Friguet B, and Hirsch EC (2003) Dysfunction of mitochondrial complex I and the proteasome: interactions between two biochemical deficits in a cellular model of Parkinson's disease. J Neurochem 86:1297-1307.
    • (2003) J Neurochem , vol.86 , pp. 1297-1307
    • Höglinger, G.U.1    Carrard, G.2    Michel, P.P.3    Medja, F.4    Lombès, A.5    Ruberg, M.6    Friguet, B.7    Hirsch, E.C.8
  • 20
    • 0032213139 scopus 로고    scopus 로고
    • Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change
    • Jameson GB, Anderson BF, Norris GE, Thomas DH, and Baker EN (1998) Structure of human apolactoferrin at 2.0 A resolution. Refinement and analysis of ligand-induced conformational change. Acta Crystallogr D Biol Crystallogr 54 :1319-1335.
    • (1998) Acta Crystallogr D Biol Crystallogr , vol.54 , pp. 1319-1335
    • Jameson, G.B.1    Anderson, B.F.2    Norris, G.E.3    Thomas, D.H.4    Baker, E.N.5
  • 21
    • 57349138396 scopus 로고    scopus 로고
    • Shuttling of calcium between endoplasmic reticulum and mitochondria in the renal vasculature
    • Kanwar YS and Sun L (2008) Shuttling of calcium between endoplasmic reticulum and mitochondria in the renal vasculature. Am J Physiol Renal Physiol 295: F1301-F1302.
    • (2008) Am J Physiol Renal Physiol , vol.295
    • Kanwar, Y.S.1    Sun, L.2
  • 23
    • 33645642577 scopus 로고    scopus 로고
    • Akt kinase phosphorylation of inositol 1,4,5-trisphosphate receptors
    • Khan MT, Wagner L, 2nd, Yule DI, Bhanumathy C, and Joseph SK (2006) Akt kinase phosphorylation of inositol 1,4,5-trisphosphate receptors. J Biol Chem 281: 3731-3737.
    • (2006) J Biol Chem , vol.281 , pp. 3731-3737
    • Khan, M.T.1    Wagner II, L.2    Yule, D.I.3    Bhanumathy, C.4    Joseph, S.K.5
  • 24
    • 67449128162 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase p85alpha regulatory subunit gene Met326Ile polymorphism in women with polycystic ovary syndrome
    • Kim JJ, Choi YM, Hong MA, Hwang SS, Yoon SH, Chae SJ, Jee BC, Ku SY, Kim JG, and Moon SY (2009) Phosphatidylinositol 3-kinase p85alpha regulatory subunit gene Met326Ile polymorphism in women with polycystic ovary syndrome. Hum Reprod 24:1184-1190.
    • (2009) Hum Reprod , vol.24 , pp. 1184-1190
    • Kim, J.J.1    Choi, Y.M.2    Hong, M.A.3    Hwang, S.S.4    Yoon, S.H.5    Chae, S.J.6    Jee, B.C.7    Ku, S.Y.8    Kim, J.G.9    Moon, S.Y.10
  • 25
    • 33748751668 scopus 로고    scopus 로고
    • Lactoferrin decreases pollen antigen-induced allergic airway inflammation in a murine model of asthma
    • Kruzel ML, Bacsi A, Choudhury B, Sur S, and Boldogh I (2006) Lactoferrin decreases pollen antigen-induced allergic airway inflammation in a murine model of asthma. Immunology 119:159-166.
    • (2006) Immunology , vol.119 , pp. 159-166
    • Kruzel, M.L.1    Bacsi, A.2    Choudhury, B.3    Sur, S.4    Boldogh, I.5
  • 26
    • 80051922480 scopus 로고    scopus 로고
    • Inhibition of SARS pseudovirus cell entry by lactoferrin binding to heparan sulfate proteoglycans
    • Lang J, Yang N, Deng J, Liu K, Yang P, Zhang G, and Jiang C (2011) Inhibition of SARS pseudovirus cell entry by lactoferrin binding to heparan sulfate proteoglycans. PLoS ONE 6:e23710.
    • (2011) PLoS ONE , vol.6
    • Lang, J.1    Yang, N.2    Deng, J.3    Liu, K.4    Yang, P.5    Zhang, G.6    Jiang, C.7
  • 27
    • 0029126185 scopus 로고
    • Lactoferrin: A general review
    • Levay PF and Viljoen M (1995) Lactoferrin: a general review. Haematologica 80: 252-267.
    • (1995) Haematologica , vol.80 , pp. 252-267
    • Levay, P.F.1    Viljoen, M.2
  • 28
    • 0029997918 scopus 로고    scopus 로고
    • Cellular distribution of the iron-binding protein lactotransferrin in the mesencephalon of Parkinson's disease cases
    • Leveugle B, Faucheux BA, Bouras C, Nillesse N, Spik G, Hirsch EC, Agid Y, and Hof PR (1996) Cellular distribution of the iron-binding protein lactotransferrin in the mesencephalon of Parkinson's disease cases. Acta Neuropathol 91:566-572.
    • (1996) Acta Neuropathol , vol.91 , pp. 566-572
    • Leveugle, B.1    Faucheux, B.A.2    Bouras, C.3    Nillesse, N.4    Spik, G.5    Hirsch, E.C.6    Agid, Y.7    Hof, P.R.8
  • 29
    • 0033557640 scopus 로고    scopus 로고
    • Distinct mechanisms underlie neurotoxin-mediated cell death in cultured dopaminergic neurons
    • Lotharius J, Dugan LL, and O'Malley KL (1999) Distinct mechanisms underlie neurotoxin-mediated cell death in cultured dopaminergic neurons. J Neurosci 19: 1284-1293.
    • (1999) J Neurosci , vol.19 , pp. 1284-1293
    • Lotharius, J.1    Dugan, L.L.2    O'Malley, K.L.3
  • 31
    • 84883357109 scopus 로고    scopus 로고
    • Specific needs of dopamine neurons for stimulation in order to survive: Implication for Parkinson disease
    • Michel PP, Toulorge D, Guerreiro S, and Hirsch EC (2013) Specific needs of dopamine neurons for stimulation in order to survive: implication for Parkinson disease. FASEB J 27:3414-3423.
    • (2013) FASEB J , vol.27 , pp. 3414-3423
    • Michel, P.P.1    Toulorge, D.2    Guerreiro, S.3    Hirsch, E.C.4
  • 32
    • 65649103043 scopus 로고    scopus 로고
    • Synthetic RGDS peptide attenuates lipopolysaccharide-induced pulmonary inflammation by inhibiting integrin signaled MAP kinase pathways
    • Moon C, Han JR, Park HJ, Hah JS, and Kang JL (2009) Synthetic RGDS peptide attenuates lipopolysaccharide-induced pulmonary inflammation by inhibiting integrin signaled MAP kinase pathways. Respir Res 10:18.
    • (2009) Respir Res , vol.10 , pp. 18
    • Moon, C.1    Han, J.R.2    Park, H.J.3    Hah, J.S.4    Kang, J.L.5
  • 33
    • 0041353623 scopus 로고    scopus 로고
    • Prevention of dopaminergic neuronal death by cyclic AMP in mixed neuronal/glial mesencephalic cultures requires the repression of presumptive astrocytes
    • Mourlevat S, Troadec JD, Ruberg M, and Michel PP (2003) Prevention of dopaminergic neuronal death by cyclic AMP in mixed neuronal/glial mesencephalic cultures requires the repression of presumptive astrocytes. Mol Pharmacol 64: 578-586.
    • (2003) Mol Pharmacol , vol.64 , pp. 578-586
    • Mourlevat, S.1    Troadec, J.D.2    Ruberg, M.3    Michel, P.P.4
  • 34
    • 0034676144 scopus 로고    scopus 로고
    • Mitochondrial free calcium levels (Rhod-2 fluorescence) and ultrastructural alterations in neuronally differentiated PC12 cells during ceramide-dependent cell death
    • Muriel MP, Lambeng N, Darios F, Michel PP, Hirsch EC, Agid Y, and Ruberg M (2000) Mitochondrial free calcium levels (Rhod-2 fluorescence) and ultrastructural alterations in neuronally differentiated PC12 cells during ceramide-dependent cell death. J Comp Neurol 426:297-315.
    • (2000) J Comp Neurol , vol.426 , pp. 297-315
    • Muriel, M.P.1    Lambeng, N.2    Darios, F.3    Michel, P.P.4    Hirsch, E.C.5    Agid, Y.6    Ruberg, M.7
  • 36
    • 0036182026 scopus 로고    scopus 로고
    • Mitochondrial involvement in Parkinson's disease
    • Orth M and Schapira AH (2002) Mitochondrial involvement in Parkinson's disease. Neurochem Int 40:533-541.
    • (2002) Neurochem Int , vol.40 , pp. 533-541
    • Orth, M.1    Schapira, A.H.2
  • 37
    • 70349237594 scopus 로고    scopus 로고
    • Lactoferrin: A multifunctional protein
    • Pierce A, Legrand D, and Mazurier J (2009) [Lactoferrin: a multifunctional protein]. Med Sci (Paris) 25:361-369.
    • (2009) Med Sci (Paris) , vol.25 , pp. 361-369
    • Pierce, A.1    Legrand, D.2    Mazurier, J.3
  • 39
    • 33747672714 scopus 로고    scopus 로고
    • Interaction of human lactoferrin with cell adhesion molecules through RGD motif elucidated by lactoferrin-binding epitopes
    • Sakamoto K, Ito Y, Mori T, and Sugimura K (2006) Interaction of human lactoferrin with cell adhesion molecules through RGD motif elucidated by lactoferrin-binding epitopes. J Biol Chem 281:24472-24478.
    • (2006) J Biol Chem , vol.281 , pp. 24472-24478
    • Sakamoto, K.1    Ito, Y.2    Mori, T.3    Sugimura, K.4
  • 40
    • 3042789539 scopus 로고    scopus 로고
    • Rescue of mesencephalic dopaminergic neurons in culture by low-level stimulation of voltagegated sodium channels
    • Salthun-Lassalle B, Hirsch EC, Wolfart J, Ruberg M, and Michel PP (2004) Rescue of mesencephalic dopaminergic neurons in culture by low-level stimulation of voltagegated sodium channels. J Neurosci 24:5922-5930.
    • (2004) J Neurosci , vol.24 , pp. 5922-5930
    • Salthun-Lassalle, B.1    Hirsch, E.C.2    Wolfart, J.3    Ruberg, M.4    Michel, P.P.5
  • 42
    • 84870666521 scopus 로고    scopus 로고
    • "Iron-saturated" bovine lactoferrin improves the chemotherapeutic effects of tamoxifen in the treatment of basal-like breast cancer in mice
    • Sun X, Jiang R, Przepiorski A, Reddy S, Palmano KP, and Krissansen GW (2012) "Iron-saturated" bovine lactoferrin improves the chemotherapeutic effects of tamoxifen in the treatment of basal-like breast cancer in mice. BMC Cancer 12:591.
    • (2012) BMC Cancer , vol.12 , pp. 591
    • Sun, X.1    Jiang, R.2    Przepiorski, A.3    Reddy, S.4    Palmano, K.P.5    Krissansen, G.W.6
  • 43
    • 28344453346 scopus 로고    scopus 로고
    • Mammalian lactoferrin receptors: Structure and function
    • Suzuki YA, Lopez V, and Lönnerdal B (2005) Mammalian lactoferrin receptors: structure and function. Cell Mol Life Sci 62:2560-2575.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2560-2575
    • Suzuki, Y.A.1    Lopez, V.2    Lönnerdal, B.3
  • 44
    • 46149090133 scopus 로고    scopus 로고
    • In vivo diffusion of lactoferrin in brain extracellular space is regulated by interactions with heparan sulfate
    • Thorne RG, Lakkaraju A, Rodriguez-Boulan E, and Nicholson C (2008) In vivo diffusion of lactoferrin in brain extracellular space is regulated by interactions with heparan sulfate. Proc Natl Acad Sci USA 105:8416-8421.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8416-8421
    • Thorne, R.G.1    Lakkaraju, A.2    Rodriguez-Boulan, E.3    Nicholson, C.4
  • 45
    • 77953848545 scopus 로고    scopus 로고
    • KATP channel blockade protects midbrain dopamine neurons by repressing a glia-to-neuron signaling cascade that ultimately disrupts mitochondrial calcium homeostasis
    • Toulorge D, Guerreiro S, Hirsch EC, and Michel PP (2010) KATP channel blockade protects midbrain dopamine neurons by repressing a glia-to-neuron signaling cascade that ultimately disrupts mitochondrial calcium homeostasis. J Neurochem 114:553-564.
    • (2010) J Neurochem , vol.114 , pp. 553-564
    • Toulorge, D.1    Guerreiro, S.2    Hirsch, E.C.3    Michel, P.P.4
  • 46
    • 80051701494 scopus 로고    scopus 로고
    • Neuroprotection of midbrain dopamine neurons by nicotine is gated by cytoplasmic Ca2+
    • Toulorge D, Guerreiro S, Hild A, Maskos U, Hirsch EC, and Michel PP (2011) Neuroprotection of midbrain dopamine neurons by nicotine is gated by cytoplasmic Ca2+. FASEB J 25:2563-2573.
    • (2011) FASEB J , vol.25 , pp. 2563-2573
    • Toulorge, D.1    Guerreiro, S.2    Hild, A.3    Maskos, U.4    Hirsch, E.C.5    Michel, P.P.6
  • 47
    • 33745289118 scopus 로고    scopus 로고
    • The phenotypic differentiation of locus ceruleus noradrenergic neurons mediated by brain-derived neurotrophic factor is enhanced by corticotropin releasing factor through the activation of a cAMP-dependent signaling pathway
    • Traver S, Marien M, Martin E, Hirsch EC, and Michel PP (2006) The phenotypic differentiation of locus ceruleus noradrenergic neurons mediated by brain-derived neurotrophic factor is enhanced by corticotropin releasing factor through the activation of a cAMP-dependent signaling pathway. Mol Pharmacol 70:30-40.
    • (2006) Mol Pharmacol , vol.70 , pp. 30-40
    • Traver, S.1    Marien, M.2    Martin, E.3    Hirsch, E.C.4    Michel, P.P.5
  • 48
    • 84875550832 scopus 로고    scopus 로고
    • Bovine lactoferrin inhibits lung cancer growth through suppression of both inflammation and expression of vascular endothelial growth factor
    • Tung YT, Chen HL, Yen CC, Lee PY, Tsai HC, Lin MF, and Chen CM (2013) Bovine lactoferrin inhibits lung cancer growth through suppression of both inflammation and expression of vascular endothelial growth factor. J Dairy Sci 96:2095-2106.
    • (2013) J Dairy Sci , vol.96 , pp. 2095-2106
    • Tung, Y.T.1    Chen, H.L.2    Yen, C.C.3    Lee, P.Y.4    Tsai, H.C.5    Lin, M.F.6    Chen, C.M.7
  • 49
    • 34248641665 scopus 로고    scopus 로고
    • A structural comparison of human serum transferrin and human lactoferrin
    • Wally J and Buchanan SK (2007) A structural comparison of human serum transferrin and human lactoferrin. Biometals 20:249-262.
    • (2007) Biometals , vol.20 , pp. 249-262
    • Wally, J.1    Buchanan, S.K.2
  • 50
    • 3342965285 scopus 로고    scopus 로고
    • Lactoferrin: Role in iron homeostasis and host defense against microbial infection
    • Ward PP and Conneely OM (2004) Lactoferrin: role in iron homeostasis and host defense against microbial infection. Biometals 17:203-208.
    • (2004) Biometals , vol.17 , pp. 203-208
    • Ward, P.P.1    Conneely, O.M.2
  • 51
    • 77953544756 scopus 로고    scopus 로고
    • Lactoferrin induces growth arrest and nuclear accumulation of Smad-2 in HeLa cells
    • Zemann N, Klein P, Wetzel E, Huettinger F, and Huettinger M (2010) Lactoferrin induces growth arrest and nuclear accumulation of Smad-2 in HeLa cells. Biochimie 92:880-884.
    • (2010) Biochimie , vol.92 , pp. 880-884
    • Zemann, N.1    Klein, P.2    Wetzel, E.3    Huettinger, F.4    Huettinger, M.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.