메뉴 건너뛰기




Volumn 13, Issue 8, 2007, Pages 337-344

Amyloid beta as a regulator of lipid homeostasis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA GALACTOSIDASE; ALPHA SECRETASE; AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; APOLIPOPROTEIN E; BETA N ACETYLHEXOSAMINIDASE; BETA N ACETYLHEXOSAMINIDASE A; BETA SECRETASE; CERAMIDE; CEREBROSIDE SULFATASE; GALACTOSYLCERAMIDE; GAMMA SECRETASE; GANGLIOSIDE GM1; GANGLIOSIDE GM2; GLOBOTRIAOSYLCERAMIDE; GLYCOGEN SYNTHASE KINASE 3BETA; HYDROXYMETHYLGLUTARYL COENZYME A REDUCTASE; LOW DENSITY LIPOPROTEIN RECEPTOR; MEMBRANE METALLOENDOPEPTIDASE; N ACETYLGALACTOSAMINE 4 SULFATASE; PSYCHOSINE; SPHINGOLIPID; SPHINGOMYELIN; SPHINGOMYELIN PHOSPHODIESTERASE; STEROL REGULATORY ELEMENT BINDING PROTEIN; STERYL SULFATASE; SULFATIDE; TETRASPANIN;

EID: 34547145226     PISSN: 14714914     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molmed.2007.06.004     Document Type: Review
Times cited : (68)

References (93)
  • 1
    • 0031695197 scopus 로고    scopus 로고
    • Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset
    • Brookmeyer R., et al. Projections of Alzheimer's disease in the United States and the public health impact of delaying disease onset. Am. J. Public Health 88 (1998) 1337-1342
    • (1998) Am. J. Public Health , vol.88 , pp. 1337-1342
    • Brookmeyer, R.1
  • 2
    • 5344240284 scopus 로고    scopus 로고
    • Amyloid-beta precursor protein processing in neurodegeneration
    • Wilquet V., and De Strooper B. Amyloid-beta precursor protein processing in neurodegeneration. Curr. Opin. Neurobiol. 14 (2004) 582-588
    • (2004) Curr. Opin. Neurobiol. , vol.14 , pp. 582-588
    • Wilquet, V.1    De Strooper, B.2
  • 3
    • 0029671451 scopus 로고    scopus 로고
    • Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains
    • Kuo Y.M., et al. Water-soluble Abeta (N-40, N-42) oligomers in normal and Alzheimer disease brains. J. Biol. Chem. 271 (1996) 4077-4081
    • (1996) J. Biol. Chem. , vol.271 , pp. 4077-4081
    • Kuo, Y.M.1
  • 4
    • 0034049944 scopus 로고    scopus 로고
    • Proteolytic processing and cell biological functions of the amyloid precursor protein
    • De Strooper B., and Annaert W. Proteolytic processing and cell biological functions of the amyloid precursor protein. J. Cell Sci. 113 (2000) 1857-1870
    • (2000) J. Cell Sci. , vol.113 , pp. 1857-1870
    • De Strooper, B.1    Annaert, W.2
  • 5
    • 0027258525 scopus 로고
    • The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease
    • Jarrett J.T., et al. The carboxy terminus of the beta amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 32 (1993) 4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1
  • 6
    • 0034329291 scopus 로고    scopus 로고
    • Mice with combined gene knock-outs reveal essential and partially redundant functions of amyloid precursor protein family members
    • Heber S., et al. Mice with combined gene knock-outs reveal essential and partially redundant functions of amyloid precursor protein family members. J. Neurosci. 20 (2000) 7951-7963
    • (2000) J. Neurosci. , vol.20 , pp. 7951-7963
    • Heber, S.1
  • 7
    • 13944274830 scopus 로고    scopus 로고
    • Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2
    • Wang P., et al. Defective neuromuscular synapses in mice lacking amyloid precursor protein (APP) and APP-Like protein 2. J. Neurosci. 25 (2005) 1219-1225
    • (2005) J. Neurosci. , vol.25 , pp. 1219-1225
    • Wang, P.1
  • 8
    • 8144230876 scopus 로고    scopus 로고
    • Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members
    • Herms J., et al. Cortical dysplasia resembling human type 2 lissencephaly in mice lacking all three APP family members. EMBO J. 23 (2004) 4106-4115
    • (2004) EMBO J. , vol.23 , pp. 4106-4115
    • Herms, J.1
  • 10
    • 34547223895 scopus 로고    scopus 로고
    • Amyloid precursor protein knockdown by siRNA impairs spontaneous alteration in adult mice
    • 10.1111/j.1471-4159.2007.04672.x
    • Senechal Y., et al. Amyloid precursor protein knockdown by siRNA impairs spontaneous alteration in adult mice. J. Neurochem. (2007) 10.1111/j.1471-4159.2007.04672.x
    • (2007) J. Neurochem.
    • Senechal, Y.1
  • 11
    • 1442306058 scopus 로고    scopus 로고
    • Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage
    • Ho A., and Sudhof T.C. Binding of F-spondin to amyloid-beta precursor protein: a candidate amyloid-beta precursor protein ligand that modulates amyloid-beta precursor protein cleavage. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 2548-2553
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2548-2553
    • Ho, A.1    Sudhof, T.C.2
  • 12
    • 33750194498 scopus 로고    scopus 로고
    • Functional role of the low-density lipoprotein receptor-related protein in Alzheimer's disease
    • Waldron E., et al. Functional role of the low-density lipoprotein receptor-related protein in Alzheimer's disease. Neurodegener. Dis. 3 (2006) 233-238
    • (2006) Neurodegener. Dis. , vol.3 , pp. 233-238
    • Waldron, E.1
  • 13
    • 27144547977 scopus 로고    scopus 로고
    • Homo- and heterodimerization of APP family members promotes intercellular adhesion
    • Soba P., et al. Homo- and heterodimerization of APP family members promotes intercellular adhesion. EMBO J. 24 (2005) 3624-3634
    • (2005) EMBO J. , vol.24 , pp. 3624-3634
    • Soba, P.1
  • 14
    • 0033301776 scopus 로고    scopus 로고
    • Neurite-outgrowth regulating functions of the amyloid protein precursor of Alzheimer's disease
    • Small D.H., et al. Neurite-outgrowth regulating functions of the amyloid protein precursor of Alzheimer's disease. J. Alzheimers Dis. 1 (1999) 275-285
    • (1999) J. Alzheimers Dis. , vol.1 , pp. 275-285
    • Small, D.H.1
  • 15
    • 0028874953 scopus 로고
    • PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities
    • Wolf G., et al. PTB domains of IRS-1 and Shc have distinct but overlapping binding specificities. J. Biol. Chem. 270 (1995) 27407-27410
    • (1995) J. Biol. Chem. , vol.270 , pp. 27407-27410
    • Wolf, G.1
  • 16
    • 0037827785 scopus 로고    scopus 로고
    • X11alpha modulates secretory and endocytic trafficking and metabolism of amyloid precursor protein: mutational analysis of the YENPTY sequence
    • King G.D., et al. X11alpha modulates secretory and endocytic trafficking and metabolism of amyloid precursor protein: mutational analysis of the YENPTY sequence. Neuroscience 120 (2003) 143-154
    • (2003) Neuroscience , vol.120 , pp. 143-154
    • King, G.D.1
  • 17
    • 0042357124 scopus 로고    scopus 로고
    • Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor protein
    • Noviello C., et al. Autosomal recessive hypercholesterolemia protein interacts with and regulates the cell surface level of Alzheimer's amyloid beta precursor protein. J. Biol. Chem. 278 (2003) 31843-31847
    • (2003) J. Biol. Chem. , vol.278 , pp. 31843-31847
    • Noviello, C.1
  • 18
    • 0034638843 scopus 로고    scopus 로고
    • Numb is an endocytic protein
    • Santolini E., et al. Numb is an endocytic protein. J. Cell Biol. 151 (2000) 1345-1352
    • (2000) J. Cell Biol. , vol.151 , pp. 1345-1352
    • Santolini, E.1
  • 19
    • 0037119952 scopus 로고    scopus 로고
    • Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor
    • Mishra S.K., et al. Disabled-2 exhibits the properties of a cargo-selective endocytic clathrin adaptor. EMBO J. 21 (2002) 4915-4926
    • (2002) EMBO J. , vol.21 , pp. 4915-4926
    • Mishra, S.K.1
  • 20
    • 0029008666 scopus 로고
    • The reeler gene-associated antigen on Cajal-Retzius neurons is a crucial molecule for laminar organization of cortical neurons
    • Ogawa M., et al. The reeler gene-associated antigen on Cajal-Retzius neurons is a crucial molecule for laminar organization of cortical neurons. Neuron 14 (1995) 899-912
    • (1995) Neuron , vol.14 , pp. 899-912
    • Ogawa, M.1
  • 21
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni R., et al. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J. Neurosci. 19 (1999) 7507-7515
    • (1999) J. Neurosci. , vol.19 , pp. 7507-7515
    • Homayouni, R.1
  • 22
    • 0038603918 scopus 로고    scopus 로고
    • A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1
    • Inomata H., et al. A scaffold protein JIP-1b enhances amyloid precursor protein phosphorylation by JNK and its association with kinesin light chain 1. J. Biol. Chem. 278 (2003) 22946-22955
    • (2003) J. Biol. Chem. , vol.278 , pp. 22946-22955
    • Inomata, H.1
  • 23
    • 0037205493 scopus 로고    scopus 로고
    • Interaction of Alzheimer's beta -amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade
    • Taru H., et al. Interaction of Alzheimer's beta -amyloid precursor family proteins with scaffold proteins of the JNK signaling cascade. J. Biol. Chem. 277 (2002) 20070-20078
    • (2002) J. Biol. Chem. , vol.277 , pp. 20070-20078
    • Taru, H.1
  • 24
    • 0037053281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
    • Tarr P.E., et al. Tyrosine phosphorylation of the beta-amyloid precursor protein cytoplasmic tail promotes interaction with Shc. J. Biol. Chem. 277 (2002) 16798-16804
    • (2002) J. Biol. Chem. , vol.277 , pp. 16798-16804
    • Tarr, P.E.1
  • 25
    • 0027447656 scopus 로고
    • Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o)
    • Nishimoto I., et al. Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o). Nature 362 (1993) 75-79
    • (1993) Nature , vol.362 , pp. 75-79
    • Nishimoto, I.1
  • 26
    • 5444275067 scopus 로고    scopus 로고
    • The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor
    • von Rotz R.C., et al. The APP intracellular domain forms nuclear multiprotein complexes and regulates the transcription of its own precursor. J. Cell Sci. 117 (2004) 4435-4448
    • (2004) J. Cell Sci. , vol.117 , pp. 4435-4448
    • von Rotz, R.C.1
  • 27
    • 0037067655 scopus 로고    scopus 로고
    • Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein
    • Baek S.H., et al. Exchange of N-CoR corepressor and Tip60 coactivator complexes links gene expression by NF-kappaB and beta-amyloid precursor protein. Cell 110 (2002) 55-67
    • (2002) Cell , vol.110 , pp. 55-67
    • Baek, S.H.1
  • 28
    • 33845324145 scopus 로고    scopus 로고
    • C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression
    • Kim H.S., et al. C-terminal fragments of amyloid precursor protein exert neurotoxicity by inducing glycogen synthase kinase-3beta expression. FASEB J. 17 (2003) 1951-1953
    • (2003) FASEB J. , vol.17 , pp. 1951-1953
    • Kim, H.S.1
  • 29
    • 20444398562 scopus 로고    scopus 로고
    • Presenilin-dependent transcriptional control of the Abeta-degrading enzyme neprilysin by intracellular domains of betaAPP and APLP
    • Pardossi-Piquard R., et al. Presenilin-dependent transcriptional control of the Abeta-degrading enzyme neprilysin by intracellular domains of betaAPP and APLP. Neuron 46 (2005) 541-554
    • (2005) Neuron , vol.46 , pp. 541-554
    • Pardossi-Piquard, R.1
  • 30
    • 33745584643 scopus 로고    scopus 로고
    • Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes
    • Hebert S.S., et al. Regulated intramembrane proteolysis of amyloid precursor protein and regulation of expression of putative target genes. EMBO Rep. 7 (2006) 739-745
    • (2006) EMBO Rep. , vol.7 , pp. 739-745
    • Hebert, S.S.1
  • 31
    • 0042634362 scopus 로고    scopus 로고
    • Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory
    • Turner P.R., et al. Roles of amyloid precursor protein and its fragments in regulating neural activity, plasticity and memory. Prog. Neurobiol. 70 (2003) 1-32
    • (2003) Prog. Neurobiol. , vol.70 , pp. 1-32
    • Turner, P.R.1
  • 32
    • 2542519087 scopus 로고    scopus 로고
    • Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone
    • Caille I., et al. Soluble form of amyloid precursor protein regulates proliferation of progenitors in the adult subventricular zone. Development 131 (2004) 2173-2181
    • (2004) Development , vol.131 , pp. 2173-2181
    • Caille, I.1
  • 33
    • 0037470137 scopus 로고    scopus 로고
    • The transmembrane domain of the amyloid precursor protein in microsomal membranes is on both sides shorter than predicted
    • Grziwa B., et al. The transmembrane domain of the amyloid precursor protein in microsomal membranes is on both sides shorter than predicted. J. Biol. Chem. 278 (2003) 6803-6808
    • (2003) J. Biol. Chem. , vol.278 , pp. 6803-6808
    • Grziwa, B.1
  • 34
    • 0030769091 scopus 로고    scopus 로고
    • Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides
    • Hartmann T., et al. Distinct sites of intracellular production for Alzheimer's disease A beta40/42 amyloid peptides. Nat. Med. 3 (1997) 1016-1020
    • (1997) Nat. Med. , vol.3 , pp. 1016-1020
    • Hartmann, T.1
  • 35
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • Cook D.G., et al. Alzheimer's A beta(1-42) is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nat. Med. 3 (1997) 1021-1023
    • (1997) Nat. Med. , vol.3 , pp. 1021-1023
    • Cook, D.G.1
  • 36
    • 0037022360 scopus 로고    scopus 로고
    • The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain
    • Lichtenthaler S.F., et al. The intramembrane cleavage site of the amyloid precursor protein depends on the length of its transmembrane domain. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 1365-1370
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 1365-1370
    • Lichtenthaler, S.F.1
  • 37
    • 33745754350 scopus 로고    scopus 로고
    • Altered membrane fluidity and lipid raft composition in presenilin-deficient cells
    • Grimm M.O., et al. Altered membrane fluidity and lipid raft composition in presenilin-deficient cells. Acta Neurol. Scand. Suppl. 185 (2006) 27-32
    • (2006) Acta Neurol. Scand. Suppl. , vol.185 , pp. 27-32
    • Grimm, M.O.1
  • 38
    • 6044221306 scopus 로고    scopus 로고
    • GM1 ganglioside regulates the proteolysis of amyloid precursor protein
    • Zha Q., et al. GM1 ganglioside regulates the proteolysis of amyloid precursor protein. Mol. Psychiatry 9 (2004) 946-952
    • (2004) Mol. Psychiatry , vol.9 , pp. 946-952
    • Zha, Q.1
  • 39
    • 28644451007 scopus 로고    scopus 로고
    • Regulation of cholesterol and sphingomyelin metabolism by amyloid-beta and presenilin
    • Grimm M.O., et al. Regulation of cholesterol and sphingomyelin metabolism by amyloid-beta and presenilin. Nat. Cell Biol. 7 (2005) 1118-1123
    • (2005) Nat. Cell Biol. , vol.7 , pp. 1118-1123
    • Grimm, M.O.1
  • 40
    • 0027194791 scopus 로고
    • Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families
    • Corder E.H., et al. Gene dose of apolipoprotein E type 4 allele and the risk of Alzheimer's disease in late onset families. Science 261 (1993) 921-923
    • (1993) Science , vol.261 , pp. 921-923
    • Corder, E.H.1
  • 41
    • 0035897938 scopus 로고    scopus 로고
    • Midlife vascular risk factors and Alzheimer's disease in later life: longitudinal, population based study
    • Kivipelto M., et al. Midlife vascular risk factors and Alzheimer's disease in later life: longitudinal, population based study. BMJ 322 (2001) 1447-1451
    • (2001) BMJ , vol.322 , pp. 1447-1451
    • Kivipelto, M.1
  • 42
    • 0030928650 scopus 로고    scopus 로고
    • Lipid binding to amyloid beta-peptide aggregates: preferential binding of cholesterol as compared with phosphatidylcholine and fatty acids
    • Avdulov N.A., et al. Lipid binding to amyloid beta-peptide aggregates: preferential binding of cholesterol as compared with phosphatidylcholine and fatty acids. J. Neurochem. 69 (1997) 1746-1752
    • (1997) J. Neurochem. , vol.69 , pp. 1746-1752
    • Avdulov, N.A.1
  • 43
    • 0001504829 scopus 로고    scopus 로고
    • Simvastatin strongly reduces levels of Alzheimer's disease beta -amyloid peptides Abeta 42 and Abeta 40 in vitro and in vivo
    • Fassbender K., et al. Simvastatin strongly reduces levels of Alzheimer's disease beta -amyloid peptides Abeta 42 and Abeta 40 in vitro and in vivo. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 5856-5861
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 5856-5861
    • Fassbender, K.1
  • 44
    • 0035160066 scopus 로고    scopus 로고
    • A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease
    • Refolo L.M., et al. A cholesterol-lowering drug reduces beta-amyloid pathology in a transgenic mouse model of Alzheimer's disease. Neurobiol. Dis. 8 (2001) 890-899
    • (2001) Neurobiol. Dis. , vol.8 , pp. 890-899
    • Refolo, L.M.1
  • 45
    • 20844440894 scopus 로고    scopus 로고
    • Atorvastatin for the treatment of mild to moderate Alzheimer disease: preliminary results
    • Sparks D.L., et al. Atorvastatin for the treatment of mild to moderate Alzheimer disease: preliminary results. Arch. Neurol. 62 (2005) 753-757
    • (2005) Arch. Neurol. , vol.62 , pp. 753-757
    • Sparks, D.L.1
  • 46
    • 0033833354 scopus 로고    scopus 로고
    • Hypercholesterolemia accelerates the Alzheimer's amyloid pathology in a transgenic mouse model
    • Refolo L.M., et al. Hypercholesterolemia accelerates the Alzheimer's amyloid pathology in a transgenic mouse model. Neurobiol. Dis. 7 (2000) 321-331
    • (2000) Neurobiol. Dis. , vol.7 , pp. 321-331
    • Refolo, L.M.1
  • 47
    • 0037171095 scopus 로고    scopus 로고
    • Diet-induced hypercholesterolemia enhances brain A beta accumulation in transgenic mice
    • Shie F.S., et al. Diet-induced hypercholesterolemia enhances brain A beta accumulation in transgenic mice. Neuroreport 13 (2002) 455-459
    • (2002) Neuroreport , vol.13 , pp. 455-459
    • Shie, F.S.1
  • 48
    • 0034638746 scopus 로고    scopus 로고
    • Statins and the risk of dementia
    • Jick H., et al. Statins and the risk of dementia. Lancet 356 (2000) 1627-1631
    • (2000) Lancet , vol.356 , pp. 1627-1631
    • Jick, H.1
  • 49
    • 0033772113 scopus 로고    scopus 로고
    • Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors
    • Wolozin B., et al. Decreased prevalence of Alzheimer disease associated with 3-hydroxy-3-methyglutaryl coenzyme A reductase inhibitors. Arch. Neurol. 57 (2000) 1439-1443
    • (2000) Arch. Neurol. , vol.57 , pp. 1439-1443
    • Wolozin, B.1
  • 50
    • 0036126850 scopus 로고    scopus 로고
    • Use of lipid-lowering agents, indication bias, and the risk of dementia in community-dwelling elderly people
    • Rockwood K., et al. Use of lipid-lowering agents, indication bias, and the risk of dementia in community-dwelling elderly people. Arch. Neurol. 59 (2002) 223-227
    • (2002) Arch. Neurol. , vol.59 , pp. 223-227
    • Rockwood, K.1
  • 51
    • 0036714243 scopus 로고    scopus 로고
    • Treatment with simvastatin in normocholesterolemic patients with Alzheimer's disease: A 26-week randomized, placebo-controlled, double-blind trial
    • Simons M., et al. Treatment with simvastatin in normocholesterolemic patients with Alzheimer's disease: A 26-week randomized, placebo-controlled, double-blind trial. Ann. Neurol. 52 (2002) 346-350
    • (2002) Ann. Neurol. , vol.52 , pp. 346-350
    • Simons, M.1
  • 52
    • 0026002728 scopus 로고
    • Gangliosides in cerebrospinal fluid in 'probable Alzheimer's disease'
    • Blennow K., et al. Gangliosides in cerebrospinal fluid in 'probable Alzheimer's disease'. Arch. Neurol. 48 (1991) 1032-1035
    • (1991) Arch. Neurol. , vol.48 , pp. 1032-1035
    • Blennow, K.1
  • 53
    • 0032568552 scopus 로고    scopus 로고
    • Cholesterol depletion inhibits the generation of beta-amyloid in hippocampal neurons
    • Simons M., et al. Cholesterol depletion inhibits the generation of beta-amyloid in hippocampal neurons. Proc. Natl. Acad. Sci. U. S. A. 95 (1998) 6460-6464
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 6460-6464
    • Simons, M.1
  • 54
    • 0036180950 scopus 로고    scopus 로고
    • Cholesterol-dependent gamma-secretase activity in buoyant cholesterol-rich membrane microdomains
    • Wahrle S., et al. Cholesterol-dependent gamma-secretase activity in buoyant cholesterol-rich membrane microdomains. Neurobiol. Dis. 9 (2002) 11-23
    • (2002) Neurobiol. Dis. , vol.9 , pp. 11-23
    • Wahrle, S.1
  • 55
    • 0035830844 scopus 로고    scopus 로고
    • Accumulation and aggregation of amyloid beta-protein in late endosomes of Niemann-pick type C cells
    • Yamazaki T., et al. Accumulation and aggregation of amyloid beta-protein in late endosomes of Niemann-pick type C cells. J. Biol. Chem. 276 (2001) 4454-4460
    • (2001) J. Biol. Chem. , vol.276 , pp. 4454-4460
    • Yamazaki, T.1
  • 56
    • 0034795651 scopus 로고    scopus 로고
    • Acyl-coenzyme A: cholesterol acyltransferase modulates the generation of the amyloid beta-peptide
    • Puglielli L., et al. Acyl-coenzyme A: cholesterol acyltransferase modulates the generation of the amyloid beta-peptide. Nat. Cell Biol. 3 (2001) 905-912
    • (2001) Nat. Cell Biol. , vol.3 , pp. 905-912
    • Puglielli, L.1
  • 57
    • 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. Involvement of oxidative stress-induced abnormalities in ceramide and cholesterol metabolism in brain aging and Alzheimer's disease. Proc. Natl. Acad. Sci. U. S. A. 101 (2004) 2070-2075
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 2070-2075
    • Cutler, R.G.1
  • 58
    • 0036752025 scopus 로고    scopus 로고
    • Brain membrane cholesterol domains, aging and amyloid beta-peptides
    • Wood W.G., et al. Brain membrane cholesterol domains, aging and amyloid beta-peptides. Neurobiol. Aging 23 (2002) 685-694
    • (2002) Neurobiol. Aging , vol.23 , pp. 685-694
    • Wood, W.G.1
  • 59
    • 0026513498 scopus 로고
    • Cortical distribution of gangliosides in Alzheimer's disease
    • Kracun I., et al. Cortical distribution of gangliosides in Alzheimer's disease. Neurochem. Int. 20 (1992) 433-438
    • (1992) Neurochem. Int. , vol.20 , pp. 433-438
    • Kracun, I.1
  • 60
    • 0028099263 scopus 로고
    • Membrane lipids of adult human brain: lipid composition of frontal and temporal lobe in subjects of age 20 to 100 years
    • Svennerholm L., et al. Membrane lipids of adult human brain: lipid composition of frontal and temporal lobe in subjects of age 20 to 100 years. J. Neurochem. 63 (1994) 1802-1811
    • (1994) J. Neurochem. , vol.63 , pp. 1802-1811
    • Svennerholm, L.1
  • 61
    • 0025610029 scopus 로고
    • Brain gangliosides in Alzheimer's disease
    • Kracun I., et al. Brain gangliosides in Alzheimer's disease. J. Hirnforsch. 31 (1990) 789-793
    • (1990) J. Hirnforsch. , vol.31 , pp. 789-793
    • Kracun, I.1
  • 62
    • 23044510465 scopus 로고    scopus 로고
    • Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide
    • Tamboli I.Y., et al. Inhibition of glycosphingolipid biosynthesis reduces secretion of the beta-amyloid precursor protein and amyloid beta-peptide. J. Biol. Chem. 280 (2005) 28110-28117
    • (2005) J. Biol. Chem. , vol.280 , pp. 28110-28117
    • Tamboli, I.Y.1
  • 63
    • 0035951401 scopus 로고    scopus 로고
    • Protein sorting upon exit from the endoplasmic reticulum
    • Muniz M., et al. Protein sorting upon exit from the endoplasmic reticulum. Cell 104 (2001) 313-320
    • (2001) Cell , vol.104 , pp. 313-320
    • Muniz, M.1
  • 64
    • 0037223101 scopus 로고    scopus 로고
    • Novel therapeutic approach for the treatment of Alzheimer's disease by peripheral administration of agents with an affinity to beta-amyloid
    • Matsuoka Y., et al. Novel therapeutic approach for the treatment of Alzheimer's disease by peripheral administration of agents with an affinity to beta-amyloid. J. Neurosci. 23 (2003) 29-33
    • (2003) J. Neurosci. , vol.23 , pp. 29-33
    • Matsuoka, Y.1
  • 65
    • 0035372336 scopus 로고    scopus 로고
    • Effects of apolipoprotein E (apoE) isoforms, beta-amyloid (Abeta) and apoE/Abeta complexes on protein kinase C-alpha (PKC-alpha) translocation and amyloid precursor protein (APP) processing in human SH-SY5Y neuroblastoma cells and fibroblasts
    • Cedazo-Minguez A., et al. Effects of apolipoprotein E (apoE) isoforms, beta-amyloid (Abeta) and apoE/Abeta complexes on protein kinase C-alpha (PKC-alpha) translocation and amyloid precursor protein (APP) processing in human SH-SY5Y neuroblastoma cells and fibroblasts. Neurochem. Int. 38 (2001) 615-625
    • (2001) Neurochem. Int. , vol.38 , pp. 615-625
    • Cedazo-Minguez, A.1
  • 66
    • 0027257099 scopus 로고
    • Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells
    • Fiedler K., et al. Glycosphingolipid-enriched, detergent-insoluble complexes in protein sorting in epithelial cells. Biochemistry 32 (1993) 6365-6373
    • (1993) Biochemistry , vol.32 , pp. 6365-6373
    • Fiedler, K.1
  • 67
    • 0031558768 scopus 로고    scopus 로고
    • Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes?
    • Brown D.A., and London E. Structure of detergent-resistant membrane domains: does phase separation occur in biological membranes?. Biochem. Biophys. Res. Commun. 240 (1997) 1-7
    • (1997) Biochem. Biophys. Res. Commun. , vol.240 , pp. 1-7
    • Brown, D.A.1    London, E.2
  • 70
    • 0034529050 scopus 로고    scopus 로고
    • How cells handle cholesterol
    • Simons K., and Ikonen E. How cells handle cholesterol. Science 290 (2000) 1721-1726
    • (2000) Science , vol.290 , pp. 1721-1726
    • Simons, K.1    Ikonen, E.2
  • 71
    • 0037201965 scopus 로고    scopus 로고
    • Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: essential basis to define tumor malignancy
    • Hakomori S., and Handa K. Glycosphingolipid-dependent cross-talk between glycosynapses interfacing tumor cells with their host cells: essential basis to define tumor malignancy. FEBS Lett. 531 (2002) 88-92
    • (2002) FEBS Lett. , vol.531 , pp. 88-92
    • Hakomori, S.1    Handa, K.2
  • 72
    • 7244258941 scopus 로고    scopus 로고
    • Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes
    • Vetrivel K.S., et al. Association of gamma-secretase with lipid rafts in post-Golgi and endosome membranes. J. Biol. Chem. 279 (2004) 44945-44954
    • (2004) J. Biol. Chem. , vol.279 , pp. 44945-44954
    • Vetrivel, K.S.1
  • 73
    • 0141482022 scopus 로고    scopus 로고
    • Exclusively targeting beta-secretase to lipid rafts by GPI-anchor addition up-regulates beta-site processing of the amyloid precursor protein
    • Cordy J.M., et al. Exclusively targeting beta-secretase to lipid rafts by GPI-anchor addition up-regulates beta-site processing of the amyloid precursor protein. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 11735-11740
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 11735-11740
    • Cordy, J.M.1
  • 74
    • 0642371716 scopus 로고    scopus 로고
    • Beta-secretase processing of the Alzheimer's amyloid protein precursor (APP)
    • Marlow L., et al. Beta-secretase processing of the Alzheimer's amyloid protein precursor (APP). J. Mol. Neurosci. 20 (2003) 233-239
    • (2003) J. Mol. Neurosci. , vol.20 , pp. 233-239
    • Marlow, L.1
  • 75
    • 0037421206 scopus 로고    scopus 로고
    • Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts
    • Ehehalt R., et al. Amyloidogenic processing of the Alzheimer beta-amyloid precursor protein depends on lipid rafts. J. Cell Biol. 160 (2003) 113-123
    • (2003) J. Cell Biol. , vol.160 , pp. 113-123
    • Ehehalt, R.1
  • 76
    • 0035928732 scopus 로고    scopus 로고
    • Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts
    • Riddell D.R., et al. Compartmentalization of beta-secretase (Asp2) into low-buoyant density, noncaveolar lipid rafts. Curr. Biol. 11 (2001) 1288-1293
    • (2001) Curr. Biol. , vol.11 , pp. 1288-1293
    • Riddell, D.R.1
  • 77
    • 0033571721 scopus 로고    scopus 로고
    • Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein
    • Parkin E.T., et al. Amyloid precursor protein, although partially detergent-insoluble in mouse cerebral cortex, behaves as an atypical lipid raft protein. Biochem. J. 344 (1999) 23-30
    • (1999) Biochem. J. , vol.344 , pp. 23-30
    • Parkin, E.T.1
  • 78
    • 0031746979 scopus 로고    scopus 로고
    • A detergent-insoluble membrane compartment contains A beta in vivo
    • Lee S.J., et al. A detergent-insoluble membrane compartment contains A beta in vivo. Nat. Med. 4 (1998) 730-734
    • (1998) Nat. Med. , vol.4 , pp. 730-734
    • Lee, S.J.1
  • 79
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha -secretase ADAM 10
    • Kojro E., et al. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha -secretase ADAM 10. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 5815-5820
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 5815-5820
    • Kojro, E.1
  • 80
    • 0037135536 scopus 로고    scopus 로고
    • De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway
    • Merrill Jr. A.H. De novo sphingolipid biosynthesis: a necessary, but dangerous, pathway. J. Biol. Chem. 277 (2002) 25843-25846
    • (2002) J. Biol. Chem. , vol.277 , pp. 25843-25846
    • Merrill Jr., A.H.1
  • 81
    • 0033792671 scopus 로고    scopus 로고
    • Effects of sphingosine and other sphingolipids on protein kinase C
    • Smith E.R., et al. Effects of sphingosine and other sphingolipids on protein kinase C. Methods Enzymol. 312 (2000) 361-373
    • (2000) Methods Enzymol. , vol.312 , pp. 361-373
    • Smith, E.R.1
  • 82
    • 0034308223 scopus 로고    scopus 로고
    • Ceramide as a second messenger: sticky solutions to sticky problems
    • Venkataraman K., and Futerman A.H. Ceramide as a second messenger: sticky solutions to sticky problems. Trends Cell Biol. 10 (2000) 408-412
    • (2000) Trends Cell Biol. , vol.10 , pp. 408-412
    • Venkataraman, K.1    Futerman, A.H.2
  • 83
    • 33745058080 scopus 로고    scopus 로고
    • Ceramide involvement in apoptosis and apoptotic diseases
    • Thevissen K., et al. Ceramide involvement in apoptosis and apoptotic diseases. Mini Rev. Med. Chem. 6 (2006) 699-709
    • (2006) Mini Rev. Med. Chem. , vol.6 , pp. 699-709
    • Thevissen, K.1
  • 84
    • 33751351070 scopus 로고    scopus 로고
    • Mutant presenilin 2 causes abnormality in the brain lipid profile in the development of Alzheimer's disease
    • Nguyen H.N., et al. Mutant presenilin 2 causes abnormality in the brain lipid profile in the development of Alzheimer's disease. Arch. Pharm. Res. 29 (2006) 884-889
    • (2006) Arch. Pharm. Res. , vol.29 , pp. 884-889
    • Nguyen, H.N.1
  • 85
    • 19744382332 scopus 로고    scopus 로고
    • The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases
    • Friesen J.A., and Rodwell V.W. The 3-hydroxy-3-methylglutaryl coenzyme-A (HMG-CoA) reductases. Genome Biol. 5 (2004) 248
    • (2004) Genome Biol. , vol.5 , pp. 248
    • Friesen, J.A.1    Rodwell, V.W.2
  • 86
    • 0036671360 scopus 로고    scopus 로고
    • Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism
    • Brown A.J., et al. Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism. Mol. Cell 10 (2002) 237-245
    • (2002) Mol. Cell , vol.10 , pp. 237-245
    • Brown, A.J.1
  • 87
    • 10944272619 scopus 로고    scopus 로고
    • Fibrillar amyloid-beta peptides kill human primary neurons via NADPH oxidase-mediated activation of neutral sphingomyelinase. Implications for Alzheimer's disease
    • Jana A., and Pahan K. Fibrillar amyloid-beta peptides kill human primary neurons via NADPH oxidase-mediated activation of neutral sphingomyelinase. Implications for Alzheimer's disease. J. Biol. Chem. 279 (2004) 51451-51459
    • (2004) J. Biol. Chem. , vol.279 , pp. 51451-51459
    • Jana, A.1    Pahan, K.2
  • 88
    • 33745253950 scopus 로고    scopus 로고
    • Soluble oligomers of amyloid-beta peptide induce neuronal apoptosis by activating a cPLA2-dependent sphingomyelinase-ceramide pathway
    • Malaplate-Armand C., et al. Soluble oligomers of amyloid-beta peptide induce neuronal apoptosis by activating a cPLA2-dependent sphingomyelinase-ceramide pathway. Neurobiol. Dis. 23 (2006) 178-189
    • (2006) Neurobiol. Dis. , vol.23 , pp. 178-189
    • Malaplate-Armand, C.1
  • 90
    • 33749633921 scopus 로고    scopus 로고
    • Omega-3 fatty acid treatment in 174 patients with mild to moderate Alzheimer disease: OmegAD study: a randomized double-blind trial
    • Freund-Levi Y., et al. Omega-3 fatty acid treatment in 174 patients with mild to moderate Alzheimer disease: OmegAD study: a randomized double-blind trial. Arch. Neurol. 63 (2006) 1402-1408
    • (2006) Arch. Neurol. , vol.63 , pp. 1402-1408
    • Freund-Levi, Y.1
  • 91
    • 33747180133 scopus 로고    scopus 로고
    • Impact of different saturated fatty acid, polyunsaturated fatty acid and cholesterol containing diets on beta-amyloid accumulation in APP/PS1 transgenic mice
    • Oksman M., et al. Impact of different saturated fatty acid, polyunsaturated fatty acid and cholesterol containing diets on beta-amyloid accumulation in APP/PS1 transgenic mice. Neurobiol. Dis. 23 (2006) 563-572
    • (2006) Neurobiol. Dis. , vol.23 , pp. 563-572
    • Oksman, M.1
  • 92
    • 4444223956 scopus 로고    scopus 로고
    • Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model
    • Calon F., et al. Docosahexaenoic acid protects from dendritic pathology in an Alzheimer's disease mouse model. Neuron 43 (2004) 633-645
    • (2004) Neuron , vol.43 , pp. 633-645
    • Calon, F.1
  • 93
    • 16244416174 scopus 로고    scopus 로고
    • A diet enriched with the omega-3 fatty acid docosahexaenoic acid reduces amyloid burden in an aged Alzheimer mouse model
    • Lim G.P., et al. A diet enriched with the omega-3 fatty acid docosahexaenoic acid reduces amyloid burden in an aged Alzheimer mouse model. J. Neurosci. 25 (2005) 3032-3040
    • (2005) J. Neurosci. , vol.25 , pp. 3032-3040
    • Lim, G.P.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.