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Volumn 58, Issue 2, 2015, Pages 151-165

Melatonin stimulates the nonamyloidogenic processing of βaPP through the positive transcriptional regulation of ADAM10 and ADAM17

Author keywords

Alzheimer; apoptosis; melatonin; metabolism; secretase; transcription

Indexed keywords

ADAM PROTEIN; ADAM10 ENDOPEPTIDASE; ADAM17 PROTEIN; ALPHA SECRETASE; AMYLOID PRECURSOR PROTEIN; MELATONIN; MELATONIN RECEPTOR; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; STAUROSPORINE; UNCLASSIFIED DRUG; ADAM10 PROTEIN, HUMAN; MEMBRANE PROTEIN; SECRETASE; TUMOR NECROSIS FACTOR-ALPHA CONVERTASE;

EID: 84922771460     PISSN: 07423098     EISSN: 1600079X     Source Type: Journal    
DOI: 10.1111/jpi.12200     Document Type: Article
Times cited : (78)

References (73)
  • 1
    • 84876850102 scopus 로고    scopus 로고
    • The universal nature, unequal distribution and antioxidant function of melatonin and its derivatives
    • Reiter RJ, Tan DX, Rosales-Corral SA, et al. The universal nature, unequal distribution and antioxidant function of melatonin and its derivatives. Mini-Rev Med Chem 2013; 13: 373-384.
    • (2013) Mini-Rev Med Chem , vol.13 , pp. 373-384
    • Reiter, R.J.1    Tan, D.X.2    Rosales-Corral, S.A.3
  • 2
    • 36248949004 scopus 로고    scopus 로고
    • Role of the melatonin system in the control of sleep: Therapeutic implications
    • Pandi-Perumal SR, Srinivasan V, Spence DW, et al. Role of the melatonin system in the control of sleep: therapeutic implications. CNS Drugs 2007; 21: 995-1018.
    • (2007) CNS Drugs , vol.21 , pp. 995-1018
    • Pandi-Perumal, S.R.1    Srinivasan, V.2    Spence, D.W.3
  • 3
    • 84904469326 scopus 로고    scopus 로고
    • Melatonin prevents maternal fructose intake-induced programmed hypertension in the offspring: Roles of nitric oxide and arachidonic acid metabolites
    • Tain YL, Leu S, Wu KLH, et al. Melatonin prevents maternal fructose intake-induced programmed hypertension in the offspring: roles of nitric oxide and arachidonic acid metabolites. J Pineal Res 2014; 57: 80-89.
    • (2014) J Pineal Res , vol.57 , pp. 80-89
    • Tain, Y.L.1    Leu, S.2    Wu, K.L.H.3
  • 4
    • 84925835510 scopus 로고    scopus 로고
    • Melatonin, a well-documented antioxidant with conditional pro-oxidant activity
    • Zhang HM, Zhang Y,. Melatonin, a well-documented antioxidant with conditional pro-oxidant activity. J Pineal Res 2014; 57: 131-146.
    • (2014) J Pineal Res , vol.57 , pp. 131-146
    • Zhang, H.M.1    Zhang, Y.2
  • 5
    • 0022484725 scopus 로고
    • Changes in melatonin secretion with age and pubescence
    • Waldhauser F, Steger H,. Changes in melatonin secretion with age and pubescence. J Neural Transm Suppl 1986; 21: 183-197.
    • (1986) J Neural Transm Suppl , vol.21 , pp. 183-197
    • Waldhauser, F.1    Steger, H.2
  • 6
    • 0023863323 scopus 로고
    • Alterations in nocturnal serum melatonin levels in humans with growth and aging
    • Waldhauser F, Weiszenbacher G, Tatzer E, et al. Alterations in nocturnal serum melatonin levels in humans with growth and aging. J Clin Endocrinol Metab 1988; 66: 648-652.
    • (1988) J Clin Endocrinol Metab , vol.66 , pp. 648-652
    • Waldhauser, F.1    Weiszenbacher, G.2    Tatzer, E.3
  • 7
    • 0025063656 scopus 로고
    • Daily variation in the concentration of melatonin and 5-methoxytryptophol in the human pineal gland: Effect of age and Alzheimer's disease
    • Skene DJ, Vivien-Roels B, Sparks DL, et al. Daily variation in the concentration of melatonin and 5-methoxytryptophol in the human pineal gland: effect of age and Alzheimer's disease. Brain Res 1990; 528: 170-174.
    • (1990) Brain Res , vol.528 , pp. 170-174
    • Skene, D.J.1    Vivien-Roels, B.2    Sparks, D.L.3
  • 8
    • 0033564472 scopus 로고    scopus 로고
    • Daily rhythm of serum melatonin levels and effect of light exposure in patients with dementia of the Alzheimer's type
    • Ohashi Y, Okamoto N, Uchida K, et al. Daily rhythm of serum melatonin levels and effect of light exposure in patients with dementia of the Alzheimer's type. Biol Psychiatry 1999; 45: 1646-1652.
    • (1999) Biol Psychiatry , vol.45 , pp. 1646-1652
    • Ohashi, Y.1    Okamoto, N.2    Uchida, K.3
  • 9
    • 0032901972 scopus 로고    scopus 로고
    • Decreased melatonin levels in postmortem cerebrospinal fluid in relation to aging, Alzheimer's disease, and apolipoprotein E-{epsilon}4/4 genotype
    • Liu RY, Zhou JN, van Heerikhuize J, et al. Decreased melatonin levels in postmortem cerebrospinal fluid in relation to aging, Alzheimer's disease, and apolipoprotein E-{epsilon}4/4 genotype. J Clin Endocrinol Metab 1999; 84: 323-327.
    • (1999) J Clin Endocrinol Metab , vol.84 , pp. 323-327
    • Liu, R.Y.1    Zhou, J.N.2    Van Heerikhuize, J.3
  • 10
    • 0033558327 scopus 로고    scopus 로고
    • Melatonin secretion rhythm disorders in patients with senile dementia of Alzheimer's type with disturbed sleep-waking
    • Mishima K, Tozawa T, Satoh K, et al. Melatonin secretion rhythm disorders in patients with senile dementia of Alzheimer's type with disturbed sleep-waking. Biol Psychiatry 1999; 45: 417-421.
    • (1999) Biol Psychiatry , vol.45 , pp. 417-421
    • Mishima, K.1    Tozawa, T.2    Satoh, K.3
  • 11
    • 0042090064 scopus 로고    scopus 로고
    • Early neuropathological Alzheimer's changes in aged individuals are accompanied by decreased cerebrospinal fluid melatonin levels
    • Zhou JN, Liu RY, Kamphorst W, et al. Early neuropathological Alzheimer's changes in aged individuals are accompanied by decreased cerebrospinal fluid melatonin levels. J Pineal Res 2003; 35: 125-130.
    • (2003) J Pineal Res , vol.35 , pp. 125-130
    • Zhou, J.N.1    Liu, R.Y.2    Kamphorst, W.3
  • 12
    • 0031981072 scopus 로고    scopus 로고
    • Amyloid-beta deposition in Alzheimer transgenic mice is associated with oxidative stress
    • Smith MA, Hirai K, Hsiao K, et al. Amyloid-beta deposition in Alzheimer transgenic mice is associated with oxidative stress. J Neurochem 1998; 70: 2212-2215.
    • (1998) J Neurochem , vol.70 , pp. 2212-2215
    • Smith, M.A.1    Hirai, K.2    Hsiao, K.3
  • 13
    • 79960380554 scopus 로고    scopus 로고
    • Melatonin is a natural ally against oxidative stress: A physiochemical examination
    • Galano A, Tan DX, Reiter RJ,. Melatonin is a natural ally against oxidative stress: a physiochemical examination. J Pineal Res 2011; 51: 1-16.
    • (2011) J Pineal Res , vol.51 , pp. 1-16
    • Galano, A.1    Tan, D.X.2    Reiter, R.J.3
  • 14
    • 84874949228 scopus 로고    scopus 로고
    • On the free radical scavenging activities of melatonin and its metabolites
    • Galano A, Tan DX, Reiter RJ,. On the free radical scavenging activities of melatonin and its metabolites. J Pineal Res 2013; 54: 245-257.
    • (2013) J Pineal Res , vol.54 , pp. 245-257
    • Galano, A.1    Tan, D.X.2    Reiter, R.J.3
  • 15
    • 84856718797 scopus 로고    scopus 로고
    • Alzheimer's disease: Pathological mechanisms and the beneficial role of melatonin
    • Rosales-Corral SA, Acuna-Castroviejo D, Cotomontes A, et al. Alzheimer's disease: pathological mechanisms and the beneficial role of melatonin. J Pineal Res 2012; 52: 167-202.
    • (2012) J Pineal Res , vol.52 , pp. 167-202
    • Rosales-Corral, S.A.1    Acuna-Castroviejo, D.2    Cotomontes, A.3
  • 16
    • 84880118137 scopus 로고    scopus 로고
    • Melatonin in Alzheimer's disease
    • Lin L, Huang QX, Yang SS, et al. Melatonin in Alzheimer's disease. Int J Mol Sci 2013; 14: 14575-14593.
    • (2013) Int J Mol Sci , vol.14 , pp. 14575-14593
    • Lin, L.1    Huang, Q.X.2    Yang, S.S.3
  • 17
    • 0032571381 scopus 로고    scopus 로고
    • Inhibition of Alzheimer β-fibrillogenesis by melatonin
    • Pappolla MA, Bozner P, Soto C, et al. Inhibition of Alzheimer β-fibrillogenesis by melatonin. J Biol Chem 1998; 273: 7185-7188.
    • (1998) J Biol Chem , vol.273 , pp. 7185-7188
    • Pappolla, M.A.1    Bozner, P.2    Soto, C.3
  • 18
    • 0031053554 scopus 로고    scopus 로고
    • Melatonin prevents death of neuroblastoma cells exposed to the Alzheimer amyloid peptide
    • Pappolla MA, Sos M, Omar RA, et al. Melatonin prevents death of neuroblastoma cells exposed to the Alzheimer amyloid peptide. J Neurosci 1997; 17: 1683-1690.
    • (1997) J Neurosci , vol.17 , pp. 1683-1690
    • Pappolla, M.A.1    Sos, M.2    Omar, R.A.3
  • 19
    • 4344568620 scopus 로고    scopus 로고
    • Melatonin alleviates behavioral deficits associated with apoptosis and cholinergic system dysfunction in the APP 695 transgenic mouse model of Alzheimer's disease
    • Feng Z, Chang Y, Cheng Y, et al. Melatonin alleviates behavioral deficits associated with apoptosis and cholinergic system dysfunction in the APP 695 transgenic mouse model of Alzheimer's disease. J Pineal Res 2004; 37: 129-136.
    • (2004) J Pineal Res , vol.37 , pp. 129-136
    • Feng, Z.1    Chang, Y.2    Cheng, Y.3
  • 20
    • 7444246751 scopus 로고    scopus 로고
    • Protective effect of melatonin on β-amyloid-induced apoptosis in rat astroglioma C6 cells and its mechanism
    • Feng Z, Zhang JT,. Protective effect of melatonin on β-amyloid-induced apoptosis in rat astroglioma C6 cells and its mechanism. Free Rad Biol Med 2004; 37: 1790-1801.
    • (2004) Free Rad Biol Med , vol.37 , pp. 1790-1801
    • Feng, Z.1    Zhang, J.T.2
  • 21
    • 18044386381 scopus 로고    scopus 로고
    • Melatonin attenuates amyloid beta25-35-induced apoptosis in mouse microglial BV2 cells
    • Jang MH, Jung SB, Lee MH, et al. Melatonin attenuates amyloid beta25-35-induced apoptosis in mouse microglial BV2 cells. Neurosci Lett 2005; 380: 26-31.
    • (2005) Neurosci Lett , vol.380 , pp. 26-31
    • Jang, M.H.1    Jung, S.B.2    Lee, M.H.3
  • 22
    • 0037565622 scopus 로고    scopus 로고
    • Melatonin increases survival and inhibits oxidative and amyloid pathology in a transgenic model of Alzheimer's disease
    • Matsubara E, Bryant-Thomas T, Pacheco Quinto J, et al. Melatonin increases survival and inhibits oxidative and amyloid pathology in a transgenic model of Alzheimer's disease. J Neurochem 2003; 85: 1101-1108.
    • (2003) J Neurochem , vol.85 , pp. 1101-1108
    • Matsubara, E.1    Bryant-Thomas, T.2    Pacheco Quinto, J.3
  • 23
    • 67649905028 scopus 로고    scopus 로고
    • Protection against cognitive deficits and markers of neurodegeneration by long-term oral administration of melatonin in a transgenic model of Alzheimer disease
    • Olcese JM, Cao C, Mori T, et al. Protection against cognitive deficits and markers of neurodegeneration by long-term oral administration of melatonin in a transgenic model of Alzheimer disease. J Pineal Res 2009; 47: 82-96.
    • (2009) J Pineal Res , vol.47 , pp. 82-96
    • Olcese, J.M.1    Cao, C.2    Mori, T.3
  • 24
    • 14944341045 scopus 로고    scopus 로고
    • Chronic melatonin therapy fails to alter amyloid burden or oxidative damage in old Tg2576 mice: Implication for clinical trials
    • Quinn J, Kulhanek D, Nowlin J, et al. Chronic melatonin therapy fails to alter amyloid burden or oxidative damage in old Tg2576 mice: implication for clinical trials. Brain Res 2005; 1037: 209-213.
    • (2005) Brain Res , vol.1037 , pp. 209-213
    • Quinn, J.1    Kulhanek, D.2    Nowlin, J.3
  • 25
    • 0032909996 scopus 로고    scopus 로고
    • Melatonin affects the metabolism of the β-amyloid precursor protein in different cell types
    • Lahiri DK,. Melatonin affects the metabolism of the β-amyloid precursor protein in different cell types. J Pineal Res 1999; 26: 137-146.
    • (1999) J Pineal Res , vol.26 , pp. 137-146
    • Lahiri, D.K.1
  • 26
    • 79955655453 scopus 로고    scopus 로고
    • Activation of the α-secretase processing of AβPP as a therapeutic approach in Alzheimer's disease
    • Vincent B, Govitrapong P,. Activation of the α-secretase processing of AβPP as a therapeutic approach in Alzheimer's disease. J Alzheimers Dis 2011; 24: 75-94.
    • (2011) J Alzheimers Dis , vol.24 , pp. 75-94
    • Vincent, B.1    Govitrapong, P.2
  • 27
    • 33344458827 scopus 로고    scopus 로고
    • M1 receptors play a central role in modulating AD-like pathology in transgenic mice
    • Caccamo A, Oddo S, Billings LM, et al. M1 receptors play a central role in modulating AD-like pathology in transgenic mice. Neuron 2006; 49: 671-682.
    • (2006) Neuron , vol.49 , pp. 671-682
    • Caccamo, A.1    Oddo, S.2    Billings, L.M.3
  • 28
    • 0031922631 scopus 로고    scopus 로고
    • In vitro stimulation of protein kinase C by melatonin
    • Anton-Tay F, Ramirez G, Martinez I, et al. In vitro stimulation of protein kinase C by melatonin. Neurochem Res 1998; 23: 601-606.
    • (1998) Neurochem Res , vol.23 , pp. 601-606
    • Anton-Tay, F.1    Ramirez, G.2    Martinez, I.3
  • 29
    • 0031022252 scopus 로고    scopus 로고
    • Proteasome contributes to the α-secretase pathway of amyloid precursor protein in human cells
    • Marambaud P, Chevallier N, Barelli H, et al. Proteasome contributes to the α-secretase pathway of amyloid precursor protein in human cells. J Neurochem 1997; 68: 698-703.
    • (1997) J Neurochem , vol.68 , pp. 698-703
    • Marambaud, P.1    Chevallier, N.2    Barelli, H.3
  • 30
    • 0034634655 scopus 로고    scopus 로고
    • Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons
    • Vincent B, Paitel E, Frobert Y, et al. Phorbol ester-regulated cleavage of normal prion protein in HEK293 human cells and murine neurons. J Biol Chem 2000; 275: 35612-35616.
    • (2000) J Biol Chem , vol.275 , pp. 35612-35616
    • Vincent, B.1    Paitel, E.2    Frobert, Y.3
  • 31
    • 0026476297 scopus 로고
    • Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors
    • Nitsch RM, Slack BE, Wurtman RJ, et al. Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors. Science 1992; 258: 304-307.
    • (1992) Science , vol.258 , pp. 304-307
    • Nitsch, R.M.1    Slack, B.E.2    Wurtman, R.J.3
  • 32
    • 0030293676 scopus 로고    scopus 로고
    • Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo
    • Borchelt DR, Thinakaran G, Eckman CB, et al. Familial Alzheimer's disease-linked presenilin 1 variants elevate Aβ1-42/1-40 ratio in vitro and in vivo. Neuron 1996; 17: 1005-1013.
    • (1996) Neuron , vol.17 , pp. 1005-1013
    • Borchelt, D.R.1    Thinakaran, G.2    Eckman, C.B.3
  • 33
    • 0036796421 scopus 로고    scopus 로고
    • The disintegrin/metalloprotease ADAM10 is essential for notch signaling but not for α-secretase activity in fibroblasts
    • Hartmann D, de Strooper B, Serneels L, et al. The disintegrin/metalloprotease ADAM10 is essential for notch signaling but not for α-secretase activity in fibroblasts. Hum Mol Genet 2002; 11: 2615-2624.
    • (2002) Hum Mol Genet , vol.11 , pp. 2615-2624
    • Hartmann, D.1    De Strooper, B.2    Serneels, L.3
  • 34
    • 8044257704 scopus 로고    scopus 로고
    • A metalloproteinase disintegrin that releases tumor-necrosis factor-alpha from cells
    • Black RA, Rauch CT, Kozlosky CJ, et al. A metalloproteinase disintegrin that releases tumor-necrosis factor-alpha from cells. Nature 1997; 385: 729-733.
    • (1997) Nature , vol.385 , pp. 729-733
    • Black, R.A.1    Rauch, C.T.2    Kozlosky, C.J.3
  • 35
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM,. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72: 248-259.
    • (1976) Anal Biochem , vol.72 , pp. 248-259
    • Bradford, M.M.1
  • 36
    • 33745747556 scopus 로고    scopus 로고
    • Design and characterization of a novel cellular prion-derived quenched fluorimetric substrate of α-secretase
    • Alfa Cisse M, Gandreuil C, Hernandez JF, et al. Design and characterization of a novel cellular prion-derived quenched fluorimetric substrate of α-secretase. Biochem Biophys Res Commun 2006; 347: 254-260.
    • (2006) Biochem Biophys Res Commun , vol.347 , pp. 254-260
    • Alfa Cisse, M.1    Gandreuil, C.2    Hernandez, J.F.3
  • 37
    • 24644483112 scopus 로고    scopus 로고
    • Genomic structure and functional characterization of the human ADAM10 promoter
    • Prinzen C, Muller U, Endres K, et al. Genomic structure and functional characterization of the human ADAM10 promoter. FASEB J 2005; 19: 1522-1524.
    • (2005) FASEB J , vol.19 , pp. 1522-1524
    • Prinzen, C.1    Muller, U.2    Endres, K.3
  • 38
    • 36348972454 scopus 로고    scopus 로고
    • Hypoxia-inducible factor mediates hypoxic and tumor necrosis factor α-induced increases in tumor necrosis factor-α converting enzyme/ADAM17 expression by synovial cells
    • Charbonneau M, Harper K, Grondin F, et al. Hypoxia-inducible factor mediates hypoxic and tumor necrosis factor α-induced increases in tumor necrosis factor-α converting enzyme/ADAM17 expression by synovial cells. J Biol Chem 2007; 282: 33714-33724.
    • (2007) J Biol Chem , vol.282 , pp. 33714-33724
    • Charbonneau, M.1    Harper, K.2    Grondin, F.3
  • 39
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease
    • Lammich S, Kojro E, Postina R, et al. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid precursor protein by a disintegrin metalloprotease. Proc Natl Acad Sci USA 1999; 96: 3922-3927.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3922-3927
    • Lammich, S.1    Kojro, E.2    Postina, R.3
  • 40
    • 14444272986 scopus 로고    scopus 로고
    • Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor
    • Buxbaum JD, Liu KN, Luo Y, et al. Evidence that tumor necrosis factor α converting enzyme is involved in regulated α-secretase cleavage of the Alzheimer amyloid protein precursor. J Biol Chem 1998; 273: 27765-27767.
    • (1998) J Biol Chem , vol.273 , pp. 27765-27767
    • Buxbaum, J.D.1    Liu, K.N.2    Luo, Y.3
  • 41
    • 84904037064 scopus 로고    scopus 로고
    • Understanding melatonin receptor pharmacology: Latest insights from mouse model, and their relevance to human disease
    • Tosini G, Owino S, Guillaume JL, et al. Understanding melatonin receptor pharmacology: latest insights from mouse model, and their relevance to human disease. BioEssays 2014; 36: 778-787.
    • (2014) BioEssays , vol.36 , pp. 778-787
    • Tosini, G.1    Owino, S.2    Guillaume, J.L.3
  • 42
    • 1842759592 scopus 로고    scopus 로고
    • Melatonin attenuates β-amyloid-induced inhibition of neurofilament expression
    • Zhang YC, Wang ZF, Wang Q, et al. Melatonin attenuates β-amyloid-induced inhibition of neurofilament expression. Acta Pharmacol Sin 2004; 25: 447-451.
    • (2004) Acta Pharmacol Sin , vol.25 , pp. 447-451
    • Zhang, Y.C.1    Wang, Z.F.2    Wang, Q.3
  • 43
    • 42149135452 scopus 로고    scopus 로고
    • Effect of melatonin and melatonylvalpromide on β-amyloid and neurofilaments in N2a cells
    • Wang XC, Zhang YC, Chatterjie N, et al. Effect of melatonin and melatonylvalpromide on β-amyloid and neurofilaments in N2a cells. Neurochem Res 2008; 33: 1138-1144.
    • (2008) Neurochem Res , vol.33 , pp. 1138-1144
    • Wang, X.C.1    Zhang, Y.C.2    Chatterjie, N.3
  • 44
    • 0034754471 scopus 로고    scopus 로고
    • Melatonin protects SHSY5Y neuroblastoma cells from cobalt-induced oxidative stress, neurotoxicity and increased β-amyloid secretion
    • Olivieri G, Hess C, Savaskan E, et al. Melatonin protects SHSY5Y neuroblastoma cells from cobalt-induced oxidative stress, neurotoxicity and increased β-amyloid secretion. J Pineal Res 2001; 31: 320-325.
    • (2001) J Pineal Res , vol.31 , pp. 320-325
    • Olivieri, G.1    Hess, C.2    Savaskan, E.3
  • 45
    • 77749336528 scopus 로고    scopus 로고
    • Amyloid-β neurotoxicity in organotypic culture is attenuated by melatonin: Involvement of GSK3β, tau and neuroinflammation
    • Bender Hoppe J, Frozza RL, Horn AP, et al. Amyloid-β neurotoxicity in organotypic culture is attenuated by melatonin: involvement of GSK3β, tau and neuroinflammation. J Pineal Res 2010; 48: 230-238.
    • (2010) J Pineal Res , vol.48 , pp. 230-238
    • Bender Hoppe, J.1    Frozza, R.L.2    Horn, A.P.3
  • 46
    • 79953193013 scopus 로고    scopus 로고
    • Mechanism of neuroprotection of melatonin against beta-amyloid neurotoxicity
    • Ionov M, Burchell V, Klajnert B, et al. Mechanism of neuroprotection of melatonin against beta-amyloid neurotoxicity. Neuroscience 2011; 180: 229-237.
    • (2011) Neuroscience , vol.180 , pp. 229-237
    • Ionov, M.1    Burchell, V.2    Klajnert, B.3
  • 47
    • 0035857757 scopus 로고    scopus 로고
    • Melatonin reduces interleukin secretion in amyloid-β stressed mouse brain slices
    • Clapp-Lilly KL, Smith MA, Perry G, et al. Melatonin reduces interleukin secretion in amyloid-β stressed mouse brain slices. Chem Biol Interact 2001; 134: 101-107.
    • (2001) Chem Biol Interact , vol.134 , pp. 101-107
    • Clapp-Lilly, K.L.1    Smith, M.A.2    Perry, G.3
  • 48
    • 1942435951 scopus 로고    scopus 로고
    • Dietary supplementation with melatonin reduces levels of amyloid beta-peptides in the murine cerebral cortex
    • Lahiri DK, Chen D, Ge YW, et al. Dietary supplementation with melatonin reduces levels of amyloid beta-peptides in the murine cerebral cortex. J Pineal Res 2004; 36: 224-231.
    • (2004) J Pineal Res , vol.36 , pp. 224-231
    • Lahiri, D.K.1    Chen, D.2    Ge, Y.W.3
  • 49
    • 0031243561 scopus 로고    scopus 로고
    • Melatonin alters the metabolism of the β-amyloid precursor protein in the neuroendocrine cell line PC12
    • Song W, Lahiri DK,. Melatonin alters the metabolism of the β-amyloid precursor protein in the neuroendocrine cell line PC12. J Mol Neurosci 1997; 9: 75-92.
    • (1997) J Mol Neurosci , vol.9 , pp. 75-92
    • Song, W.1    Lahiri, D.K.2
  • 50
    • 84905089096 scopus 로고    scopus 로고
    • Extrapineal melatonin: Sources, regulation, and potential functions
    • Acuna-Castroviejo D, Escames G, Venegas C, et al. Extrapineal melatonin: sources, regulation, and potential functions. Cell Mol Life Sci 2014; 71: 2997-3025.
    • (2014) Cell Mol Life Sci , vol.71 , pp. 2997-3025
    • Acuna-Castroviejo, D.1    Escames, G.2    Venegas, C.3
  • 51
  • 52
    • 0031582089 scopus 로고    scopus 로고
    • Identification of Mel1a melatonin receptors in the human embryonic kidney cell line HEK293: Evidence of G-protein-coupled melatonin receptors which do not mediate the inhibition of stimulated cyclic AMP levels
    • Conway S, Drew JE, Canning SJ, et al. Identification of Mel1a melatonin receptors in the human embryonic kidney cell line HEK293: evidence of G-protein-coupled melatonin receptors which do not mediate the inhibition of stimulated cyclic AMP levels. FEBS Lett 1997; 407: 121-126.
    • (1997) FEBS Lett , vol.407 , pp. 121-126
    • Conway, S.1    Drew, J.E.2    Canning, S.J.3
  • 53
    • 1342324047 scopus 로고    scopus 로고
    • Expression of membrane and nuclear melatonin receptors in mouse peripheral organs
    • Naji L, Carillo-Vico A, Guerrero JM, et al. Expression of membrane and nuclear melatonin receptors in mouse peripheral organs. Life Sci 2004; 74: 2227-2236.
    • (2004) Life Sci , vol.74 , pp. 2227-2236
    • Naji, L.1    Carillo-Vico, A.2    Guerrero, J.M.3
  • 54
    • 84899829773 scopus 로고    scopus 로고
    • Melatonin receptor type 1 signals to extracellular signal-regulated kinase 1 and 2 via Gi and Gs dually coupled pathways in HEK-293 cells
    • Chen L, He X, Zhang Y, et al. Melatonin receptor type 1 signals to extracellular signal-regulated kinase 1 and 2 via Gi and Gs dually coupled pathways in HEK-293 cells. Biochemistry 2014; 53: 2827-2839.
    • (2014) Biochemistry , vol.53 , pp. 2827-2839
    • Chen, L.1    He, X.2    Zhang, Y.3
  • 55
    • 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, et al. Hypoxia induces escape from innate immunity in cancer cells via increased expression of ADAM10: role of nitric oxide. Cancer Res 2011; 71: 7433-7441.
    • (2011) Cancer Res , vol.71 , pp. 7433-7441
    • Barsoum, I.B.1    Hamilton, T.K.2    Li, X.3
  • 56
    • 39149091686 scopus 로고    scopus 로고
    • Melatonin modulates the expression of VEGF and HIF-1α induced by CoCl2 in cultured cancer cells
    • Dai M, Cui P, Yu M, et al. Melatonin modulates the expression of VEGF and HIF-1α induced by CoCl2 in cultured cancer cells. J Pineal Res 2008; 44: 121-126.
    • (2008) J Pineal Res , vol.44 , pp. 121-126
    • Dai, M.1    Cui, P.2    Yu, M.3
  • 57
    • 64649100878 scopus 로고    scopus 로고
    • Melatonin down-regulates HIF-1α expression through inhibition of protein translation in prostate cancer cells
    • Park JW, Hwang MS, Suh SI, et al. Melatonin down-regulates HIF-1α expression through inhibition of protein translation in prostate cancer cells. J Pineal Res 2009; 46: 415-421.
    • (2009) J Pineal Res , vol.46 , pp. 415-421
    • Park, J.W.1    Hwang, M.S.2    Suh, S.I.3
  • 58
    • 75149158379 scopus 로고    scopus 로고
    • Melatonin suppresses tumor angiogenesis by inhibiting HIF-1α stabilization under hypoxia
    • Park SY, Jang WJ, Yi EY, et al. Melatonin suppresses tumor angiogenesis by inhibiting HIF-1α stabilization under hypoxia. J Pineal Res 2010; 48: 178-184.
    • (2010) J Pineal Res , vol.48 , pp. 178-184
    • Park, S.Y.1    Jang, W.J.2    Yi, E.Y.3
  • 59
    • 0029789643 scopus 로고    scopus 로고
    • Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase
    • Xing J, Ginty DD, Greenberg ME,. Coupling of the RAS-MAPK pathway to gene activation by RSK2, a growth factor-regulated CREB kinase. Science 1996; 273: 959-963.
    • (1996) Science , vol.273 , pp. 959-963
    • Xing, J.1    Ginty, D.D.2    Greenberg, M.E.3
  • 60
    • 17944369097 scopus 로고    scopus 로고
    • Involvement of the MAP kinase pathways in induction of GADD45 following UV radiation
    • Tong T, Fan W, Zhao H, et al. Involvement of the MAP kinase pathways in induction of GADD45 following UV radiation. Exp Cell Res 2001; 269: 64-72.
    • (2001) Exp Cell Res , vol.269 , pp. 64-72
    • Tong, T.1    Fan, W.2    Zhao, H.3
  • 61
    • 0032725554 scopus 로고    scopus 로고
    • P42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1
    • Richard DE, Berra E, Gothie E, et al. p42/p44 mitogen-activated protein kinases phosphorylate hypoxia-inducible factor 1α (HIF-1α) and enhance the transcriptional activity of HIF-1. J Biol Chem 1999; 174: 32631-32637.
    • (1999) J Biol Chem , vol.174 , pp. 32631-32637
    • Richard, D.E.1    Berra, E.2    Gothie, E.3
  • 62
    • 0034741796 scopus 로고    scopus 로고
    • Neuronal localization of the TNFα converting enzyme (TACE) in brain tissue and its correlation to amyloid plaques
    • Skovronski DM, Fath S, Lee VMY, et al. Neuronal localization of the TNFα converting enzyme (TACE) in brain tissue and its correlation to amyloid plaques. J Neurobiol 2001; 49: 40-46.
    • (2001) J Neurobiol , vol.49 , pp. 40-46
    • Skovronski, D.M.1    Fath, S.2    Lee, V.M.Y.3
  • 63
    • 0036042518 scopus 로고    scopus 로고
    • α-secretase ADAM10 as well as αaPPs is reduced in platelets and CSF of Alzheimer disease patients
    • Colciaghi F, Borroni B, Pastorino L, et al. α-secretase ADAM10 as well as αAPPs is reduced in platelets and CSF of Alzheimer disease patients. Mol Med 2002; 8: 67-74.
    • (2002) Mol Med , vol.8 , pp. 67-74
    • Colciaghi, F.1    Borroni, B.2    Pastorino, L.3
  • 64
    • 1042265051 scopus 로고    scopus 로고
    • Platelet APP, ADAM10 and BACE alterations in the early stages of Alzheimer disease
    • Colciaghi F, Marcello E, Borroni B, et al. Platelet APP, ADAM10 and BACE alterations in the early stages of Alzheimer disease. Neurology 2004; 62: 498-501.
    • (2004) Neurology , vol.62 , pp. 498-501
    • Colciaghi, F.1    Marcello, E.2    Borroni, B.3
  • 65
    • 0036161698 scopus 로고    scopus 로고
    • Increased melatonin 1a-receptor immunoreactivity in the hippocampus of Alzheimer's disease patients
    • Savaskan E, Olivieri G, Meier F, et al. Increased melatonin 1a-receptor immunoreactivity in the hippocampus of Alzheimer's disease patients. J Pineal Res 2002; 32: 59-62.
    • (2002) J Pineal Res , vol.32 , pp. 59-62
    • Savaskan, E.1    Olivieri, G.2    Meier, F.3
  • 66
    • 12344268788 scopus 로고    scopus 로고
    • Reduced hippocampal MT2 melatonin receptor expression in Alzheimer's disease
    • Savaskan E, Ayoub MA, Ravid R, et al. Reduced hippocampal MT2 melatonin receptor expression in Alzheimer's disease. J Pineal Res 2005; 38: 10-16.
    • (2005) J Pineal Res , vol.38 , pp. 10-16
    • Savaskan, E.1    Ayoub, M.A.2    Ravid, R.3
  • 67
    • 84907808578 scopus 로고    scopus 로고
    • Melatonin: Functions and ligands
    • Singh M, Jadhav HR,. Melatonin: functions and ligands. Drug Discov Today 2014; 19: 1410-1418.
    • (2014) Drug Discov Today , vol.19 , pp. 1410-1418
    • Singh, M.1    Jadhav, H.R.2
  • 68
    • 70350370474 scopus 로고    scopus 로고
    • Nuclear signaling by the APP intracellular domain occurs predominantly through the amyloidogenic processing pathway
    • Goodger ZV, Rajendran L, Trutzel A, et al. Nuclear signaling by the APP intracellular domain occurs predominantly through the amyloidogenic processing pathway. J Cell Sci 2009; 122: 3703-3714.
    • (2009) J Cell Sci , vol.122 , pp. 3703-3714
    • Goodger, Z.V.1    Rajendran, L.2    Trutzel, A.3
  • 69
    • 78650669822 scopus 로고    scopus 로고
    • The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a beta-secretase-dependent pathway
    • Belyaev ND, Kellett KA, Beckett C, et al. The transcriptionally active amyloid precursor protein (APP) intracellular domain is preferentially produced from the 695 isoform of APP in a beta-secretase-dependent pathway. J Biol Chem 2010; 285: 41443-41454.
    • (2010) J Biol Chem , vol.285 , pp. 41443-41454
    • Belyaev, N.D.1    Kellett, K.A.2    Beckett, C.3
  • 70
    • 84861497482 scopus 로고    scopus 로고
    • Evidence that the amyloid-β protein precursor intracellular domain, AICD, derives from β-secretase-generated C-terminal fragment
    • Flammang B, Pardossi-Piquard R, Sevalle J, et al. Evidence that the amyloid-β protein precursor intracellular domain, AICD, derives from β-secretase-generated C-terminal fragment. J Alzheimers Dis 2012; 30: 145-153.
    • (2012) J Alzheimers Dis , vol.30 , pp. 145-153
    • Flammang, B.1    Pardossi-Piquard, R.2    Sevalle, J.3
  • 71
    • 33845324145 scopus 로고    scopus 로고
    • C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3β expression
    • Kim HS, Kim EM, Lee JP, et al. C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3β expression. FASEB J 2003; 17: 1951-1953.
    • (2003) FASEB J , vol.17 , pp. 1951-1953
    • Kim, H.S.1    Kim, E.M.2    Lee, J.P.3
  • 72
    • 84875270977 scopus 로고    scopus 로고
    • Disease-modified glycogen synthase kinase-3β intervention by melatonin arrests the pathology and memory deficits in an Alzheimer's animal model
    • Peng CX, Hu J, Liu D, et al. Disease-modified glycogen synthase kinase-3β intervention by melatonin arrests the pathology and memory deficits in an Alzheimer's animal model. Neurobiol Aging 2013; 34: 1555-1563.
    • (2013) Neurobiol Aging , vol.34 , pp. 1555-1563
    • Peng, C.X.1    Hu, J.2    Liu, D.3
  • 73
    • 84885640190 scopus 로고    scopus 로고
    • Melatonin and the theories of aging is a critical appraisal of melatonin's role in antiaging mechanisms
    • Hardeland R,. Melatonin and the theories of aging is a critical appraisal of melatonin's role in antiaging mechanisms. J Pineal Res 2013; 55: 325-356.
    • (2013) J Pineal Res , vol.55 , pp. 325-356
    • Hardeland, R.1


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