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Volumn 1035, Issue , 2004, Pages 1-20

Targeting amyloid-degrading enzymes as therapeutic strategies in neurodegeneration

Author keywords

Alzheimer's disease; Amyloid peptide; Amyloid degrading enzymes; Endothelin converting enzyme; Insulin degrading enzyme; Neprilysin; Neurodegeneration; Plasmin

Indexed keywords

ALPHA SECRETASE; AMYLOID BETA PROTEIN; APOLIPOPROTEIN E4; ATRIAL NATRIURETIC FACTOR; BATIMASTAT; BETA SECRETASE; BOMBESIN; CARBACHOL; CHEMOTACTIC PEPTIDE; CORTICOTROPIN; ENDOTHELIN CONVERTING ENZYME; GAMMA SECRETASE; GELATINASE B; GUANOSINE TRIPHOSPHATASE; INSULINASE; MEMBRANE METALLOENDOPEPTIDASE; MEMBRANE PROTEIN; MUSCARINE; NICASTRIN; OPIATE PEPTIDE; PLASMIN; PRESENILIN 1; PRESENILIN 2; PROTEINASE ACTIVATED RECEPTOR 4; SERINE PROTEINASE; SUBSTANCE P; TACHYKININ; TAU PROTEIN;

EID: 14944344493     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1196/annals.1332.001     Document Type: Conference Paper
Times cited : (83)

References (128)
  • 1
    • 85047694415 scopus 로고    scopus 로고
    • Amyloid at the cutting edge: Activation of α-secretase prevents amyloidogenesis in an Alzheimer disease mouse model
    • LICHTENTHALER, S.F. & C. HAASS. 2004. Amyloid at the cutting edge: activation of α-secretase prevents amyloidogenesis in an Alzheimer disease mouse model. J. Clin. Invest. 113: 1384-1387.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1384-1387
    • Lichtenthaler, S.F.1    Haass, C.2
  • 2
    • 1542299128 scopus 로고    scopus 로고
    • Toward Alzheimer therapies based on genetic knowledge
    • HARDY, J. 2004. Toward Alzheimer therapies based on genetic knowledge. Annu. Rev. Med. 55: 15-25.
    • (2004) Annu. Rev. Med. , vol.55 , pp. 15-25
    • Hardy, J.1
  • 3
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • HARDY, J. & D. SELKOE. 2002. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297: 353-356.
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.2
  • 4
    • 1842555337 scopus 로고    scopus 로고
    • Alzheimer's amyloid-β (Aβ) is an essential synaptic protein, not neurotoxic junk
    • KOUDINOV, A.R. & T.T. BEREZOV. 2004. Alzheimer's amyloid-β (Aβ) is an essential synaptic protein, not neurotoxic junk. Acta Neurobiol. Exp. (Wars) 64: 71-79.
    • (2004) Acta Neurobiol. Exp. (Wars) , vol.64 , pp. 71-79
    • Koudinov, A.R.1    Berezov, T.T.2
  • 5
    • 0034681208 scopus 로고    scopus 로고
    • 2+ channel activity by β-amyloid-(1-40) in rat cortical synaptosomes and cultured cortical neurons. Modulation by the proinflammatory cytokine interleukin-1β
    • 2+ channel activity by β-amyloid-(1-40) in rat cortical synaptosomes and cultured cortical neurons. Modulation by the proinflammatory cytokine interleukin-1β. J. Biol. Chem. 275: 4713-4718.
    • (2000) J. Biol. Chem. , vol.275 , pp. 4713-4718
    • MacManus, A.1
  • 6
    • 2642550606 scopus 로고    scopus 로고
    • Enhanced G-protein activation by a mixture of Aβ(25-35), Aβ(1-40/42) and zinc
    • MOLNAR, Z. et al. 2004. Enhanced G-protein activation by a mixture of Aβ(25-35), Aβ(1-40/42) and zinc. J. Neurochem. 89: 1215-1223.
    • (2004) J. Neurochem. , vol.89 , pp. 1215-1223
    • Molnar, Z.1
  • 7
    • 0033616716 scopus 로고    scopus 로고
    • Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid protein by a disintegrin metalloprotease
    • LAMMICH, S. et al. 1999. Constitutive and regulated α-secretase cleavage of Alzheimer's amyloid 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
  • 8
    • 0032502033 scopus 로고    scopus 로고
    • Alzheimer's amyloid precursor protein α-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: Similarities to the angiotensin converting enzyme secretase
    • PARVATHY, S. et al. 1998. Alzheimer's amyloid precursor protein α-secretase is inhibited by hydroxamic acid-based zinc metalloprotease inhibitors: similarities to the angiotensin converting enzyme secretase. Biochemistry 37: 1680-1685.
    • (1998) Biochemistry , vol.37 , pp. 1680-1685
    • Parvathy, S.1
  • 9
    • 0026448114 scopus 로고
    • Cholinergic agonists and interleukin 1 regulated processing and secretion of the Alzheimer β/A4 amyloid protein precursor
    • BUXBAUM, J.D. et al. 1992. Cholinergic agonists and interleukin 1 regulated processing and secretion of the Alzheimer β/A4 amyloid protein precursor. Proc. Natl. Acad. Sci. USA 89: 10075-10078.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10075-10078
    • Buxbaum, J.D.1
  • 10
    • 0242330374 scopus 로고    scopus 로고
    • ADAMs family members as amyloid precursor protein α-secretases
    • ALLINSON, T.M. et al. 2003. ADAMs family members as amyloid precursor protein α-secretases. J. Neurosci. Res. 74: 342-352.
    • (2003) J. Neurosci. Res. , vol.74 , pp. 342-352
    • Allinson, T.M.1
  • 11
    • 0037097492 scopus 로고    scopus 로고
    • Muscarine enhances soluble amyloid precursor protein secretion in human neuroblastoma SH-SY5Y by a pathway dependent on protein kinase C(α), src-tyrosine kinase and extracellular signal-regulated kinase but not phospholipase C
    • CANET-AVILES, R.M. et al. 2002. Muscarine enhances soluble amyloid precursor protein secretion in human neuroblastoma SH-SY5Y by a pathway dependent on protein kinase C(α), src-tyrosine kinase and extracellular signal-regulated kinase but not phospholipase C. Brain Res. Mol. Brain Res. 102: 62-72.
    • (2002) Brain Res. Mol. Brain Res. , vol.102 , pp. 62-72
    • Canet-Aviles, R.M.1
  • 12
    • 0034809846 scopus 로고    scopus 로고
    • Protein kinase C ε suppresses Aβ production and promotes activation of α-secretase
    • ZHU, G. et al. 2001. Protein kinase C ε suppresses Aβ production and promotes activation of α-secretase. Biochem. Biophys. Res. Commun. 285: 997-1006.
    • (2001) Biochem. Biophys. Res. Commun. , vol.285 , pp. 997-1006
    • Zhu, G.1
  • 13
    • 85047690140 scopus 로고    scopus 로고
    • A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model
    • POSTINA, R. et al. 2004. A disintegrin-metalloproteinase prevents amyloid plaque formation and hippocampal defects in an Alzheimer disease mouse model. J. Clin. Invest. 113: 1456-1464.
    • (2004) J. Clin. Invest. , vol.113 , pp. 1456-1464
    • Postina, R.1
  • 14
    • 3943092621 scopus 로고    scopus 로고
    • Pathways towards and away from Alzheimer's disease
    • MATTSON, M. 2004. Pathways towards and away from Alzheimer's disease. Nature 430: 631-639.
    • (2004) Nature , vol.430 , pp. 631-639
    • Mattson, M.1
  • 15
    • 0033623415 scopus 로고    scopus 로고
    • Aβ-generating enzymes: Recent advances in β- and γ-secretase search
    • VASSAR, R., & M. CITRON. 2000. Aβ-generating enzymes: recent advances in β- and γ-secretase search. Neuron 27: 419-422.
    • (2000) Neuron , vol.27 , pp. 419-422
    • Vassar, R.1    Citron, M.2
  • 16
    • 4344630985 scopus 로고    scopus 로고
    • BACE1: The β-secretase enzyme in Alzheimer's disease
    • VASSAR, R. 2004. BACE1: the β-secretase enzyme in Alzheimer's disease. J. Mol. Neurosci. 23: 105-114.
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 105-114
    • Vassar, R.1
  • 17
    • 0035116273 scopus 로고    scopus 로고
    • Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation
    • LUO, Y. et al. 2001. Mice deficient in BACE1, the Alzheimer's β-secretase, have normal phenotype and abolished β-amyloid generation. Nat. Neurosci. 4: 231-232.
    • (2001) Nat. Neurosci. , vol.4 , pp. 231-232
    • Luo, Y.1
  • 18
    • 3242785569 scopus 로고    scopus 로고
    • Targeting BACE with small inhibitory nucleic acids - A future for Alzheimer's disease therapy?
    • NAWROT, B. 2004. Targeting BACE with small inhibitory nucleic acids-a future for Alzheimer's disease therapy? Acta Biochim. Pol. 51: 431-444.
    • (2004) Acta Biochim. Pol. , vol.51 , pp. 431-444
    • Nawrot, B.1
  • 19
    • 0141994826 scopus 로고    scopus 로고
    • Intramembrane-cleaving aspartic proteases and disease: Presenilins, signal peptide peptidase and their homologs
    • MARTOGLIO, B. & T.E. GOLDE. 2003. Intramembrane-cleaving aspartic proteases and disease: presenilins, signal peptide peptidase and their homologs. Hum. Mol. Genet. 12: R201-R206.
    • (2003) Hum. Mol. Genet. , vol.12
    • Martoglio, B.1    Golde, T.E.2
  • 20
    • 0037431082 scopus 로고    scopus 로고
    • Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex
    • DE STROOPER, B. 2003. Aph-1, Pen-2, and nicastrin with presenilin generate an active γ-secretase complex. Neuron 38: 9-12.
    • (2003) Neuron , vol.38 , pp. 9-12
    • De Strooper, B.1
  • 21
    • 0034647786 scopus 로고    scopus 로고
    • Oligomerization and toxicity of β-amyloid-42 implicated in Alzheimer's disease
    • EL-AGNAF, O.M. et al. 2000. Oligomerization and toxicity of β-amyloid-42 implicated in Alzheimer's disease. Biochem. Biophys. Res. Commun. 273: 1003-1007.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 1003-1007
    • El-Agnaf, O.M.1
  • 22
    • 0032981558 scopus 로고    scopus 로고
    • Mechanism of the cleavage specificity of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein
    • LICHTENTHALER, S.F. et al. 1999. Mechanism of the cleavage specificity of Alzheimer's disease γ-secretase identified by phenylalanine-scanning mutagenesis of the transmembrane domain of the amyloid precursor protein. Proc. Natl. Acad. Sci. USA 96: 3053-3058.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3053-3058
    • Lichtenthaler, S.F.1
  • 23
    • 0030779784 scopus 로고    scopus 로고
    • Skeletal and CNS defects in presenilin-1-deficient mice
    • SHEN, J. et al. 1997. Skeletal and CNS defects in presenilin-1-deficient mice. Cell 89: 629-639.
    • (1997) Cell , vol.89 , pp. 629-639
    • Shen, J.1
  • 24
    • 4744375540 scopus 로고    scopus 로고
    • Identification of distinct γ-secretase complexes with different APH-1 variants
    • Jul 30 [Epub ahead of print]
    • SHIROTANI, K. et al. 2004. Identification of distinct γ-secretase complexes with different APH-1 variants. J. Biol. Chem. Jul 30 [Epub ahead of print].
    • (2004) J. Biol. Chem.
    • Shirotani, K.1
  • 25
    • 0035824482 scopus 로고    scopus 로고
    • Signal transduction. RIPping tyrosine kinase receptors apart
    • HELDIN, C.H & J. ERICSSON. 2001. Signal transduction. RIPping tyrosine kinase receptors apart. Science 294: 2111-2113.
    • (2001) Science , vol.294 , pp. 2111-2113
    • Heldin, C.H.1    Ericsson, J.2
  • 26
    • 0035078659 scopus 로고    scopus 로고
    • Neurodegenerative disorders and ischemic brain diseases
    • MATTSON, M.P. et al. 2001. Neurodegenerative disorders and ischemic brain diseases. Apoptosis 6: 69-81.
    • (2001) Apoptosis , vol.6 , pp. 69-81
    • Mattson, M.P.1
  • 27
    • 3242737470 scopus 로고    scopus 로고
    • Challenging the amyloid cascade hypothesis: Senile plaques and amyloid-β as protective adaptations to Alzheimer disease
    • LEE, H.-G. et al. 2004, Challenging the amyloid cascade hypothesis: senile plaques and amyloid-β as protective adaptations to Alzheimer disease. Ann. N.Y. Acad. Sci. 1019: 1-4.
    • (2004) Ann. N.Y. Acad. Sci. , vol.1019 , pp. 1-4
    • Lee, H.-G.1
  • 28
    • 0035907123 scopus 로고    scopus 로고
    • Amyloid β protein 1-40 and 1-42 levels in matched cerebrospinal fluid and plasma from patients with Alzheimer disease
    • MEHTA, P.D. et al. 2001. Amyloid β protein 1-40 and 1-42 levels in matched cerebrospinal fluid and plasma from patients with Alzheimer disease. Neurosci. Lett. 304: 102-106.
    • (2001) Neurosci. Lett. , vol.304 , pp. 102-106
    • Mehta, P.D.1
  • 29
    • 0036450037 scopus 로고    scopus 로고
    • Cerebrovascular disease is a major factor in the failure of elimination of Aβ from the aging human brain
    • WELLER, R.O. et al. 2002. Cerebrovascular disease is a major factor in the failure of elimination of Aβ from the aging human brain. Ann. N. Y. Acad. SCi. 977: 162-168.
    • (2002) Ann. N. Y. Acad. SCi. , vol.977 , pp. 162-168
    • Weller, R.O.1
  • 30
    • 0036077536 scopus 로고    scopus 로고
    • β-amyloid catabolism: Role for neprilysin (NEP) and other metallopeptidases?
    • CARSON, J.A. & A.J. TURNER. 2002. β-Amyloid catabolism: role for neprilysin (NEP) and other metallopeptidases? J. Neurochem. 81: 1-8.
    • (2002) J. Neurochem. , vol.81 , pp. 1-8
    • Carson, J.A.1    Turner, A.J.2
  • 31
    • 0141621234 scopus 로고    scopus 로고
    • Kinetics of amyloid β-protein degradation determined by novel fluorescence- and fluorescence polarization-based assays
    • LEISSRING, M.A. et al. 2003. Kinetics of amyloid β-protein degradation determined by novel fluorescence- and fluorescence polarization-based assays. J. Biol. Chem. 278: 37314-37320.
    • (2003) J. Biol. Chem. , vol.278 , pp. 37314-37320
    • Leissring, M.A.1
  • 32
    • 0030899822 scopus 로고    scopus 로고
    • Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX
    • TURNER, A.J. & K. TANZAWA. 1997. Mammalian membrane metallopeptidases: NEP, ECE, KELL, and PEX. FASEB J. 11: 355-364.
    • (1997) FASEB J. , vol.11 , pp. 355-364
    • Turner, A.J.1    Tanzawa, K.2
  • 33
    • 0022877471 scopus 로고
    • An immunohistochemical study of endopeptidase-24.11 (" enkephalinase") in the pig nervous system
    • MATSAS, R., A.J. KENNY & A.J. TURNER. 1986. An immunohistochemical study of endopeptidase-24.11 ("enkephalinase") in the pig nervous system. Neuroscience 18: 991-1012.
    • (1986) Neuroscience , vol.18 , pp. 991-1012
    • Matsas, R.1    Kenny, A.J.2    Turner, A.J.3
  • 34
  • 35
    • 0025777822 scopus 로고
    • Neutral endopeptidase 24.11 in rat peripheral tissues: Comparative localization by "ex vivo" and "in vitro" autoradiography
    • SALES, N. et al. 1991. Neutral endopeptidase 24.11 in rat peripheral tissues: comparative localization by "ex vivo" and "in vitro" autoradiography. Regul. Pept. 33: 209-222.
    • (1991) Regul. Pept. , vol.33 , pp. 209-222
    • Sales, N.1
  • 36
    • 0023796690 scopus 로고
    • Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase
    • LETARTE, M. et al. 1988. Common acute lymphocytic leukemia antigen is identical to neutral endopeptidase. Exp. Med. 168: 1247-1253.
    • (1988) Exp. Med. , vol.168 , pp. 1247-1253
    • Letarte, M.1
  • 37
    • 0024520776 scopus 로고
    • The common acute lymphoblastic leukemia antigen (CD10)-emancipation from a functional enigma
    • LEBIEN, T.W. & R.T. MCCORMACK. 1989. The common acute lymphoblastic leukemia antigen (CD10)-emancipation from a functional enigma. Blood 73: 625-635
    • (1989) Blood , vol.73 , pp. 625-635
    • Lebien, T.W.1    McCormack, R.T.2
  • 38
    • 0025885695 scopus 로고
    • CD10/neutral endopeptidase 24.11 hydrolyzes bombesin-like peptides and regulates the growth of small cell carcinomas of the lung
    • SHIPP, M.A. et al. 1991. CD10/neutral endopeptidase 24.11 hydrolyzes bombesin-like peptides and regulates the growth of small cell carcinomas of the lung. Proc. Natl. Acad. Sci. USA 88: 10662-10666.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10662-10666
    • Shipp, M.A.1
  • 39
    • 0026556775 scopus 로고
    • Immunosuppression in the definitive and intermediate hosts of the human parasite Schistosoma mansoni by release of immunoreactive neuropeptides
    • DUVAUX-MIRET, O. et al. 1992. Immunosuppression in the definitive and intermediate hosts of the human parasite Schistosoma mansoni by release of immunoreactive neuropeptides. Proc. Natl. Acad. Sci. USA 89: 778-781.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 778-781
    • Duvaux-Miret, O.1
  • 40
    • 0028909535 scopus 로고
    • Effects of neuropeptides on human lung fibroblast proliferation and chemotaxis
    • HARRISON, N. K. et al. 1995. Effects of neuropeptides on human lung fibroblast proliferation and chemotaxis. Lung Cell. Mol. Physiol. 12: L278-L283.
    • (1995) Lung Cell. Mol. Physiol. , vol.12
    • Harrison, N.K.1
  • 41
    • 0027475050 scopus 로고
    • Neutral endopeptidase 24.11: Structure, inhibition, and experimental and clinical pharmacology
    • ROQUES, B.P. et al. 1993. Neutral endopeptidase 24.11: Structure, inhibition, and experimental and clinical pharmacology. Pharmacol. Rev. 45: 87-146.
    • (1993) Pharmacol. Rev. , vol.45 , pp. 87-146
    • Roques, B.P.1
  • 42
    • 0024538318 scopus 로고
    • Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones
    • ERDOS, E.G. & R.A. SKIDGEL. 1989. Neutral endopeptidase 24.11 (enkephalinase) and related regulators of peptide hormones. FASEB J. 3: 145-151.
    • (1989) FASEB J. , vol.3 , pp. 145-151
    • Erdos, E.G.1    Skidgel, R.A.2
  • 43
    • 0022295187 scopus 로고
    • Neutral endopeptidase 24.11 in human neutrophils: Cleavage of chemotactic peptide
    • CONNELLY, J.C. et al. 1985. Neutral endopeptidase 24.11 in human neutrophils: cleavage of chemotactic peptide. Proc. Natl. Acad. Sci. USA 82: 8737-8741.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 8737-8741
    • Connelly, J.C.1
  • 44
    • 0027051566 scopus 로고
    • Localization of the enzyme neutral endopeptidase to the human synovium
    • MAPP, P.I. et al. 1992. Localization of the enzyme neutral endopeptidase to the human synovium. J. Rheumatol. 19: 1838-1844.
    • (1992) J. Rheumatol. , vol.19 , pp. 1838-1844
    • Mapp, P.I.1
  • 45
    • 0023875732 scopus 로고
    • Effect of human endopeptidase 24.11 ("enkephalinase") on IL-1-induced thymocyte proliferation activity
    • PIERART, M.E. et al. 1988. Effect of human endopeptidase 24.11 ("enkephalinase") on IL-1-induced thymocyte proliferation activity. J. Immunol. 140: 3808-3811.
    • (1988) J. Immunol. , vol.140 , pp. 3808-3811
    • Pierart, M.E.1
  • 46
    • 0033621739 scopus 로고    scopus 로고
    • Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: Suppression leads to biochemical and pathological deposition
    • IWATA, N. et al. 2000. Identification of the major Aβ1-42-degrading catabolic pathway in brain parenchyma: suppression leads to biochemical and pathological deposition. Nat Med. 6: 143-150.
    • (2000) Nat Med. , vol.6 , pp. 143-150
    • Iwata, N.1
  • 47
    • 0141907379 scopus 로고    scopus 로고
    • Alzheimer's disease, neuropeptides, neuropeptidase, and amyloid-β peptide metabolism
    • SAITO, T. et al. 2003. Alzheimer's disease, neuropeptides, neuropeptidase, and amyloid-β peptide metabolism. Sci. Aging Knowledge Environ. 3: PE1.
    • (2003) Sci. Aging Knowledge Environ. , vol.3
    • Saito, T.1
  • 48
    • 0035877747 scopus 로고    scopus 로고
    • Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases
    • SHIROTANI, K. et al. 2001. Neprilysin degrades both amyloid β peptides 1-40 and 1-42 most rapidly and efficiently among thiorphan- and phosphoramidon-sensitive endopeptidases. J. Biol. Chem. 276: 21895-21901.
    • (2001) J. Biol. Chem. , vol.276 , pp. 21895-21901
    • Shirotani, K.1
  • 49
    • 0042827324 scopus 로고    scopus 로고
    • Human neprilysin is capable of degrading amyloid β peptide not only in the monomeric form, but also the pathological oligomeric form
    • KANEMITSU, H. et al. 2003. Human neprilysin is capable of degrading amyloid β peptide not only in the monomeric form, but also the pathological oligomeric form. Neurosci. Lett. 350: 113-116.
    • (2003) Neurosci. Lett. , vol.350 , pp. 113-116
    • Kanemitsu, H.1
  • 50
    • 0035846826 scopus 로고    scopus 로고
    • Reduced neprilysin in high plaque areas of Alzheimer brain: A possible relationship to deficient degradation of β-amyloid peptide
    • YASOJIMA, K. et al. 2001. Reduced neprilysin in high plaque areas of Alzheimer brain: a possible relationship to deficient degradation of β-amyloid peptide. Neurosci. Lett. 297: 97-100.
    • (2001) Neurosci. Lett. , vol.297 , pp. 97-100
    • Yasojima, K.1
  • 51
    • 0026741209 scopus 로고
    • Membrane localization of endopeptidase-24.11 and peptidyl dipeptidase a (angiotensin converting enzyme) in the pig brain: A study using subcellular fractionation and electron microscopic immunocytochemistry
    • BARNES, K., A.J. TURNER & A.J. KENNY. 1992. Membrane localization of endopeptidase-24.11 and peptidyl dipeptidase A (angiotensin converting enzyme) in the pig brain: a study using subcellular fractionation and electron microscopic immunocytochemistry. J. Neurochem. 58: 2088-2096.
    • (1992) J. Neurochem. , vol.58 , pp. 2088-2096
    • Barnes, K.1    Turner, A.J.2    Kenny, A.J.3
  • 52
    • 0037010286 scopus 로고    scopus 로고
    • Region-specific reduction of Aβ-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging
    • IWATA, N. et al. 2002. Region-specific reduction of Aβ-degrading endopeptidase, neprilysin, in mouse hippocampus upon aging. J. Neurosci. Res. 70: 493-500.
    • (2002) J. Neurosci. Res. , vol.70 , pp. 493-500
    • Iwata, N.1
  • 53
    • 14944358001 scopus 로고    scopus 로고
    • Effects of prenatal hypoxia on expression of amyloid precursor protein and metallopeptidases in the rat brain
    • NALIVAEVA, N.N. et al. 2004. Effects of prenatal hypoxia on expression of amyloid precursor protein and metallopeptidases in the rat brain. Lett. Peptide Sci. 10: 455-462.
    • (2004) Lett. Peptide Sci. , vol.10 , pp. 455-462
    • Nalivaeva, N.N.1
  • 54
    • 14944380978 scopus 로고    scopus 로고
    • Effect of hypoxia/ischaemia and hypoxic preconditioning/reperfusion on expression of some amyloid degrading enzymes
    • This volume
    • NALIVAEVA, N.N. et al. 2004. Effect of hypoxia/ischaemia and hypoxic preconditioning/reperfusion on expression of some amyloid degrading enzymes. Ann. N.Y. Acad. Sci. This volume.
    • (2004) Ann. N.Y. Acad. Sci.
    • Nalivaeva, N.N.1
  • 55
    • 0037468588 scopus 로고    scopus 로고
    • Ageing-related downregulation of neprilysin, a putative β-amyloid-degrading enzyme, in transgenic Tg2576 Alzheimer-like mouse brain is accompanied by an astroglial upregulation in the vicinity of β-amyloid plaques
    • APELT, J., K. ACH & R. SCHLIEBS. 2003. Ageing-related downregulation of neprilysin, a putative β-amyloid-degrading enzyme, in transgenic Tg2576 Alzheimer-like mouse brain is accompanied by an astroglial upregulation in the vicinity of β-amyloid plaques. Neurosci. Lett. 339: 183-186.
    • (2003) Neurosci. Lett. , vol.339 , pp. 183-186
    • Apelt, J.1    Ach, K.2    Schliebs, R.3
  • 56
    • 12144286112 scopus 로고    scopus 로고
    • Association of the neprilysin gene with susceptibility to late-onset Alzheimer's disease
    • SAKAI, A. et al. 2004. Association of the neprilysin gene with susceptibility to late-onset Alzheimer's disease. Dement. Geriatr. Cogn. Disord. 17: 164-169.
    • (2004) Dement. Geriatr. Cogn. Disord. , vol.17 , pp. 164-169
    • Sakai, A.1
  • 57
    • 0037421496 scopus 로고    scopus 로고
    • No association between polymorphisms in the neprilysin promoter region and Swedish Alzheimer's disease patients
    • LILIUS, L. et al. 2003. No association between polymorphisms in the neprilysin promoter region and Swedish Alzheimer's disease patients. Neurosci. Lett. 337: 111-113.
    • (2003) Neurosci. Lett. , vol.337 , pp. 111-113
    • Lilius, L.1
  • 58
    • 0036498998 scopus 로고    scopus 로고
    • Dinucleotide repeat polymorphisms in the neprilysin gene are not associated with sporadic Alzheimer's disease
    • ODA, M. et al. 2002. Dinucleotide repeat polymorphisms in the neprilysin gene are not associated with sporadic Alzheimer's disease. Neurosci. Lett. 320: 105-107.
    • (2002) Neurosci. Lett. , vol.320 , pp. 105-107
    • Oda, M.1
  • 59
    • 0037466757 scopus 로고    scopus 로고
    • Ontogeny, regional and cellular distribution of the novel metalloprotease neprilysin 2 in the rat: A comparison with neprilysin and endothelin-converting enzyme-1
    • FACCHINETTI, P. et al. 2003. Ontogeny, regional and cellular distribution of the novel metalloprotease neprilysin 2 in the rat: a comparison with neprilysin and endothelin-converting enzyme-1. Neuroscience 118: 627-639.
    • (2003) Neuroscience , vol.118 , pp. 627-639
    • Facchinetti, P.1
  • 60
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • LEISSRING. M.A. et al. 2003. Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40: 1087-1093.
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1
  • 61
    • 0031690490 scopus 로고    scopus 로고
    • Insulin degradation: Progress and potential
    • DUCKWORTH, W.C., R.G. BENNETT & F.G. HAMEL. 1998. Insulin degradation: progress and potential. Endocr. Rev. 19: 608-624.
    • (1998) Endocr. Rev. , vol.19 , pp. 608-624
    • Duckworth, W.C.1    Bennett, R.G.2    Hamel, F.G.3
  • 62
    • 0031550507 scopus 로고    scopus 로고
    • Overexpression of insulin degrading enzyme: Cellular localization and effects on insulin signaling
    • SETA, K.A. & R.A. ROTH. 1997. Overexpression of insulin degrading enzyme: cellular localization and effects on insulin signaling. Biochem. Biophys. Res. Commun. 231: 167-171.
    • (1997) Biochem. Biophys. Res. Commun. , vol.231 , pp. 167-171
    • Seta, K.A.1    Roth, R.A.2
  • 63
    • 0034161516 scopus 로고    scopus 로고
    • Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme
    • VEKRELLIS, K. et al. 2000. Neurons regulate extracellular levels of amyloid β-protein via proteolysis by insulin-degrading enzyme. J. Neurosci. 20: 1657-1665.
    • (2000) J. Neurosci. , vol.20 , pp. 1657-1665
    • Vekrellis, K.1
  • 64
    • 0000398342 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates extracellular levels of amyloid β-protein by degradation
    • QIU, W.Q. et al. 1998. Insulin-degrading enzyme regulates extracellular levels of amyloid β-protein by degradation. J. Biol. Chem. 273: 32730-32738.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32730-32738
    • Qiu, W.Q.1
  • 65
    • 9144260111 scopus 로고    scopus 로고
    • Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria
    • Epub ahead of print
    • LEISSRING, M.A. et al. 2004. Alternative translation initiation generates a novel isoform of insulin-degrading enzyme targeted to mitochondria. Biochem. J. [Epub ahead of print.]
    • (2004) Biochem. J.
    • Leissring, M.A.1
  • 66
    • 0028176821 scopus 로고
    • Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme
    • KUROCHKIN, I.V. & S. GOTO. 1994. Alzheimer's β-amyloid peptide specifically interacts with and is degraded by insulin degrading enzyme. FEBS Lett. 345: 33-37.
    • (1994) FEBS Lett. , vol.345 , pp. 33-37
    • Kurochkin, I.V.1    Goto, S.2
  • 67
    • 0035399887 scopus 로고    scopus 로고
    • Insulin-degrading enzyme: Embarking on amyloid destruction
    • KUROCHKIN, I.V. 2001. Insulin-degrading enzyme: embarking on amyloid destruction. Trends Biochem. Sci. 26: 421-425.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 421-425
    • Kurochkin, I.V.1
  • 68
    • 0034038036 scopus 로고    scopus 로고
    • Degradation of soluble amyloid β-peptides 1-40, 1-42, and the Dutch variant 1-40Q by insulin degrading enzyme from Alzheimer disease and control brains
    • PEREZ, A. et al. 2000. Degradation of soluble amyloid β-peptides 1-40, 1-42, and the Dutch variant 1-40Q by insulin degrading enzyme from Alzheimer disease and control brains. Neurochem. Res. 2: 247-255.
    • (2000) Neurochem. Res. , vol.2 , pp. 247-255
    • Perez, A.1
  • 69
    • 0346101885 scopus 로고    scopus 로고
    • Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death
    • LEISSRING, M.A. et al. 2003. Enhanced proteolysis of β-amyloid in APP transgenic mice prevents plaque formation, secondary pathology, and premature death. Neuron 40: 1087-1093.
    • (2003) Neuron , vol.40 , pp. 1087-1093
    • Leissring, M.A.1
  • 70
    • 0030610902 scopus 로고    scopus 로고
    • 125I]insulin receptor binding sites in the hippocampus of aged memory-unimpaired and -impaired rats
    • 125I]insulin receptor binding sites in the hippocampus of aged memory-unimpaired and -impaired rats. Neuroscience 80: 1033-1040.
    • (1997) Neuroscience , vol.80 , pp. 1033-1040
    • Dore, S.1
  • 71
    • 12244312497 scopus 로고    scopus 로고
    • Cortical glucose metabolism is altered in aged transgenic Tg2576 mice that demonstrate Alzheimer plaque pathology
    • BIGL, M. et al. 2003. Cortical glucose metabolism is altered in aged transgenic Tg2576 mice that demonstrate Alzheimer plaque pathology. J. Neural. Transm. 110: 77-94.
    • (2003) J. Neural. Transm. , vol.110 , pp. 77-94
    • Bigl, M.1
  • 72
    • 0036813726 scopus 로고    scopus 로고
    • Amyloid β antagonizes insulin promoted secretion of the amyloid β protein precursor
    • LING, X. et al. 2002. Amyloid β antagonizes insulin promoted secretion of the amyloid β protein precursor. J. Alzheimers Dis. 4: 369-374.
    • (2002) J. Alzheimers Dis. , vol.4 , pp. 369-374
    • Ling, X.1
  • 73
    • 18744438248 scopus 로고    scopus 로고
    • Alzheimer's β-amyloid peptides compete for insulin binding to the insulin receptor
    • XIE, L. et al. 2002. Alzheimer's β-amyloid peptides compete for insulin binding to the insulin receptor. J. Neurosci. 22: RC221.
    • (2002) J. Neurosci. , vol.22
    • Xie, L.1
  • 74
    • 0037390039 scopus 로고    scopus 로고
    • Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo
    • FARRIS, W. et al. 2003. Insulin-degrading enzyme regulates the levels of insulin, amyloid β-protein, and the β-amyloid precursor protein intracellular domain in vivo. Proc. Natl. Acad. Sci. USA 100: 4162-4167.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4162-4167
    • Farris, W.1
  • 75
    • 1642290835 scopus 로고    scopus 로고
    • Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid β-protein
    • FARRIS, W. et al. 2004. Partial loss-of-function mutations in insulin-degrading enzyme that induce diabetes also impair degradation of amyloid β-protein. Am. J. Pathol. 164: 1425-1434.
    • (2004) Am. J. Pathol. , vol.164 , pp. 1425-1434
    • Farris, W.1
  • 76
    • 4644286910 scopus 로고    scopus 로고
    • Diet-induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease
    • HO, L. et al. 2004. Diet-induced insulin resistance promotes amyloidosis in a transgenic mouse model of Alzheimer's disease. FASEB J. 18: 902-904.
    • (2004) FASEB J. , vol.18 , pp. 902-904
    • Ho, L.1
  • 77
    • 1042292018 scopus 로고    scopus 로고
    • Endoplasmic reticulum-localized amyloid β-peptide is degraded in the cytosol by two distinct degradation pathways
    • SCHMITZ, A. et al. 2004. Endoplasmic reticulum-localized amyloid β-peptide is degraded in the cytosol by two distinct degradation pathways. Traffic 5: 89-101.
    • (2004) Traffic , vol.5 , pp. 89-101
    • Schmitz, A.1
  • 78
    • 1542752823 scopus 로고    scopus 로고
    • Does diabetes protect or provoke Alzheimer's disease? Insights into the pathobiology and future treatment of Alzheimer's disease
    • GROSSMAN, H. 2003. Does diabetes protect or provoke Alzheimer's disease? Insights into the pathobiology and future treatment of Alzheimer's disease. CNS Spectr. 8: 815-823.
    • (2003) CNS Spectr. , vol.8 , pp. 815-823
    • Grossman, H.1
  • 79
    • 0242321663 scopus 로고    scopus 로고
    • Genetic variation in a haplotype block spanning IDE influences Alzheimer disease
    • PRINCE, J.A. et al. 2003. Genetic variation in a haplotype block spanning IDE influences Alzheimer disease. Hum. Mutat. 22: 363-371.
    • (2003) Hum. Mutat. , vol.22 , pp. 363-371
    • Prince, J.A.1
  • 80
    • 0037162647 scopus 로고    scopus 로고
    • Polymorphisms of insulin degrading enzyme gene are not associated with Alzheimer's disease
    • BOUSSAHA, M. et al. 2002. Polymorphisms of insulin degrading enzyme gene are not associated with Alzheimer's disease. Neurosci. Lett. 329: 121-123.
    • (2002) Neurosci. Lett. , vol.329 , pp. 121-123
    • Boussaha, M.1
  • 81
    • 3042675764 scopus 로고    scopus 로고
    • Sequence variation in the proximity of IDE may impact age at onset of both Parkinson disease and Alzheimer disease
    • BLOMQVIST, M.E. et al. 2004. Sequence variation in the proximity of IDE may impact age at onset of both Parkinson disease and Alzheimer disease. Neurogenetics 5: 115-119.
    • (2004) Neurogenetics , vol.5 , pp. 115-119
    • Blomqvist, M.E.1
  • 82
    • 0033030332 scopus 로고    scopus 로고
    • The endothelin converting enzyme is located on α-actin filaments in smooth muscle cells
    • BARNES, K. & A.J. TURNER. 1999. The endothelin converting enzyme is located on α-actin filaments in smooth muscle cells. Cardiovasc. Res. 42: 814-822.
    • (1999) Cardiovasc. Res. , vol.42 , pp. 814-822
    • Barnes, K.1    Turner, A.J.2
  • 83
    • 0030791618 scopus 로고    scopus 로고
    • The endothelin system and endothelin-converting enzyme in the brain: Molecular and cellular studies
    • BARNES, K & A.J. TURNER. 1997. The endothelin system and endothelin-converting enzyme in the brain: molecular and cellular studies. Neurochem. Res. 22: 1033-1040.
    • (1997) Neurochem. Res. , vol.22 , pp. 1033-1040
    • Barnes, K.1    Turner, A.J.2
  • 84
    • 0029585975 scopus 로고
    • Organization of the gene encoding the human endothelin-converting enzyme (ECE-1)
    • VALDENAIRE, O., E. ROHRBACHER & M.G. MATTEL 1995. Organization of the gene encoding the human endothelin-converting enzyme (ECE-1). J. Biol. Chem. 270: 29794-2978.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29794-32978
    • Valdenaire, O.1    Rohrbacher, E.2    Mattel, M.G.3
  • 85
    • 0031440109 scopus 로고    scopus 로고
    • Human endothelin-converting enzyme (ECE-1): Three isoforms with distinct subcellular localizations
    • SCHWEIZER, A. et al. 1997. Human endothelin-converting enzyme (ECE-1): three isoforms with distinct subcellular localizations. Biochem. J. 328: 871-877.
    • (1997) Biochem. J. , vol.328 , pp. 871-877
    • Schweizer, A.1
  • 86
    • 0030700341 scopus 로고    scopus 로고
    • Novel activity for endothelin-converting enzyme: Hydrolysis of bradykinin
    • HOANG, M.V. & A.J. TURNER. 1997. Novel activity for endothelin-converting enzyme: hydrolysis of bradykinin. Biochem. J. 327: 23-26.
    • (1997) Biochem. J. , vol.327 , pp. 23-26
    • Hoang, M.V.1    Turner, A.J.2
  • 87
    • 0029017876 scopus 로고
    • Endothelin-converting enzyme-2 is a membrane-bound, phorphoramidon- sensitive metalloprotease with acidic pH optimum
    • EMOTO, N. & M. YANAGISAWA. 1995. Endothelin-converting enzyme-2 is a membrane-bound, phorphoramidon-sensitive metalloprotease with acidic pH optimum. J. Biol. Chem. 270: 15262-15268.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15262-15268
    • Emoto, N.1    Yanagisawa, M.2
  • 88
    • 0035816707 scopus 로고    scopus 로고
    • Degradation of the Alzheimer's amyloid β peptide by endothelin-converting enzyme
    • ECKMAN, E.A., D.K. REED & C.B. ECKMAN. 2001. Degradation of the Alzheimer's amyloid β peptide by endothelin-converting enzyme. J. Biol. Chem. 276: 24540-24548.
    • (2001) J. Biol. Chem. , vol.276 , pp. 24540-24548
    • Eckman, E.A.1    Reed, D.K.2    Eckman, C.B.3
  • 89
    • 0037462769 scopus 로고    scopus 로고
    • Alzheimer's disease β-amyloid peptide is increased in mice deficient in endothelin-converting enzyme
    • ECKMAN, E.A. et al. 2003. Alzheimer's disease β-amyloid peptide is increased in mice deficient in endothelin-converting enzyme. J. Biol. Chem. 278: 2081-2084.
    • (2003) J. Biol. Chem. , vol.278 , pp. 2081-2084
    • Eckman, E.A.1
  • 90
    • 0030715322 scopus 로고    scopus 로고
    • ECM and cell surface proteolysis: Regulating cellular ecology
    • WERB, Z. 1997. ECM and cell surface proteolysis: regulating cellular ecology. Cell 91: 439-442.
    • (1997) Cell , vol.91 , pp. 439-442
    • Werb, Z.1
  • 92
    • 0034161441 scopus 로고    scopus 로고
    • Laminin degradation by plasmin regulates long-term potentiation
    • NAKAGAMI, Y. et al. 2000. Laminin degradation by plasmin regulates long-term potentiation. J. Neurosci. 20: 2003-2010.
    • (2000) J. Neurosci. , vol.20 , pp. 2003-2010
    • Nakagami, Y.1
  • 93
    • 0037833494 scopus 로고    scopus 로고
    • Emotions are building up in the field of extracellular proteolysis
    • MADANI, R., S. NEF & J.D. VASSALLI. 2003. Emotions are building up in the field of extracellular proteolysis. Trends Mol. Med. 9: 183-185.
    • (2003) Trends Mol. Med. , vol.9 , pp. 183-185
    • Madani, R.1    Nef, S.2    Vassalli, J.D.3
  • 94
    • 0034602091 scopus 로고    scopus 로고
    • Plasminogen activation in experimental permanent focal cerebral ischemia
    • PFEFFERKORN, T. et al. 2000. Plasminogen activation in experimental permanent focal cerebral ischemia. Brain Res. 882: 19-25.
    • (2000) Brain Res. , vol.882 , pp. 19-25
    • Pfefferkorn, T.1
  • 95
    • 0034573026 scopus 로고    scopus 로고
    • Brain plasmin enhances APP α-cleavage and Aβ degradation and is reduced in Alzheimer's disease brains
    • LEDESMA, M.D. et al. 2000. Brain plasmin enhances APP α-cleavage and Aβ degradation and is reduced in Alzheimer's disease brains. EMBO Rep. 1: 530-535.
    • (2000) EMBO Rep. , vol.1 , pp. 530-535
    • Ledesma, M.D.1
  • 96
    • 0346463111 scopus 로고    scopus 로고
    • Raft disorganization leads to reduced plasmin activity in Alzheimer's disease brains
    • LEDESMA, M.D. et al. 2003. Raft disorganization leads to reduced plasmin activity in Alzheimer's disease brains. EMBO Rep. 4: 1190-1196.
    • (2003) EMBO Rep. , vol.4 , pp. 1190-1196
    • Ledesma, M.D.1
  • 97
    • 0033621048 scopus 로고    scopus 로고
    • Plasmin cleavage of the amyloid β-protein: Alteration of secondary structure and stimulation of tissue plasminogen activator activity
    • VAN NOSTRAND, W.E. & M. PORTER. 1999. Plasmin cleavage of the amyloid β-protein: alteration of secondary structure and stimulation of tissue plasminogen activator activity. Biochemistry 38: 11570-11576.
    • (1999) Biochemistry , vol.38 , pp. 11570-11576
    • Van Nostrand, W.E.1    Porter, M.2
  • 98
    • 18544410708 scopus 로고    scopus 로고
    • The plasmin system is induced by and degrades amyloid-β aggregates
    • TUCKER, H.M. et al. 2000. The plasmin system is induced by and degrades amyloid-β aggregates. J. Neurosci. 20: 3937-3946.
    • (2000) J. Neurosci. , vol.20 , pp. 3937-3946
    • Tucker, H.M.1
  • 99
    • 0033788789 scopus 로고    scopus 로고
    • Tissue plasminogen activator requires plasminogen to modulate amyloid-β neurotoxicity and deposition
    • TUCKER, H.M. et al. 2000. Tissue plasminogen activator requires plasminogen to modulate amyloid-β neurotoxicity and deposition. J. Neurochem. 75: 2172-2177.
    • (2000) J. Neurochem. , vol.75 , pp. 2172-2177
    • Tucker, H.M.1
  • 100
    • 0142106462 scopus 로고    scopus 로고
    • Proteomic characterisation of neuronal sphingolipid-cholesterol microdomains: Role in plasminogen activation
    • LEDESMA, M.D. et al. 2003. Proteomic characterisation of neuronal sphingolipid-cholesterol microdomains: role in plasminogen activation. Brain Res. 987: 107-116.
    • (2003) Brain Res. , vol.987 , pp. 107-116
    • Ledesma, M.D.1
  • 101
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts
    • EHEHALT, R. et al. 2003. Amyloidogenic processing of the Alzheimer β-amyloid precursor protein depends on lipid rafts. J. Cell Biol. 160: 113-123.
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1
  • 102
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein
    • CORDY, J.M. et al. 2003. Exclusively targeting β-secretase to lipid rafts by GPI-anchor addition up-regulates β-site processing of the amyloid precursor protein. Proc. Natl. Acad. Sci. USA 100: 11735-11740.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 11735-11740
    • Cordy, J.M.1
  • 103
    • 0028928084 scopus 로고
    • In vitro stimulation of tissue-type plasminogen activator by Alzheimer amyloid β-peptide analogues
    • KINGSTON, I.B., M.J.M. CASTRO & S.A. ANDERSON. 1995. In vitro stimulation of tissue-type plasminogen activator by Alzheimer amyloid β-peptide analogues. Nat. Med. 1: 138-142.
    • (1995) Nat. Med. , vol.1 , pp. 138-142
    • Kingston, I.B.1    Castro, M.J.M.2    Anderson, S.A.3
  • 104
    • 0034703979 scopus 로고    scopus 로고
    • Linkage of plasma Aβ42 to a quantitative locus on chromosome 10 in late-onset Alzheimer's disease pedigrees
    • ERTEKIN-TANER, N. et al. 2000. Linkage of plasma Aβ42 to a quantitative locus on chromosome 10 in late-onset Alzheimer's disease pedigrees. Science 290: 2303-2304.
    • (2000) Science , vol.290 , pp. 2303-2304
    • Ertekin-Taner, N.1
  • 105
    • 0037107974 scopus 로고    scopus 로고
    • Urokinase-type plasminogen activator inhibits amyloid-β neurotoxicity and fibrillogenesis via plasminogen
    • TUCKER, H.M., M. KIHIKO-EHMANN & S. ESTUS. 2002. Urokinase-type plasminogen activator inhibits amyloid-β neurotoxicity and fibrillogenesis via plasminogen. J. Neurosci. Res. 70: 249-255.
    • (2002) J. Neurosci. Res. , vol.70 , pp. 249-255
    • Tucker, H.M.1    Kihiko-Ehmann, M.2    Estus, S.3
  • 106
    • 0035930538 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme degrades Alzheimer amyloid β-peptide (Aβ); retards Aβ aggregation, deposition, fibril formation; and inhibits cytotoxicity
    • HU, J. et al. 2001. Angiotensin-converting enzyme degrades Alzheimer amyloid β-peptide (Aβ); retards Aβ aggregation, deposition, fibril formation; and inhibits cytotoxicity. J. Biol. Chem. 276: 47863-47868.
    • (2001) J. Biol. Chem. , vol.276 , pp. 47863-47868
    • Hu, J.1
  • 107
    • 0029852887 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1-40)
    • BACKSTROM, J.R. et al. 1996. Matrix metalloproteinase-9 (MMP-9) is synthesized in neurons of the human hippocampus and is capable of degrading the amyloid-β peptide (1-40). J. Neurosci. 16: 7910-7919.
    • (1996) J. Neurosci. , vol.16 , pp. 7910-7919
    • Backstrom, J.R.1
  • 108
    • 0345060484 scopus 로고    scopus 로고
    • Degradation of β-amyloid by proteolytic antibody light chains
    • RANGAN, S.K. et al. 2003. Degradation of β-amyloid by proteolytic antibody light chains. Biochemistry 42: 14328-14334.
    • (2003) Biochemistry , vol.42 , pp. 14328-14334
    • Rangan, S.K.1
  • 109
    • 3543054598 scopus 로고    scopus 로고
    • Proteolytic antibody light chains alter β-amyloid aggregation and prevent cytotoxicity
    • LIU, R. et al. 2004. Proteolytic antibody light chains alter β-amyloid aggregation and prevent cytotoxicity. Biochemistry 43: 9999-10007.
    • (2004) Biochemistry , vol.43 , pp. 9999-10007
    • Liu, R.1
  • 110
    • 3442896818 scopus 로고    scopus 로고
    • A new Alzheimer's disease interventive strategy: GLP-1
    • PERRY, T.A. & N.H. GREIG. 2004. A new Alzheimer's disease interventive strategy: GLP-1. Curr. Drug Targets 5: 565-571.
    • (2004) Curr. Drug Targets , vol.5 , pp. 565-571
    • Perry, T.A.1    Greig, N.H.2
  • 111
    • 0027320916 scopus 로고
    • Hippocampal atrophy in normal aging. An association with recent memory impairment
    • GOLOMB, J. et al. 1993. Hippocampal atrophy in normal aging. An association with recent memory impairment. Arch. Neurol. 50: 967-973.
    • (1993) Arch. Neurol. , vol.50 , pp. 967-973
    • Golomb, J.1
  • 112
    • 0036710931 scopus 로고    scopus 로고
    • Lipid peroxidation in aging brain and Alzheimer's disease
    • MONTINE, T.J. et al. 2002. Lipid peroxidation in aging brain and Alzheimer's disease. Free Radic. Biol. Med. 33: 620-626.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 620-626
    • Montine, T.J.1
  • 113
    • 14944356256 scopus 로고    scopus 로고
    • 2+ and mitochondria as substrates for deficits in synaptic plasticity in normal brain aging
    • 2+ and mitochondria as substrates for deficits in synaptic plasticity in normal brain aging. J. Cell. Mol. Med. 8: 181-190.
    • (2004) J. Cell. Mol. Med. , vol.8 , pp. 181-190
    • Toescu, B.C.1    Verkhratsky, A.2
  • 114
    • 1242338183 scopus 로고    scopus 로고
    • Involvement of oxidative stress-induced abnormalities in ceramide and cholesterol metabolism in brain aging and Alzheimer's disease
    • CUTLER, R.G. et al. 2004. Involvement of oxidative stress-induced abnormalities in ceramide and cholesterol metabolism in brain aging and Alzheimer's disease. Proc. Natl. Acad. Sci. USA 101: 2070-2075.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 2070-2075
    • Cutler, R.G.1
  • 115
    • 0034095485 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy: Accumulation of Aβ in interstitial fluid drainage pathways in Alzheimer's disease
    • WELLER, R.O. et al. 2000. Cerebral amyloid angiopathy: accumulation of Aβ in interstitial fluid drainage pathways in Alzheimer's disease. Ann. N.Y. Acad. Sci. 903: 110-117.
    • (2000) Ann. N.Y. Acad. Sci. , vol.903 , pp. 110-117
    • Weller, R.O.1
  • 116
    • 0035194145 scopus 로고    scopus 로고
    • Evidence of oxidative damage in Alzheimer's disease brain: Central role for amyloid β-peptide
    • BUTTERFIELD, D.A. et al. 2002. Evidence of oxidative damage in Alzheimer's disease brain: central role for amyloid β-peptide. Trends Mol. Med. 7: 548-554.
    • (2002) Trends Mol. Med. , vol.7 , pp. 548-554
    • Butterfield, D.A.1
  • 117
    • 0034925118 scopus 로고    scopus 로고
    • The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: The role of Aβ1-42
    • LAUDERBACK, C.M. et al. 2001. The glial glutamate transporter, GLT-1, is oxidatively modified by 4-hydroxy-2-nonenal in the Alzheimer's disease brain: the role of Aβ1-42. J. Neurochem. 78: 413-416.
    • (2001) J. Neurochem. , vol.78 , pp. 413-416
    • Lauderback, C.M.1
  • 118
    • 0030989545 scopus 로고    scopus 로고
    • 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease
    • SAYRE, L.M. et al. 1997. 4-Hydroxynonenal-derived advanced lipid peroxidation end products are increased in Alzheimer's disease. J. Neurochem. 68: 2092-2097.
    • (1997) J. Neurochem. , vol.68 , pp. 2092-2097
    • Sayre, L.M.1
  • 119
    • 0141514419 scopus 로고    scopus 로고
    • Oxidized neprilysin in aging and Alzheimer's disease brains
    • WANG, D.S. et al. 2003. Oxidized neprilysin in aging and Alzheimer's disease brains. Biochem. Biophys. Res. Commun. 310: 236-241.
    • (2003) Biochem. Biophys. Res. Commun. , vol.310 , pp. 236-241
    • Wang, D.S.1
  • 120
    • 0023494793 scopus 로고
    • Proteolytic degradation of insulin and glucagon in rat brain during ontogenesis
    • REISER, M. et al. 1987. Proteolytic degradation of insulin and glucagon in rat brain during ontogenesis. Acta Histochem. 82: 35-39.
    • (1987) Acta Histochem. , vol.82 , pp. 35-39
    • Reiser, M.1
  • 121
    • 12144287738 scopus 로고    scopus 로고
    • Low cholesterol levels are associated with short-term mortality in older patients with ischemic stroke
    • ZULIANI, G. et al. 2004. Low cholesterol levels are associated with short-term mortality in older patients with ischemic stroke. J. Gerontol. A. Biol. Sci. Med. Sci. 59: 293-297.
    • (2004) J. Gerontol. A. Biol. Sci. Med. Sci. , vol.59 , pp. 293-297
    • Zuliani, G.1
  • 122
    • 18544386562 scopus 로고    scopus 로고
    • Increased a β peptides and reduced cholesterol and myelin proteins characterize white matter degeneration in Alzheimer's disease
    • ROHER, A.E. et al. 2002. Increased A β peptides and reduced cholesterol and myelin proteins characterize white matter degeneration in Alzheimer's disease. Biochemistry 37: 11080-11090.
    • (2002) Biochemistry , vol.37 , pp. 11080-11090
    • Roher, A.E.1
  • 124
    • 0033827766 scopus 로고    scopus 로고
    • Global hypoxia per se is an unusual cause of axonal injury
    • DOLINAK, D., C. SMITH & D.I. GRAHAM. 2000. Global hypoxia per se is an unusual cause of axonal injury. Acta Neuropathol. (Berl.) 100: 553-560.
    • (2000) Acta Neuropathol. (Berl.) , vol.100 , pp. 553-560
    • Dolinak, D.1    Smith, C.2    Graham, D.I.3
  • 125
    • 3242688902 scopus 로고    scopus 로고
    • Tissue-type plasminogen activator and neuroserpin: A well-balanced act in the nervous system?
    • YEPES, M. & D.A. LAWRENCE. 2004. Tissue-type plasminogen activator and neuroserpin: a well-balanced act in the nervous system? Trends Cardiovasc. Med. 14: 173-180.
    • (2004) Trends Cardiovasc. Med. , vol.14 , pp. 173-180
    • Yepes, M.1    Lawrence, D.A.2
  • 126
    • 9144266913 scopus 로고    scopus 로고
    • Presynaptic localization of neprilysin contributes to efficient clearance of amyloid-β peptide in mouse brain
    • IWATA, N. et al. 2004. Presynaptic localization of neprilysin contributes to efficient clearance of amyloid-β peptide in mouse brain. J. Neurosci. 24: 991-998.
    • (2004) J. Neurosci. , vol.24 , pp. 991-998
    • Iwata, N.1
  • 127
    • 0037444432 scopus 로고    scopus 로고
    • Neprilysin gene transfer reduces human amyloid pathology in transgenic mice
    • MARR, R.A. et al. 2003. Neprilysin gene transfer reduces human amyloid pathology in transgenic mice. J. Neurosci. 23: 1992-1996.
    • (2003) J. Neurosci. , vol.23 , pp. 1992-1996
    • Marr, R.A.1
  • 128
    • 0038661168 scopus 로고    scopus 로고
    • Neuroprotection and neurorescue against Aβ toxicity and PKC-dependent release of nonamyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate
    • LEVITES, Y. et al. 2003. Neuroprotection and neurorescue against Aβ toxicity and PKC-dependent release of nonamyloidogenic soluble precursor protein by green tea polyphenol (-)-epigallocatechin-3-gallate. FASEB J. 17: 952-954.
    • (2003) FASEB J. , vol.17 , pp. 952-954
    • Levites, Y.1


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