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Volumn 42, Issue 13, 2017, Pages 2504-2515

Intranasal lactoferrin enhances α-secretase-dependent amyloid precursor protein processing via the ERK1/2-CREB and HIF-1α pathways in an Alzheimer's disease mouse model

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ADAM10 ENDOPEPTIDASE; ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; COPPER ZINC SUPEROXIDE DISMUTASE; CYCLIC AMP RESPONSIVE ELEMENT BINDING PROTEIN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; INTERLEUKIN 6; LACTOFERRIN; LIFICIGUAT; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; N [2 (4 BROMOCINNAMYLAMINO)ETHYL] 5 ISOQUINOLINESULFONAMIDE; REACTIVE OXYGEN METABOLITE; TUMOR NECROSIS FACTOR; VASCULOTROPIN; CREB1 PROTEIN, MOUSE; HIF1A PROTEIN, MOUSE; LTF PROTEIN, HUMAN; MAPK1 PROTEIN, MOUSE; NEUROPROTECTIVE AGENT; NOOTROPIC AGENT; PRESENILIN 1; PSEN1 PROTEIN, HUMAN; SECRETASE;

EID: 85033587544     PISSN: 0893133X     EISSN: 1740634X     Source Type: Journal    
DOI: 10.1038/npp.2017.8     Document Type: Article
Times cited : (77)

References (50)
  • 1
    • 56249097900 scopus 로고    scopus 로고
    • Neuroscience: The plaque plan
    • Abbott A. (2008). Neuroscience: the plaque plan. Nature 456: 161-164.
    • (2008) Nature , vol.456 , pp. 161-164
    • Abbott, A.1
  • 2
    • 0015528159 scopus 로고
    • Lactoferrin and transferrin: A comparative study
    • Aisen P, Leibman A. (1972). Lactoferrin and transferrin: a comparative study. Biochim Biophys Acta 257: 314-323.
    • (1972) Biochim Biophys Acta , vol.257 , pp. 314-323
    • Aisen, P.1    Leibman, A.2
  • 4
    • 0017389761 scopus 로고
    • A bactericidal effect for human lactoferrin
    • Arnold RR, Cole MF, McGhee JR. (1977). A bactericidal effect for human lactoferrin. Science 197: 263-265.
    • (1977) Science , vol.197 , pp. 263-265
    • Arnold, R.R.1    Cole, M.F.2    McGhee, J.R.3
  • 5
    • 84255170452 scopus 로고    scopus 로고
    • Hypoxia induces escape from innate immunity in cancer cells via increased expression of ADAM10: Role of nitric oxide
    • Barsoum IB, Hamilton TK, Li X, Cotechini T, Miles EA, Siemens DR, et al. (2011). Hypoxia induces escape from innate immunity in cancer cells via increased expression of ADAM10: role of nitric oxide. Cancer Res 71: 7433-7441.
    • (2011) Cancer Res , vol.71 , pp. 7433-7441
    • Barsoum, I.B.1    Hamilton, T.K.2    Li, X.3    Cotechini, T.4    Miles, E.A.5    Siemens, D.R.6
  • 6
    • 84255170452 scopus 로고    scopus 로고
    • Hypoxia induces escape from innate immunity in cancer cells via increased expression of ADAM10: Role of nitric oxide
    • Barsoum IB, Hamilton TK, Li X, Cotechini T, Miles EA, Siemens DR, et al. (2012). Hypoxia induces escape from innate immunity in cancer cells via increased expression of ADAM10: role of nitric oxide. Cancer Res 71: 7433-7441.
    • (2012) Cancer Res , vol.71 , pp. 7433-7441
    • Barsoum, I.B.1    Hamilton, T.K.2    Li, X.3    Cotechini, T.4    Miles, E.A.5    Siemens, D.R.6
  • 7
    • 84973520116 scopus 로고    scopus 로고
    • Neuroinflammation in Alzheimer's disease: Current evidence and future directions
    • Calsolaro V, Edison P. (2016). Neuroinflammation in Alzheimer's disease: current evidence and future directions. Alzheimers Dement 12: 719-732.
    • (2016) Alzheimers Dement , vol.12 , pp. 719-732
    • Calsolaro, V.1    Edison, P.2
  • 8
    • 84873346887 scopus 로고    scopus 로고
    • Distinct roles of methamphetamine in modulating spatial memory consolidation, retrieval, reconsolidation and the accompanying changes of ERK and CREB activation in hippocampus and prefrontal cortex
    • Cao G, Zhu J, Zhong Q, Shi C, Dang Y, HanWet al. (2013). Distinct roles of methamphetamine in modulating spatial memory consolidation, retrieval, reconsolidation and the accompanying changes of ERK and CREB activation in hippocampus and prefrontal cortex. Neuropharmacology 67: 144-154.
    • (2013) Neuropharmacology , vol.67 , pp. 144-154
    • Cao, G.1    Zhu, J.2    Zhong, Q.3    Shi, C.4    Dang, Y.5    Han, W.6
  • 10
    • 84980053547 scopus 로고    scopus 로고
    • Fundamental role of pan-inflammation and oxidative-nitrosative pathways in neuropathogenesis of Alzheimer's disease in focal cerebral ischemic rats
    • Daulatzai MA. (2016). Fundamental role of pan-inflammation and oxidative-nitrosative pathways in neuropathogenesis of Alzheimer's disease in focal cerebral ischemic rats. Am J Neurodegener Dis 5: 102-130.
    • (2016) Am J Neurodegener Dis , vol.5 , pp. 102-130
    • Daulatzai, M.A.1
  • 11
    • 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, Benaissa M, 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    Benaissa, M.5    Pierce, A.6
  • 12
    • 77955281765 scopus 로고    scopus 로고
    • Activated astroglia during chronic inflammation in Alzheimer's disease-do they neglect their neurosupportive roles?
    • Fuller S, Steele M, Munch G. (2010). Activated astroglia during chronic inflammation in Alzheimer's disease-do they neglect their neurosupportive roles? Mutat Res 690: 40-49.
    • (2010) Mutat Res , vol.690 , pp. 40-49
    • Fuller, S.1    Steele, M.2    Munch, G.3
  • 14
    • 84962295938 scopus 로고    scopus 로고
    • Deferoxamine-mediated up-regulation of HIF-1alpha prevents dopaminergic neuronal death via the activation of MAPK family proteins in MPTP-Treated mice
    • Guo C, Hao LJ, Yang ZH, Chai R, Zhang S, Gu Y, et al. (2016). Deferoxamine-mediated up-regulation of HIF-1alpha prevents dopaminergic neuronal death via the activation of MAPK family proteins in MPTP-Treated mice. Exp Neurol 280: 13-23.
    • (2016) Exp Neurol , vol.280 , pp. 13-23
    • Guo, C.1    Hao, L.J.2    Yang, Z.H.3    Chai, R.4    Zhang, S.5    Gu, Y.6
  • 15
    • 84869080922 scopus 로고    scopus 로고
    • Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloidogenic APP processing in a transgenic mouse model of Alzheimer's disease
    • Guo C, Wang T, Zheng W, Shan ZY, Teng WP, Wang ZY. (2013). Intranasal deferoxamine reverses iron-induced memory deficits and inhibits amyloidogenic APP processing in a transgenic mouse model of Alzheimer's disease. Neurobiol Aging 34: 562-575.
    • (2013) Neurobiol Aging , vol.34 , pp. 562-575
    • Guo, C.1    Wang, T.2    Zheng, W.3    Shan, Z.Y.4    Teng, W.P.5    Wang, Z.Y.6
  • 16
    • 84936118142 scopus 로고    scopus 로고
    • Intranasal deferoxamine attenuates synapse loss via upregulating the P38/HIF-1alpha pathway on the brain of APP/PS1 transgenic mice
    • Guo C, Zhang YX, Wang T, Zhong ML, Yang ZH, Hao LJ, et al. (2015). Intranasal deferoxamine attenuates synapse loss via upregulating the P38/HIF-1alpha pathway on the brain of APP/PS1 transgenic mice. Front Aging Neurosci 7: 104.
    • (2015) Front Aging Neurosci , vol.7 , pp. 104
    • Guo, C.1    Zhang, Y.X.2    Wang, T.3    Zhong, M.L.4    Yang, Z.H.5    Hao, L.J.6
  • 17
    • 84949575479 scopus 로고    scopus 로고
    • Role of LRP1 and ERK and cAMP signaling pathways in lactoferrin-induced lipolysis in mature rat adipocytes
    • Ikoma-Seki K, Nakamura K, Morishita S, Ono T, Sugiyama K, Nishino H, et al. (2015). Role of LRP1 and ERK and cAMP signaling pathways in lactoferrin-induced lipolysis in mature rat adipocytes. PLoS One 10: e0141378.
    • (2015) PLoS One , vol.10 , pp. e0141378
    • Ikoma-Seki, K.1    Nakamura, K.2    Morishita, S.3    Ono, T.4    Sugiyama, K.5    Nishino, H.6
  • 18
    • 53749089729 scopus 로고    scopus 로고
    • Lactoferrin induces cell surface retention of prion protein and inhibits prion accumulation
    • Iwamaru Y, Shimizu Y, Imamura M, Murayama Y, Endo R, Tagawa Y, et al. (2008). Lactoferrin induces cell surface retention of prion protein and inhibits prion accumulation. J Neurochem 107: 636-646.
    • (2008) J Neurochem , vol.107 , pp. 636-646
    • Iwamaru, Y.1    Shimizu, Y.2    Imamura, M.3    Murayama, Y.4    Endo, R.5    Tagawa, Y.6
  • 19
    • 80051937861 scopus 로고    scopus 로고
    • Apo- and holo-lactoferrin are both internalized by lactoferrin receptor via clathrin-mediated endocytosis but differentially affect ERKsignaling and cell proliferation in Caco-2 cells
    • Jiang R, Lopez V, Kelleher SL, Lonnerdal B. (2011). Apo- And holo-lactoferrin are both internalized by lactoferrin receptor via clathrin-mediated endocytosis but differentially affect ERKsignaling and cell proliferation in Caco-2 cells. J Cell Physiol 226: 3022-3031.
    • (2011) J Cell Physiol , vol.226 , pp. 3022-3031
    • Jiang, R.1    Lopez, V.2    Kelleher, S.L.3    Lonnerdal, B.4
  • 20
    • 84856327464 scopus 로고    scopus 로고
    • Iron metabolism and the innate immune response to infection
    • Johnson EE, Wessling-Resnick M. (2012). Iron metabolism and the innate immune response to infection. Microbes Infect 14: 207-216.
    • (2012) Microbes Infect , vol.14 , pp. 207-216
    • Johnson, E.E.1    Wessling-Resnick, M.2
  • 21
    • 84889237760 scopus 로고    scopus 로고
    • Enhanced brain delivery of deferasirox-lactoferrin conjugates for iron chelation therapy in neurodegenerative disorders: In vitro and in vivo studies
    • Kamalinia G, Khodagholi F, Atyabi F, Amini M, Shaerzadeh F, Sharifzadeh M, et al. (2013). Enhanced brain delivery of deferasirox-lactoferrin conjugates for iron chelation therapy in neurodegenerative disorders: in vitro and in vivo studies. Mol Pharm 10: 4418-4431.
    • (2013) Mol Pharm , vol.10 , pp. 4418-4431
    • Kamalinia, G.1    Khodagholi, F.2    Atyabi, F.3    Amini, M.4    Shaerzadeh, F.5    Sharifzadeh, M.6
  • 22
    • 0027723591 scopus 로고
    • Lactotransferrin immunocytochemistry in Alzheimer and normal human brain
    • Kawamata T, Tooyama I, Yamada T, Walker DG, McGeer PL. (1993). Lactotransferrin immunocytochemistry in Alzheimer and normal human brain. Am J Pathol 142: 1574-1585.
    • (1993) Am J Pathol , vol.142 , pp. 1574-1585
    • Kawamata, T.1    Tooyama, I.2    Yamada, T.3    Walker, D.G.4    McGeer, P.L.5
  • 23
    • 77954917968 scopus 로고    scopus 로고
    • Activity-dependent alpha-cleavage of nectin-1 is mediated by a disintegrin and metalloprotease 10 (ADAM10
    • Kim J, Lilliehook C, Dudak A, Prox J, Saftig P, Federoff HJ, et al. (2010). Activity-dependent alpha-cleavage of nectin-1 is mediated by a disintegrin and metalloprotease 10 (ADAM10). J Biol Chem 285: 22919-22926.
    • (2010) J Biol Chem , vol.285 , pp. 22919-22926
    • Kim, J.1    Lilliehook, C.2    Dudak, A.3    Prox, J.4    Saftig, P.5    Federoff, H.J.6
  • 24
    • 77953256518 scopus 로고    scopus 로고
    • The role of iron and chelators on infections in iron overload and non iron loaded conditions: Prospects for the design of new antimicrobial therapies
    • Kontoghiorghes GJ, Kolnagou A, Skiada A, Petrikkos G. (2010). The role of iron and chelators on infections in iron overload and non iron loaded conditions: prospects for the design of new antimicrobial therapies. Hemoglobin 34: 227-239.
    • (2010) Hemoglobin , vol.34 , pp. 227-239
    • Kontoghiorghes, G.J.1    Kolnagou, A.2    Skiada, A.3    Petrikkos, G.4
  • 25
    • 84879456908 scopus 로고    scopus 로고
    • CREB phosphorylation regulates striatal transcriptional responses in the self-Administration model of methamphetamine addiction in the rat
    • Krasnova IN, Chiflikyan M, Justinova Z, McCoy MT, Ladenheim B, Jayanthi S, et al. (2013). CREB phosphorylation regulates striatal transcriptional responses in the self-Administration model of methamphetamine addiction in the rat. Neurobiol Dis 58: 132-143.
    • (2013) Neurobiol Dis , vol.58 , pp. 132-143
    • Krasnova, I.N.1    Chiflikyan, M.2    Justinova, Z.3    McCoy, M.T.4    Ladenheim, B.5    Jayanthi, S.6
  • 26
    • 77952395053 scopus 로고    scopus 로고
    • Lactoferrin decreases LPS-induced mitochondrial dysfunction in cultured cells and in animal endotoxemia model
    • Kruzel ML, Actor JK, Radak Z, Bacsi A, Saavedra-Molina A, Boldogh I. (2010). Lactoferrin decreases LPS-induced mitochondrial dysfunction in cultured cells and in animal endotoxemia model. Innate Immun 16: 67-79.
    • (2010) Innate Immun , vol.16 , pp. 67-79
    • Kruzel, M.L.1    Actor, J.K.2    Radak, Z.3    Bacsi, A.4    Saavedra-Molina, A.5    Boldogh, I.6
  • 27
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • Lammich S, Kojro E, Postina R, Gilbert S, Pfeiffer R, Jasionowski M, et al. (1999). Constitutive and regulated alpha-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc Natl Acad Sci USA 96: 3922-3927.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3922-3927
    • Lammich, S.1    Kojro, E.2    Postina, R.3    Gilbert, S.4    Pfeiffer, R.5    Jasionowski, M.6
  • 28
    • 0028321575 scopus 로고
    • The iron-binding protein lactotransferrin is present in pathologic lesions in a variety of neurodegenerative disorders: A comparative immunohistochemical analysis
    • Leveugle B, Spik G, Perl DP, Bouras C, Fillit HM, Hof PR. (1994). The iron-binding protein lactotransferrin is present in pathologic lesions in a variety of neurodegenerative disorders: a comparative immunohistochemical analysis. Brain Res 650: 20-31.
    • (1994) Brain Res , vol.650 , pp. 20-31
    • Leveugle, B.1    Spik, G.2    Perl, D.P.3    Bouras, C.4    Fillit, H.M.5    Hof, P.R.6
  • 29
    • 84957536870 scopus 로고    scopus 로고
    • RACK1 promotes maintenance of morphine-Associated memory via activation of an ERK-CREB dependent pathway in hippocampus
    • Liu L, Zhu J, Zhou L, Wan L. (2016). RACK1 promotes maintenance of morphine-Associated memory via activation of an ERK-CREB dependent pathway in hippocampus. Sci Rep 6: 20183.
    • (2016) Sci Rep , vol.6 , pp. 20183
    • Liu, L.1    Zhu, J.2    Zhou, L.3    Wan, L.4
  • 30
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calciumregulating roles for secreted forms of the beta-Amyloid precursor protein
    • Mattson MP, Cheng B, Culwell AR, Esch FS, Lieberburg I, Rydel RE. (1993). Evidence for excitoprotective and intraneuronal calciumregulating roles for secreted forms of the beta-Amyloid precursor protein. Neuron 10: 243-254.
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1    Cheng, B.2    Culwell, A.R.3    Esch, F.S.4    Lieberburg, I.5    Rydel, R.E.6
  • 31
    • 84969776833 scopus 로고    scopus 로고
    • Lactoferrin, a pleiotropic protein in health and disease
    • Mayeur S, Spahis S, Pouliot Y, Levy E. (2015). Lactoferrin, a pleiotropic protein in health and disease. Antioxid Redox Signal 24: 813-836.
    • (2015) Antioxid Redox Signal , vol.24 , pp. 813-836
    • Mayeur, S.1    Spahis, S.2    Pouliot, Y.3    Levy, E.4
  • 32
    • 3342928851 scopus 로고    scopus 로고
    • The antimicrobial activity of lactoferrin: Current status and perspectives
    • Orsi N. (2004). The antimicrobial activity of lactoferrin: current status and perspectives. Biometals 17: 189-196.
    • (2004) Biometals , vol.17 , pp. 189-196
    • Orsi, N.1
  • 33
    • 0010487727 scopus 로고    scopus 로고
    • Expression of iron transport proteins and excessive iron accumulation in the brain in neurodegenerative disorders
    • Qian ZM, Wang Q. (1998). Expression of iron transport proteins and excessive iron accumulation in the brain in neurodegenerative disorders. Brain Res Brain Res Rev 27: 257-267.
    • (1998) Brain Res Brain Res Rev , vol.27 , pp. 257-267
    • Qian, Z.M.1    Wang, Q.2
  • 34
    • 84860342691 scopus 로고    scopus 로고
    • CREB-dependent transcriptional control and quantal changes in persistent long-Term potentiation in hippocampal interneurons
    • Ran I, Laplante I, Lacaille JC. (2012). CREB-dependent transcriptional control and quantal changes in persistent long-Term potentiation in hippocampal interneurons. J Neurosci 32: 6335-6350.
    • (2012) J Neurosci , vol.32 , pp. 6335-6350
    • Ran, I.1    Laplante, I.2    Lacaille, J.C.3
  • 35
    • 84888878250 scopus 로고    scopus 로고
    • The iron-binding protein lactoferrin protects vulnerable dopamine neurons from degeneration by preserving mitochondrial calcium homeostasis
    • Rousseau E, Michel PP, Hirsch EC. (2013). The iron-binding protein lactoferrin protects vulnerable dopamine neurons from degeneration by preserving mitochondrial calcium homeostasis. Mol Pharmacol 84: 888-898.
    • (2013) Mol Pharmacol , vol.84 , pp. 888-898
    • Rousseau, E.1    Michel, P.P.2    Hirsch, E.C.3
  • 36
    • 0024314702 scopus 로고
    • Amyloid beta protein precursor and the pathogenesis of Alzheimer's disease
    • Selkoe DJ. (1989). Amyloid beta protein precursor and the pathogenesis of Alzheimer's disease. Cell 58: 611-612.
    • (1989) Cell , vol.58 , pp. 611-612
    • Selkoe, D.J.1
  • 37
    • 0037174618 scopus 로고    scopus 로고
    • Alzheimer's disease is a synaptic failure
    • Selkoe DJ. (2002). Alzheimer's disease is a synaptic failure. Science 298: 789-791.
    • (2002) Science , vol.298 , pp. 789-791
    • Selkoe, D.J.1
  • 38
    • 84922771460 scopus 로고    scopus 로고
    • Melatonin stimulates the nonamyloidogenic processing of betaAPP through the positive transcriptional regulation of ADAM10 and ADAM17
    • Shukla M, Htoo HH, Wintachai P, Hernandez JF, Dubois C, Postina R, et al. (2015). Melatonin stimulates the nonamyloidogenic processing of betaAPP through the positive transcriptional regulation of ADAM10 and ADAM17. J Pineal Res 58: 151-165.
    • (2015) J Pineal Res , vol.58 , pp. 151-165
    • Shukla, M.1    Htoo, H.H.2    Wintachai, P.3    Hernandez, J.F.4    Dubois, C.5    Postina, R.6
  • 39
    • 0032431973 scopus 로고    scopus 로고
    • Reactions of denatured proteins with other cellular components to form insoluble aggregates and protection by lactoferrin
    • Takase K. (1998). Reactions of denatured proteins with other cellular components to form insoluble aggregates and protection by lactoferrin. FEBS Lett 441: 271-274.
    • (1998) FEBS Lett , vol.441 , pp. 271-274
    • Takase, K.1
  • 40
    • 0042634362 scopus 로고    scopus 로고
    • Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory
    • Turner PR, O'Connor K, Tate WP, Abraham WC. (2003). Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory. Prog Neurobiol 70: 1-32.
    • (2003) Prog Neurobiol , vol.70 , pp. 1-32
    • Turner, P.R.1    O'Connor, K.2    Tate, W.P.3    Abraham, W.C.4
  • 42
    • 26244462301 scopus 로고    scopus 로고
    • Proteolytic mechanisms in amyloid-beta metabolism: Therapeutic implications for Alzheimer's disease
    • Vardy ER, Catto AJ, Hooper NM. (2005). Proteolytic mechanisms in amyloid-beta metabolism: therapeutic implications for Alzheimer's disease. Trends Mol Med 11: 464-472.
    • (2005) Trends Mol Med , vol.11 , pp. 464-472
    • Vardy, E.R.1    Catto, A.J.2    Hooper, N.M.3
  • 43
    • 84891501352 scopus 로고    scopus 로고
    • Protective effects of human lactoferrin during Aggregatibacter actinomycetemcomitans-induced bacteremia in lactoferrin-deficient mice
    • Velusamy SK, Poojary R, Ardeshna R, Alabdulmohsen W, Fine DH, Velliyagounder K. (2014). Protective effects of human lactoferrin during Aggregatibacter actinomycetemcomitans-induced bacteremia in lactoferrin-deficient mice. Antimicrob Agents Chemother 58: 397-404.
    • (2014) Antimicrob Agents Chemother , vol.58 , pp. 397-404
    • Velusamy, S.K.1    Poojary, R.2    Ardeshna, R.3    Alabdulmohsen, W.4    Fine, D.H.5    Velliyagounder, K.6
  • 44
    • 79955655453 scopus 로고    scopus 로고
    • Activation of the alpha-secretase processing of AbetaPP as a therapeutic approach in Alzheimer's disease
    • Vincent B, Govitrapong P. (2011). Activation of the alpha-secretase processing of AbetaPP as a therapeutic approach in Alzheimer's disease. J Alzheimers Dis 24(Suppl 2): 75-94.
    • (2011) J Alzheimers Dis , vol.24 , pp. 75-94
    • Vincent, B.1    Govitrapong, P.2
  • 45
    • 84863253131 scopus 로고    scopus 로고
    • Activation of NMDA receptors upregulates a disintegrin and metalloproteinase 10 via a Wnt/MAPK signaling pathway
    • Wan XZ, Li B, Li YC, Yang XL, Zhang W, Zhong L, et al. (2012). Activation of NMDA receptors upregulates a disintegrin and metalloproteinase 10 via a Wnt/MAPK signaling pathway. J Neurosci 32: 3910-3916.
    • (2012) J Neurosci , vol.32 , pp. 3910-3916
    • Wan, X.Z.1    Li, B.2    Li, Y.C.3    Yang, X.L.4    Zhang, W.5    Zhong, L.6
  • 46
    • 84934880850 scopus 로고    scopus 로고
    • The protective effect of lactoferrin on ventral mesencephalon neurons against MPP+ is not connected with its iron binding ability
    • Wang J, Bi M, Liu H, Song N, Xie J. (2015). The protective effect of lactoferrin on ventral mesencephalon neurons against MPP+ is not connected with its iron binding ability. Sci Rep 5: 10729.
    • (2015) Sci Rep , vol.5 , pp. 10729
    • Wang, J.1    Bi, M.2    Liu, H.3    Song, N.4    Xie, J.5
  • 47
    • 77955341230 scopus 로고    scopus 로고
    • Deposition of lactoferrin in fibrillar-Type senile plaques in the brains of transgenic mouse models of Alzheimer's disease
    • Wang L, Sato H, Zhao S, Tooyama I. (2010). Deposition of lactoferrin in fibrillar-Type senile plaques in the brains of transgenic mouse models of Alzheimer's disease. Neurosci Lett 481: 164-167.
    • (2010) Neurosci Lett , vol.481 , pp. 164-167
    • Wang, L.1    Sato, H.2    Zhao, S.3    Tooyama, I.4
  • 48
    • 78650450609 scopus 로고    scopus 로고
    • Natural products as a source of Alzheimer's drug leads
    • Williams P, Sorribas A, Howes MJ. (2011). Natural products as a source of Alzheimer's drug leads. Nat Prod Rep 28: 48-77.
    • (2011) Nat Prod Rep , vol.28 , pp. 48-77
    • Williams, P.1    Sorribas, A.2    Howes, M.J.3
  • 49
    • 84873524215 scopus 로고    scopus 로고
    • Bovine lactoferricin induces TIMP-3 via the ERK1/2-Sp1 axis in human articular chondrocytes
    • Yan D, Chen D, Hawse JR, van Wijnen AJ, Im HJ. (2013). Bovine lactoferricin induces TIMP-3 via the ERK1/2-Sp1 axis in human articular chondrocytes. Gene 517: 12-18.
    • (2013) Gene , vol.517 , pp. 12-18
    • Yan, D.1    Chen, D.2    Hawse, J.R.3    Van Wijnen, A.J.4    Im, H.J.5
  • 50
    • 84874107679 scopus 로고    scopus 로고
    • Human apo-lactoferrin as a physiological mimetic of hypoxia stabilizes hypoxia-inducible factor-1 alpha
    • Zakharova ET, Kostevich VA, Sokolov AV, Vasilyev VB. (2012). Human apo-lactoferrin as a physiological mimetic of hypoxia stabilizes hypoxia-inducible factor-1 alpha. Biometals 25: 1247-1259.
    • (2012) Biometals , vol.25 , pp. 1247-1259
    • Zakharova, E.T.1    Kostevich, V.A.2    Sokolov, A.V.3    Vasilyev, V.B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.