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Volumn 3, Issue 11, 2002, Pages 862-872

Calcium dyshomeostasis and intracellular signalling in alzheimer's disease

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; CALCIUM; MEMBRANE PROTEIN; PRESENILIN 1; PSEN1 PROTEIN, HUMAN;

EID: 0036830947     PISSN: 1471003X     EISSN: 14710048     Source Type: Journal    
DOI: 10.1038/nrn960     Document Type: Article
Times cited : (877)

References (145)
  • 1
    • 0036548070 scopus 로고    scopus 로고
    • γ-Secretase, Notch, Aβ and Alzheimer's disease: Where do the presenilins fit in?
    • Sisodia, S. S. & St George-Hyslop, P H. γ-Secretase, Notch, Aβ and Alzheimer's disease: where do the presenilins fit in? Nature Rev. Neurosci. 3, 281-290 (2002).
    • (2002) Nature Rev. Neurosci. , vol.3 , pp. 281-290
    • Sisodia, S.S.1    St George-Hyslop, P.H.2
  • 2
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer's disease: Progress and problems on the road to therapeutics
    • Hardy, J. & Selkoe, D. J. The amyloid hypothesis of Alzheimer's disease: progress and problems on the road to therapeutics. Science 297, 353-356 (2002).
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 0024954067 scopus 로고
    • Calcium, membranes, aging, and Alzheimer's disease. Introduction and overview
    • Khachaturian, Z. S. Calcium, membranes, aging, and Alzheimer's disease. Introduction and overview. Ann. NY Acad. Sci. 568, 1-4 (1989).
    • (1989) Ann. NY Acad. Sci. , vol.568 , pp. 1-4
    • Khachaturian, Z.S.1
  • 4
    • 0034194089 scopus 로고    scopus 로고
    • Calcium signaling in the ER: Its role in neuronal plasticity and neurodegenerative disorders
    • Mattson, M. P et al. Calcium signaling in the ER: its role in neuronal plasticity and neurodegenerative disorders. Trends Neurosci. 23, 222-229 (2000).
    • (2000) Trends Neurosci , vol.23 , pp. 222-229
    • Mattson, M.P.1
  • 5
    • 0032127927 scopus 로고    scopus 로고
    • Calcium responses in fibroblasts from asymptomatic members of Alzheimer's disease families
    • Etcheberrigaray, R. et al. Calcium responses in fibroblasts from asymptomatic members of Alzheimer's disease families. Neurobiol. Dis. 5, 37-45 (1998).
    • (1998) Neurobiol. Dis. , vol.5 , pp. 37-45
    • Etcheberrigaray, R.1
  • 6
    • 0033523480 scopus 로고    scopus 로고
    • Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice
    • Larson, J., Lynch, G., Games, D. & Seubert, P. Alterations in synaptic transmission and long-term potentiation in hippocampal slices from young and aged PDAPP mice. Brain Res. 840, 23-35 (1999).
    • (1999) Brain Res , vol.840 , pp. 23-35
    • Larson, J.1    Lynch, G.2    Games, D.3    Seubert, P.4
  • 7
    • 0033016172 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice
    • Guo, Q. et al. Increased vulnerability of hippocampal neurons to excitotoxic necrosis in presenilin-1 mutant knock-in mice. Nature Med. 5, 101-106 (1999).
    • (1999) Nature Med , vol.5 , pp. 101-106
    • Guo, Q.1
  • 8
    • 0034657414 scopus 로고    scopus 로고
    • Capacitative calcium entry deficits and elevated luminal calcium content in mutant presenilin-1 knockin mice
    • Leissring, M. A. et al. Capacitative calcium entry deficits and elevated luminal calcium content in mutant presenilin-1 knockin mice. J. Cell Biol. 149, 793-798 (2000).
    • (2000) J. Cell Biol. , vol.149 , pp. 793-798
    • Leissring, M.A.1
  • 9
    • 0026570528 scopus 로고
    • β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity
    • Mattson, M. P. et al. β-Amyloid peptides destabilize calcium homeostasis and render human cortical neurons vulnerable to excitotoxicity. J. Neurosci. 12, 376-389 (1992).
    • (1992) J. Neurosci. , vol.12 , pp. 376-389
    • Mattson, M.P.1
  • 10
    • 0027297138 scopus 로고
    • Calcium- destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF
    • Mattson, M. P, Tomaselli, K. J. & Rydel, R. E. Calcium- destabilizing and neurodegenerative effects of aggregated β-amyloid peptide are attenuated by basic FGF. Brain Res. 621, 35-49 (1993).
    • (1993) Brain Res , vol.621 , pp. 35-49
    • Mattson, M.P.1    Tomaselli, K.J.2    Rydel, R.E.3
  • 11
    • 0033712477 scopus 로고    scopus 로고
    • Presenilin-mediated modulation of capacitative calcium entry
    • Yoo, A. S. et al. Presenilin-mediated modulation of capacitative calcium entry. Neuron 27, 561-572 (2000).
    • (2000) Neuron , vol.27 , pp. 561-572
    • Yoo, A.S.1
  • 12
    • 0032895651 scopus 로고    scopus 로고
    • Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation
    • Chui, D. H. et al. Transgenic mice with Alzheimer presenilin 1 mutations show accelerated neurodegeneration without amyloid plaque formation. Nature Med. 5, 560-564 (1999).
    • (1999) Nature Med , vol.5 , pp. 560-564
    • Chui, D.H.1
  • 13
    • 0037007140 scopus 로고    scopus 로고
    • A physiologic signaling role for the γ-secretase-derived intracellular fragment of APP Proc
    • Leissring, M. A. et al. A physiologic signaling role for the γ-secretase-derived intracellular fragment of APP Proc. Natl Acad. Sci. USA 99, 4697-4702 (2002).
    • (2002) Natl Acad. Sci. USA , vol.99 , pp. 4697-4702
    • Leissring, M.A.1
  • 14
    • 0027526631 scopus 로고
    • Comparison of the effects of elevated intracellular aluminum and calcium levels on neuronal survival and tau immunoreactivity
    • Mattson, M. P, Lovell, M. A., Ehmann, W. D. & Markesbery, W. R. Comparison of the effects of elevated intracellular aluminum and calcium levels on neuronal survival and tau immunoreactivity. Brain Res. 602, 21-31 (1993).
    • (1993) Brain Res , vol.602 , pp. 21-31
    • Mattson, M.P.1    Lovell, M.A.2    Ehmann, W.D.3    Markesbery, W.R.4
  • 15
    • 0025273543 scopus 로고
    • Antigenic changes similar to those seen in neurofibrillary tangles are elicited by glutamate and Ca2+ influx in cultured hippocampal neurons
    • 2+influx in cultured hippocampal neurons. Neuron 4, 105-117 (1990).
    • (1990) Neuron , vol.4 , pp. 105-117
    • Mattson, M.P.1
  • 16
    • 0029873515 scopus 로고    scopus 로고
    • Mice deficient for the amyloid precursor protein gene
    • Zheng, H. et al. Mice deficient for the amyloid precursor protein gene. Ann. NY Acad. Sci. 777, 421-426 (1996).
    • (1996) Ann. NY Acad. Sci , vol.777 , pp. 421-426
    • Zheng, H.1
  • 17
    • 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, 7951-7963 (2000).
    • (2000) J. Neurosci. , vol.20 , pp. 7951-7963
    • Heber, S.1
  • 18
    • 0031470093 scopus 로고    scopus 로고
    • Generation of APLP2 KO mice and early postnatal lethality in APLP2/APP double KO mice
    • von Koch, C. S. et al. Generation of APLP2 KO mice and early postnatal lethality in APLP2/APP double KO mice. Neurobiol. Aging 18, 661-669 (1997).
    • (1997) Neurobiol. Aging , vol.18 , pp. 661-669
    • Von Koch, C.S.1
  • 19
    • 0033636136 scopus 로고    scopus 로고
    • Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I
    • Kamal, A., Stokin, G. B., Yang, Z., Xia, C. H. & Goldstein, L. S. Axonal transport of amyloid precursor protein is mediated by direct binding to the kinesin light chain subunit of kinesin-I. Neuron 28, 449-459 (2000).
    • (2000) Neuron , vol.28 , pp. 449-459
    • Kamal, A.1    Stokin, G.B.2    Yang, Z.3    Xia, C.H.4    Goldstein, L.S.5
  • 20
    • 0035818998 scopus 로고    scopus 로고
    • Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP
    • Kamal, A., Almenar-Queralt, A., LeBlanc, J. F., Roberts, E. A. & Goldstein, L. S. Kinesin-mediated axonal transport of a membrane compartment containing β-secretase and presenilin-1 requires APP. Nature 414, 643-648 (2001).
    • (2001) Nature , vol.414 , pp. 643-648
    • Kamal, A.1    Almenar-Queralt, A.2    Leblanc, J.F.3    Roberts, E.A.4    Goldstein, L.S.5
  • 21
    • 0027447656 scopus 로고
    • Alzheimer amyloid protein precursor complexes with brain GTP-binding protein Go
    • o. Nature 362, 75-79 (1993).
    • (1993) Nature , vol.362 , pp. 75-79
    • Nishimoto, I.1
  • 22
    • 0029739316 scopus 로고    scopus 로고
    • Intrinsic signaling function of APP as a novel target of three V642 mutations linked to familial Alzheimer's disease
    • Okamoto, T. et al. Intrinsic signaling function of APP as a novel target of three V642 mutations linked to familial Alzheimer's disease. EMBO J. 15, 3769-3777 (1996).
    • (1996) EMBO J , vol.15 , pp. 3769-3777
    • Okamoto, T.1
  • 23
    • 0037036463 scopus 로고    scopus 로고
    • Amyloid precursor protein family-induced neuronal death is mediated by impairment of the neuroprotective calcium/calmodulin protein kinase IV-dependent signaling pathway
    • Mbebi, C. et al. Amyloid precursor protein family-induced neuronal death is mediated by impairment of the neuroprotective calcium/calmodulin protein kinase IV-dependent signaling pathway. J. Biol. Chem. 277, 20979-20990 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 20979-20990
    • Mbebi, C.1
  • 24
    • 0035864169 scopus 로고    scopus 로고
    • Amyloid β42 activates a G-protein-coupled chemoattractant receptor, FPR-like-1
    • Le, Y. et al. Amyloid β42 activates a G-protein-coupled chemoattractant receptor, FPR-like-1. J. Neurosci. 21, RC123 (2001).
    • (2001) J. Neurosci , vol.21 , pp. RC123
    • Le, Y.1
  • 25
    • 0035816661 scopus 로고    scopus 로고
    • A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60
    • Cao, X. & Sudhof, T. C. A transcriptionally active complex of APP with Fe65 and histone acetyltransferase Tip60. Science 293, 115-120 (2001).
    • (2001) Science , vol.293 , pp. 115-120
    • Cao, X.1    Sudhof, T.C.2
  • 26
    • 0028169905 scopus 로고
    • P Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid p-peptide-induced oxidative injury
    • Goodman, Y. & Mattson, M. P Secreted forms of β-amyloid precursor protein protect hippocampal neurons against amyloid p-peptide-induced oxidative injury. Exp. Neurol. 128, 1-12 (1994).
    • (1994) Exp. Neurol. , vol.128 , pp. 1-12
    • Goodman, Y.1    Mattson, M.2
  • 27
    • 0027478347 scopus 로고
    • Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein
    • Mattson, M. P. et al. Evidence for excitoprotective and intraneuronal calcium-regulating roles for secreted forms of the β-amyloid precursor protein. Neuron 10, 243-254 (1993).
    • (1993) Neuron , vol.10 , pp. 243-254
    • Mattson, M.P.1
  • 28
    • 0028175579 scopus 로고
    • Secreted forms of β-amyloid precursor protein modulate dendrite outgrowth and calcium responses to glutamate in cultured embryonic hippocampal neurons
    • Mattson, M. P. Secreted forms of β-amyloid precursor protein modulate dendrite outgrowth and calcium responses to glutamate in cultured embryonic hippocampal neurons. J. Neurobiol. 25, 439-450 (1994).
    • (1994) J. Neurobiol. , vol.25 , pp. 439-450
    • Mattson, M.P.1
  • 29
    • 0031944765 scopus 로고    scopus 로고
    • The effect of a secreted form of β-amyloid- precursor protein on intracellular Ca2+ increase in rat cultured hippocampal neurones
    • 2+ increase in rat cultured hippocampal neurones. Br. J. Pharmacol. 123, 1483-1489 (1998).
    • (1998) Br. J. Pharmacol. , vol.123 , pp. 1483-1489
    • Koizumi, S.1
  • 30
    • 0028912956 scopus 로고
    • Role of cyclic GMP in the regulation of neuronal calcium and survival by secreted forms of β-amyloid precursor
    • Barger, S. W., Fiscus, R. R., Ruth, P., Hofmann, F. & Mattson, M. P. Role of cyclic GMP in the regulation of neuronal calcium and survival by secreted forms of β-amyloid precursor. J. Neurochem. 64, 2087-2096 (1995).
    • (1995) J. Neurochem. , vol.64 , pp. 2087-2096
    • Barger, S.W.1    Fiscus, R.R.2    Ruth, P.3    Hofmann, F.4    Mattson, M.P.5
  • 31
    • 0032704781 scopus 로고    scopus 로고
    • Suppression of an amyloid β peptide- mediated calcium channel response by a secreted β-amyloid precursor protein
    • Li, W. Y. et al. Suppression of an amyloid β peptide- mediated calcium channel response by a secreted β-amyloid precursor protein. Neuroscience 95, 1-4 (2000).
    • (2000) Neuroscience , vol.95 , pp. 1-4
    • Li, W.Y.1
  • 32
    • 0032524319 scopus 로고    scopus 로고
    • Secreted β-amyloid precursor protein counteracts the proapoptotic action of mutant presenilin-1 by activation of NF- κB and stabilization of calcium homeostasis
    • Guo, Q., Robinson, N. & Mattson, M. P. Secreted β-amyloid precursor protein counteracts the proapoptotic action of mutant presenilin-1 by activation of NF- κB and stabilization of calcium homeostasis. J. Biol. Chem. 273, 12341-12351 (1998).
    • (1998) J. Biol. Chem. , vol.273 , pp. 12341-12351
    • Guo, Q.1    Robinson, N.2    Mattson, M.P.3
  • 33
    • 0032514633 scopus 로고    scopus 로고
    • Memory-enhancing effects of secreted forms of the β-amyloid precursor protein in normal and amnestic mice
    • Meziane, H. et al. Memory-enhancing effects of secreted forms of the β-amyloid precursor protein in normal and amnestic mice. Proc. Natl Acad. Sci. USA 95, 12683-12688 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12683-12688
    • Meziane, H.1
  • 34
    • 0028650421 scopus 로고
    • Calcium and neuronal injury in Alzheimer's disease. Contributions of β-amyloid precursor protein mismetabolism, free radicals, and metabolic compromise
    • Mattson, M. P. Calcium and neuronal injury in Alzheimer's disease. Contributions of β-amyloid precursor protein mismetabolism, free radicals, and metabolic compromise. Ann. NY Acad. Sci. 747, 50-76 (1994).
    • (1994) Ann. NY Acad. Sci. , vol.747 , pp. 50-76
    • Mattson, M.P.1
  • 35
    • 0028656522 scopus 로고
    • Calcium-activated neutral proteinase (Calpain) system in aging and Alzheimer's disease
    • Nixon, R. A. et al. Calcium-activated neutral proteinase (calpain) system in aging and Alzheimer's disease. Ann. NY Acad. Sci. 747, 77-91 (1994).
    • (1994) Ann. NY Acad. Sci , vol.747 , pp. 77-91
    • Nixon, R.A.1
  • 36
    • 0026349379 scopus 로고
    • Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons
    • Mattson, M. P., Engle, M. G. & Rychlik, B. Effects of elevated intracellular calcium levels on the cytoskeleton and tau in cultured human cortical neurons. Mol. Chem. Neuropathol. 15, 117-142 (1991).
    • (1991) Mol. Chem. Neuropathol. , vol.15 , pp. 117-142
    • Mattson, M.P.1    Engle, M.G.2    Rychlik, B.3
  • 37
    • 0029175202 scopus 로고
    • Calcium, free radicals, and excitotoxic neuronal death in primary cell culture
    • Mattson, M. P., Barger, S. W., Begley, J. G. & Mark, R. J. Calcium, free radicals, and excitotoxic neuronal death in primary cell culture. Methods Cell Biol. 46, 187-216 (1995).
    • (1995) Methods Cell Biol , vol.46 , pp. 187-216
    • Mattson, M.P.1    Barger, S.W.2    Begley, J.G.3    Mark, R.J.4
  • 38
    • 0029162101 scopus 로고
    • Free radicals and disruption of neuronal ion homeostasis in AD: A role for amyloid β-peptide? Neurobiol
    • Mattson, M. P. Free radicals and disruption of neuronal ion homeostasis in AD: a role for amyloid β-peptide? Neurobiol. Aging 16, 679-682 (1995).
    • (1995) Aging , vol.16 , pp. 679-682
    • Mattson, M.P.1
  • 39
    • 0031470172 scopus 로고    scopus 로고
    • Abnormalities in Alzheimer's disease fibroblasts bearing the APP670/671 mutation
    • Gibson, G. E. et al. Abnormalities in Alzheimer's disease fibroblasts bearing the APP670/671 mutation. Neurobiol. Aging 18, 573-580 (1997).
    • (1997) Neurobiol. Aging , vol.18 , pp. 573-580
    • Gibson, G.E.1
  • 40
    • 0035997234 scopus 로고    scopus 로고
    • The channel hypothesis of Alzheimer's disease: Current status
    • Kagan, B. L., Hirakura, Y., Azimov, R., Azimova, R. & Lin, M. C. The channel hypothesis of Alzheimer's disease: current status. Peptides 23, 1311-1315 (2002).
    • (2002) Peptides , vol.23 , pp. 1311-1315
    • Kagan, B.L.1    Hirakura, Y.2    Azimov, R.3    Azimova, R.4    Lin, M.C.5
  • 41
    • 0027508926 scopus 로고
    • Alzheimer disease amyloid p protein forms calcium channels in bilayer membranes: Blockade by tromethamine and aluminum
    • Arispe, N., Rojas, E. & Pollard, H. B. Alzheimer disease amyloid p protein forms calcium channels in bilayer membranes: blockade by tromethamine and aluminum. Proc. Natl Acad. Sci. USA 90, 567-571 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 567-571
    • Arispe, N.1    Rojas, E.2    Pollard, H.B.3
  • 42
    • 0027490362 scopus 로고
    • Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP-(1-40)] in bilayer membranes
    • Arispe, N., Pollard, H. B. & Rojas, E. Giant multilevel cation channels formed by Alzheimer disease amyloid β-protein [AβP-(1-40)] in bilayer membranes. Proc. Natl Acad. Sci. USA 90, 10573-10577 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 10573-10577
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 43
    • 0028649480 scopus 로고
    • The ability of amyloid β-protein [AβP (1 -40)] to form Ca2+ channels provides a mechanism for neuronal death in Alzheimer's disease
    • 2+ channels provides a mechanism for neuronal death in Alzheimer's disease. Ann. NY Acad. Sci. 747, 256-266 (1994).
    • (1994) Ann. NY Acad. Sci. , vol.747 , pp. 256-266
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 44
    • 0028670272 scopus 로고
    • β-Amyloid Ca2+- channel hypothesis for neuronal death in Alzheimer disease
    • 2+- channel hypothesis for neuronal death in Alzheimer disease. Mol. Cell. Biochem. 140, 119-125 (1994).
    • (1994) Mol. Cell. Biochem. , vol.140 , pp. 119-125
    • Arispe, N.1    Pollard, H.B.2    Rojas, E.3
  • 45
    • 0034087948 scopus 로고    scopus 로고
    • Fresh and globular amyloid β protein (1 -42) induces rapid cellular degeneration: Evidence for AβP channel-mediated cellular toxicity
    • Bhatia, R., Lin, H. & Lal, R. Fresh and globular amyloid β protein (1 -42) induces rapid cellular degeneration: evidence for AβP channel-mediated cellular toxicity. FASEB J. 14, 1233-1243 (2000).
    • (2000) FASEB J , vol.14 , pp. 1233-1243
    • Bhatia, R.1    Lin, H.2    Lal, R.3
  • 46
    • 0034319190 scopus 로고    scopus 로고
    • Molecular mechanism of neurodegeneration induced by Alzheimer's β-amyloid protein: Channel formation and disruption of calcium homeostasis
    • Kawahara, M. & Kuroda, Y. Molecular mechanism of neurodegeneration induced by Alzheimer's β-amyloid protein: channel formation and disruption of calcium homeostasis. Brain Res. Bull. 53, 389-397 (2000).
    • (2000) Brain Res. Bull. , vol.53 , pp. 389-397
    • Kawahara, M.1    Kuroda, Y.2
  • 47
    • 0031024927 scopus 로고    scopus 로고
    • Channel formation by a neurotoxic prion protein fragment
    • Lin, M. C., Mirzabekov, T. & Kagan, B. L. Channel formation by a neurotoxic prion protein fragment. J. Biol. Chem. 272, 44-47 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 44-47
    • Lin, M.C.1    Mirzabekov, T.2    Kagan, B.L.3
  • 48
    • 0030044018 scopus 로고    scopus 로고
    • Pore formation by the cytotoxic islet amyloid peptide amylin
    • Mirzabekov, T. A., Lin, M. C. & Kagan, B. L. Pore formation by the cytotoxic islet amyloid peptide amylin. J. Biol. Chem. 271, 1988-1992 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 1988-1992
    • Mirzabekov, T.A.1    Lin, M.C.2    Kagan, B.L.3
  • 49
    • 0034640372 scopus 로고    scopus 로고
    • Alzheimer's β-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line
    • Kawahara, M., Kuroda, Y., Arispe, N. & Rojas, E. Alzheimer's β-amyloid, human islet amylin, and prion protein fragment evoke intracellular free calcium elevations by a common mechanism in a hypothalamic GnRH neuronal cell line. J. Biol. Chem. 275, 14077-14083 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14077-14083
    • Kawahara, M.1    Kuroda, Y.2    Arispe, N.3    Rojas, E.4
  • 50
    • 0028180518 scopus 로고
    • A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: Relevance to Alzheimer disease
    • Hensley, K. et al. A model for β-amyloid aggregation and neurotoxicity based on free radical generation by the peptide: relevance to Alzheimer disease. Proc. Natl Acad. Sci. USA 91, 3270-3274 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3270-3274
    • Hensley, K.1
  • 52
    • 0029924284 scopus 로고    scopus 로고
    • Estrogens attenuate and corticosterone exacerbates excitotoxicity, oxidative injury, and amyloid β-peptide toxicity in hippocampal neurons
    • Goodman, Y., Bruce, A. J., Cheng, B. & Mattson, M. P. Estrogens attenuate and corticosterone exacerbates excitotoxicity, oxidative injury, and amyloid β-peptide toxicity in hippocampal neurons. J. Neurochem. 66, 1836-1844 (1996).
    • (1996) J. Neurochem. , vol.66 , pp. 1836-1844
    • Goodman, Y.1    Bruce, A.J.2    Cheng, B.3    Mattson, M.P.4
  • 53
    • 0030608841 scopus 로고    scopus 로고
    • 17β-Estradiol attenuates oxidative impairment of synaptic Na+/K+-ATPase activity, glucose transport, and glutamate transport induced by amyloid p-peptide and iron
    • +-ATPase activity, glucose transport, and glutamate transport induced by amyloid p-peptide and iron. J. Neurosci. Res. 50, 522-530 (1997).
    • (1997) J. Neurosci. Res. , vol.50 , pp. 522-530
    • Keller, J.N.1    Germeyer, A.2    Begley, J.G.3    Mattson, M.P.4
  • 54
    • 0028204224 scopus 로고
    • Calcium ionophore increases amyloid β peptide production by cultured cells
    • Querfurth, H. W. & Selkoe, D. J. Calcium ionophore increases amyloid β peptide production by cultured cells. Biochemistry 33, 4550-4561 (1994).
    • (1994) Biochemistry , vol.33 , pp. 4550-4561
    • Querfurth, H.W.1    Selkoe, D.J.2
  • 55
    • 0030987603 scopus 로고    scopus 로고
    • Caffeine stimulates amyloid β-peptide release from p-amyloid precursor protein-transfected HEK293 cells
    • Querfurth, H. W., Jiang, J., Geiger, J. D. & Selkoe, D. J. Caffeine stimulates amyloid β-peptide release from p-amyloid precursor protein-transfected HEK293 cells. J. Neurochem. 69, 1580-1591 (1997).
    • (1997) J. Neurochem. , vol.69 , pp. 1580-1591
    • Querfurth, H.W.1    Jiang, J.2    Geiger, J.D.3    Selkoe, D.J.4
  • 56
    • 0028207004 scopus 로고
    • Calcium regulates processing of the Alzheimer amyloid protein precursor in a protein kinase C-independent manner
    • Buxbaum, J. D., Ruefli, A. A., Parker, C. A., Cypess, A. M. & Greengard, P. Calcium regulates processing of the Alzheimer amyloid protein precursor in a protein kinase C-independent manner. Proc. Natl Acad. Sci. USA 91, 4489-4493 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4489-4493
    • Buxbaum, J.D.1    Ruefli, A.A.2    Parker, C.A.3    Cypess, A.M.4    Greengard, P.5
  • 57
    • 0346631295 scopus 로고    scopus 로고
    • Modulation of β-amyloid production through calcium signaling pathways
    • (in the press)
    • Akbari, Y. et al. Modulation of β-amyloid production through calcium signaling pathways. Soc. Neurosci. Abstr. 28 (in the press).
    • Soc. Neurosci. Abstr , vol.28
    • Akbari, Y.1
  • 58
    • 0030769092 scopus 로고    scopus 로고
    • Alzheimer's AβV42 is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells
    • V42 is generated in the endoplasmic reticulum/intermediate compartment of NT2N cells. Nature Med. 3, 1021-1023 (1997).
    • (1997) Nature Med , vol.3 , pp. 1021-1023
    • Cook, D.G.1
  • 59
    • 0035949487 scopus 로고    scopus 로고
    • Presenilin, Notch, and the genesis and treatment of Alzheimer's disease
    • Selkoe, D. J. Presenilin, Notch, and the genesis and treatment of Alzheimer's disease. Proc. Natl Acad. Sci. USA 98, 11039-11041 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 11039-11041
    • Selkoe, D.J.1
  • 60
    • 0032556859 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein
    • De Strooper, B. et al. Deficiency of presenilin-1 inhibits the normal cleavage of amyloid precursor protein. Nature 391, 387-390 (1998).
    • (1998) Nature , vol.391 , pp. 387-390
    • De Strooper, B.1
  • 61
    • 0033535504 scopus 로고    scopus 로고
    • A presenilin-1-dependent y-secretase- like protease mediates release of Notch intracellular domain
    • De Strooper, B. et al. A presenilin-1-dependent y-secretase- like protease mediates release of Notch intracellular domain. Nature 398, 518-522 (1999).
    • (1999) Nature , vol.398 , pp. 518-522
    • De Strooper, B.1
  • 62
    • 0035824391 scopus 로고    scopus 로고
    • γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase
    • Ni, C. Y., Murphy, M. P., Golde, T. E. & Carpenter, G. γ-Secretase cleavage and nuclear localization of ErbB-4 receptor tyrosine kinase. Science 294, 2179-2181 (2001).
    • (2001) Science , vol.294 , pp. 2179-2181
    • Ni, C.Y.1    Murphy, M.P.2    Golde, T.E.3    Carpenter, G.4
  • 63
    • 0037155219 scopus 로고    scopus 로고
    • Presenilin-dependent γ-secretase-like intramembrane cleavage of ErbB4
    • Lee, H. J. et al. Presenilin-dependent γ-secretase-like intramembrane cleavage of ErbB4. J. Biol. Chem. 277, 6318-6323 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 6318-6323
    • Lee, H.J.1
  • 64
    • 18344380083 scopus 로고    scopus 로고
    • A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions
    • Marambaud, P et al. A presenilin-1/γ-secretase cleavage releases the E-cadherin intracellular domain and regulates disassembly of adherens junctions. EMBO J. 21, 1948-1956 (2002).
    • (2002) EMBO J , vol.21 , pp. 1948-1956
    • Marambaud, P.1
  • 65
    • 16044373524 scopus 로고    scopus 로고
    • Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased In vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease
    • Scheuner, D. et al. Secreted amyloid β-protein similar to that in the senile plaques of Alzheimer's disease is increased In vivo by the presenilin 1 and 2 and APP mutations linked to familial Alzheimer's disease. Nature Med. 2, 864-870 (1996).
    • (1996) Nature Med , vol.2 , pp. 864-870
    • Scheuner, D.1
  • 66
    • 0034621824 scopus 로고    scopus 로고
    • Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1
    • Li, Y. M. et al. Photoactivated γ-secretase inhibitors directed to the active site covalently label presenilin 1. Nature 405, 689-694 (2000).
    • (2000) Nature , vol.405 , pp. 689-694
    • Li, Y.M.1
  • 67
    • 0033535553 scopus 로고    scopus 로고
    • Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity
    • Wolfe, M. S. et al. Two transmembrane aspartates in presenilin-1 required for presenilin endoproteolysis and γ-secretase activity. Nature 398, 513-517 (1999).
    • (1999) Nature , vol.398 , pp. 513-517
    • Wolfe, M.S.1
  • 68
    • 0037150534 scopus 로고    scopus 로고
    • Intramembrane proteases — mixing oil and water
    • Wolfe, M. S. & Selkoe, D. J. Intramembrane proteases — mixing oil and water. Science 296, 2156-2157 (2002).
    • (2002) Science , vol.296 , pp. 2156-2157
    • Wolfe, M.S.1    Selkoe, D.J.2
  • 69
    • 0035106128 scopus 로고    scopus 로고
    • Presenilin and γ-secretase: Structure meets function
    • Wolfe, M. S. Presenilin and γ-secretase: structure meets function. J. Neurochem. 76, 1615-1620 (2001).
    • (2001) J. Neurochem. , vol.76 , pp. 1615-1620
    • Wolfe, M.S.1
  • 70
    • 0037150672 scopus 로고    scopus 로고
    • Identification of signal peptide peptidase, a presenilin-type aspartic protease
    • Weihofen, A., Binns, K., Lemberg, M. K., Ashman, K. & Martoglio, B. Identification of signal peptide peptidase, a presenilin-type aspartic protease. Science 296, 2215-22218 (2002).
    • (2002) Science , vol.296 , pp. 2215-22218
    • Weihofen, A.1    Binns, K.2    Lemberg, M.K.3    Ashman, K.4    Martoglio, B.5
  • 71
    • 0036180950 scopus 로고    scopus 로고
    • Cholesterol-dependent γ-secretase activity in buoyant cholesterol-rich membrane microdomains
    • Wahrle, S. et al. Cholesterol-dependent γ-secretase activity in buoyant cholesterol-rich membrane microdomains. Neurobiol. Dis. 9, 11-23 (2002).
    • (2002) Neurobiol. Dis. , vol.9 , pp. 11-23
    • Wahrle, S.1
  • 72
    • 0034618715 scopus 로고    scopus 로고
    • Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and PAPP processing
    • Yu, G. et al. Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and PAPP processing. Nature 407, 48-54 (2000).
    • (2000) Nature , vol.407 , pp. 48-54
    • Yu, G.1
  • 73
    • 18444417998 scopus 로고    scopus 로고
    • Aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation
    • Francis, R. et al. aph-1 and pen-2 are required for Notch pathway signaling, γ-secretase cleavage of βAPP, and presenilin protein accumulation. Dev. Cell 3, 85-97 (2002).
    • (2002) Dev. Cell , vol.3 , pp. 85-97
    • Francis, R.1
  • 74
    • 0037204122 scopus 로고    scopus 로고
    • Aph-2/Nicastrin: An essential component of γ-secretase and regulator of Notch signaling and Presenilin localization
    • Kopan, R. & Goate, A. Aph-2/Nicastrin: an essential component of γ-secretase and regulator of Notch signaling and Presenilin localization. Neuron 33, 321-324 (2002).
    • (2002) Neuron , vol.33 , pp. 321-324
    • Kopan, R.1    Goate, A.2
  • 75
    • 0036727463 scopus 로고    scopus 로고
    • Presenilins are not required for AP42 production in the early secretory pathway
    • Wilson, C. A., Doms, R. W., Zheng, H. & Lee, V M. Presenilins are not required for AP42 production in the early secretory pathway. Nature Neurosci. 5, 849-855 (2002).
    • (2002) Nature Neurosci , vol.5 , pp. 849-855
    • Wilson, C.A.1    Doms, R.W.2    Zheng, H.3    Lee, V.M.4
  • 76
    • 0034882422 scopus 로고    scopus 로고
    • Deficiency of presenilin-1 increases calcium-dependent vulnerability of neurons to oxidative stress in vitro
    • Nakajima, M., Miura, M., Aosaki, T. & Shirasawa, T. Deficiency of presenilin-1 increases calcium-dependent vulnerability of neurons to oxidative stress in vitro. J. Neurochem. 78, 807-814 (2001).
    • (2001) J. Neurochem. , vol.78 , pp. 807-814
    • Nakajima, M.1    Miura, M.2    Aosaki, T.3    Shirasawa, T.4
  • 77
    • 0028179578 scopus 로고
    • Internal Ca2+ mobilization is altered in fibroblasts from patients with Alzheimer disease
    • 2+ mobilization is altered in fibroblasts from patients with Alzheimer disease. Proc. Natl Acad. Sci. USA 91, 534-538 (1994).
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 534-538
    • Ito, E.1
  • 78
    • 0032972683 scopus 로고    scopus 로고
    • Alzheimer's presenilin-1 mutation potentiates inositol 1, 4, 5-trisphosphate-mediated calcium signaling in Xenopus oocytes
    • Leissring, M. A., Paul, B. A., Parker, I., Cotman, C. W. & LaFerla, F. M. Alzheimer's presenilin-1 mutation potentiates inositol 1, 4, 5-trisphosphate-mediated calcium signaling in Xenopus oocytes. J. Neurochem. 72, 1061-1068 (1999).
    • (1999) J. Neurochem , vol.72 , pp. 1061-1068
    • Leissring, M.A.1    Paul, B.A.2    Parker, I.3    Cotman, C.W.4    Laferla, F.M.5
  • 79
    • 84984777875 scopus 로고    scopus 로고
    • Ca2+stores and capacitative Ca2+entry in human neuroblastoma (SH-SY5Y) cells expressing a familial Alzheimer's disease presenilin-1 mutation
    • (in the press)
    • 2+entry in human neuroblastoma (SH-SY5Y) cells expressing a familial Alzheimer's disease presenilin-1 mutation. Brain Res. (in the press).
    • Brain Res
    • Smith, I.F.1
  • 80
    • 0036310603 scopus 로고    scopus 로고
    • Different calcium sources are narrowly tuned to the induction of different forms of LTP
    • Raymond, C. R. & Redman, S. J. Different calcium sources are narrowly tuned to the induction of different forms of LTP J. Neurophysiol. 88, 249-255 (2002).
    • (2002) J. Neurophysiol , vol.88 , pp. 249-255
    • Raymond, C.R.1    Redman, S.J.2
  • 81
    • 0032945724 scopus 로고    scopus 로고
    • Synaptic transmission and hippocampal long-term potentiation in transgenic mice expressing FAD-linked presenilin 1
    • Parent, A., Linden, D. J., Sisodia, S. S. & Borchelt, D. R. Synaptic transmission and hippocampal long-term potentiation in transgenic mice expressing FAD-linked presenilin 1. Neurobiol. Dis. 6, 56-62 (1999).
    • (1999) Neurobiol. Dis. , vol.6 , pp. 56-62
    • Parent, A.1    Linden, D.J.2    Sisodia, S.S.3    Borchelt, D.R.4
  • 82
    • 0034095106 scopus 로고    scopus 로고
    • Enhanced synaptic potentiation in transgenic mice expressing presenilin 1 familial Alzheimer's disease mutation is normalized with a benzodiazepine
    • Zaman, S. H. et al. Enhanced synaptic potentiation in transgenic mice expressing presenilin 1 familial Alzheimer's disease mutation is normalized with a benzodiazepine. Neurobiol. Dis. 7, 54-63 (2000).
    • (2000) Neurobiol. Dis. , vol.7 , pp. 54-63
    • Zaman, S.H.1
  • 83
    • 0034058834 scopus 로고    scopus 로고
    • Functional phenotype in transgenic mice expressing mutant human presenilin-1
    • Barrow, P. A. et al. Functional phenotype in transgenic mice expressing mutant human presenilin-1. Neurobiol. Dis. 7, 119-126 (2000).
    • (2000) Neurobiol. Dis. , vol.7 , pp. 119-126
    • Barrow, P.A.1
  • 84
    • 0034674730 scopus 로고    scopus 로고
    • Presenilin-1 mutations increase levels of ryanodine receptors and calcium release in PC12 cells and cortical neurons
    • Chan, S. L., Mayne, M., Holden, C. P., Geiger, J. D. & Mattson, M. P Presenilin-1 mutations increase levels of ryanodine receptors and calcium release in PC12 cells and cortical neurons. J. Biol. Chem. 275, 18195-18200 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 18195-18200
    • Chan, S.L.1    Mayne, M.2    Holden, C.P.3    Geiger, J.D.4    Mattson, M.P.5
  • 85
    • 0037183702 scopus 로고    scopus 로고
    • The presenilin 1 AE9 mutation gives enhanced basal phospholipase C activity and a resultant increase in intracellular calcium concentrations
    • Cedazo-Minguez, A., Popescu, B. O., Ankarcrona, M., Nishimura, T. & Cowburn, R. F. The presenilin 1 AE9 mutation gives enhanced basal phospholipase C activity and a resultant increase in intracellular calcium concentrations. J. Biol. Chem. 277, 36646-36655 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 36646-36655
    • Cedazo-Minguez, A.1    Popescu, B.O.2    Ankarcrona, M.3    Nishimura, T.4    Cowburn, R.F.5
  • 86
    • 0032539814 scopus 로고    scopus 로고
    • P Calbindin D28k blocks the proapoptotic actions of mutant presenilin 1: Reduced oxidative stress and preserved mitochondrial function
    • Guo, Q., Christakos, S., Robinson, N. & Mattson, M. P Calbindin D28k blocks the proapoptotic actions of mutant presenilin 1: reduced oxidative stress and preserved mitochondrial function. Proc. Natl Acad. Sci. USA 95, 3227-3232 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 3227-3232
    • Guo, Q.1    Christakos, S.2    Robinson, N.3    Mattson, M.4
  • 87
    • 0031721511 scopus 로고    scopus 로고
    • Calsenilin: A calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment
    • Buxbaum, J. D. et al. Calsenilin: a calcium-binding protein that interacts with the presenilins and regulates the levels of a presenilin fragment. Nature Med. 4, 1177-1181 (1998).
    • (1998) Nature Med , vol.4 , pp. 1177-1181
    • Buxbaum, J.D.1
  • 88
    • 0034682541 scopus 로고    scopus 로고
    • Calsenilin reverses presenilin-mediated enhancement of calcium signaling
    • Leissring, M. A. et al. Calsenilin reverses presenilin-mediated enhancement of calcium signaling. Proc. Natl Acad. Sci. USA 97, 8590-8593 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 8590-8593
    • Leissring, M.A.1
  • 91
    • 0034210793 scopus 로고    scopus 로고
    • Binding partners of Alzheimer's disease proteins: Are they physiologically relevant?
    • Van Gassen, G., Annaert, W. & Van Broeckhoven, C. Binding partners of Alzheimer's disease proteins: are they physiologically relevant? Neurobiol. Dis. 7, 135-151 (2000).
    • (2000) Neurobiol. Dis. , vol.7 , pp. 135-151
    • Van Gassen, G.1    Annaert, W.2    Van Broeckhoven, C.3
  • 92
    • 0033553908 scopus 로고    scopus 로고
    • A myristoylated calcium-binding protein that preferentially interacts with the Alzheimer's disease presenilin 2 protein
    • Stabler, S. M., Ostrowski, L. L., Janicki, S. M. & Monteiro, M. J. A myristoylated calcium-binding protein that preferentially interacts with the Alzheimer's disease presenilin 2 protein. J. Cell Biol. 145, 1277-1292 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 1277-1292
    • Stabler, S.M.1    Ostrowski, L.L.2    Janicki, S.M.3    Monteiro, M.J.4
  • 93
    • 0032057279 scopus 로고    scopus 로고
    • The presenilin 2 loop domain interacts with the µ-calpain C-terminal region
    • Shinozaki, K. et al. The presenilin 2 loop domain interacts with the µ-calpain C-terminal region. Int. J. Mol. Med. 1, 797-799 (1998).
    • (1998) Int. J. Mol. Med. , vol.1 , pp. 797-799
    • Shinozaki, K.1
  • 94
    • 0034640292 scopus 로고    scopus 로고
    • Presenilin 2 interacts with sorcin, a modulator of the ryanodine receptor
    • Pack-Chung, E. et al. Presenilin 2 interacts with sorcin, a modulator of the ryanodine receptor. J. Biol. Chem. 275, 14440-14445 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 14440-14445
    • Pack-Chung, E.1
  • 95
    • 0032704888 scopus 로고    scopus 로고
    • Presenilin-2 mutations modulate amplitude and kinetics of inositol 1, 4, 5- trisphosphate-mediated calcium signals
    • Leissring, M. A., Parker, I. & LaFerla, F. M. Presenilin-2 mutations modulate amplitude and kinetics of inositol 1, 4, 5- trisphosphate-mediated calcium signals. J. Biol. Chem. 274, 32535-32538 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 32535-32538
    • Leissring, M.A.1    Parker, I.2    Laferla, F.M.3
  • 96
    • 0034488295 scopus 로고    scopus 로고
    • Generation of an apoptotic intracellular peptide by γ-secretase cleavage of Alzheimer's amyloid-β protein precursor
    • Passer, B. et al. Generation of an apoptotic intracellular peptide by γ-secretase cleavage of Alzheimer's amyloid-β protein precursor. J. Alzheimers Dis. 2, 289-301 (2000).
    • (2000) J. Alzheimers Dis. , vol.2 , pp. 289-301
    • Passer, B.1
  • 97
    • 0035941278 scopus 로고    scopus 로고
    • Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment y. Evidence for distinct mechanisms involved in y-secretase processing of the APP and Notch1 transmembrane domains
    • Yu, C. et al. Characterization of a presenilin-mediated amyloid precursor protein carboxyl-terminal fragment y. Evidence for distinct mechanisms involved in y-secretase processing of the APP and Notch1 transmembrane domains. J. Biol. Chem. 276, 43756-43760 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 43756-43760
    • Yu, C.1
  • 98
    • 18444391830 scopus 로고    scopus 로고
    • Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Aβ42 production
    • Moehlmann, T. et al. Presenilin-1 mutations of leucine 166 equally affect the generation of the Notch and APP intracellular domains independent of their effect on Aβ42 production. Proc. Natl Acad. Sci. USA 99, 8025-8030 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 8025-8030
    • Moehlmann, T.1
  • 99
    • 0037176727 scopus 로고    scopus 로고
    • A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing
    • Weidemann, A. et al. A novel ε-cleavage within the transmembrane domain of the Alzheimer amyloid precursor protein demonstrates homology with Notch processing. Biochemistry 41, 2825-2835 (2002).
    • (2002) Biochemistry , vol.41 , pp. 2825-2835
    • Weidemann, A.1
  • 100
    • 0035929554 scopus 로고    scopus 로고
    • Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase- like cleavage of Notch
    • Gu, Y. et al. Distinct intramembrane cleavage of the β-amyloid precursor protein family resembling γ-secretase- like cleavage of Notch. J. Biol. Chem. 276, 35235-35238 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 35235-35238
    • Gu, Y.1
  • 101
    • 0037134505 scopus 로고    scopus 로고
    • Insulin-degrading enzyme rapidly removes the β-amyloid precursor protein intracellular domain (AICD)
    • Edbauer, D., Willem, M., Lammich, S., Steiner, H. & Haass, C. Insulin-degrading enzyme rapidly removes the β-amyloid precursor protein intracellular domain (AICD). J. Biol. Chem. 277, 13389-13393 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 13389-13393
    • Edbauer, D.1    Willem, M.2    Lammich, S.3    Steiner, H.4    Haass, C.5
  • 102
    • 0035955693 scopus 로고    scopus 로고
    • The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner
    • Kimberly, W. T, Zheng, J. B., Guenette, S. Y. & Selkoe, D. J. The intracellular domain of the β-amyloid precursor protein is stabilized by Fe65 and translocates to the nucleus in a notch-like manner. J. Biol. Chem. 276, 40288-40292 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 40288-40292
    • Kimberly, W.T.1    Zheng, J.B.2    Guenette, S.Y.3    Selkoe, D.J.4
  • 103
    • 0029598484 scopus 로고
    • The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein
    • Fiore, F. et al. The regions of the Fe65 protein homologous to the phosphotyrosine interaction/phosphotyrosine binding domain of Shc bind the intracellular domain of the Alzheimer's amyloid precursor protein. J. Biol. Chem. 270, 30853-30856 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 30853-30856
    • Fiore, F.1
  • 104
    • 0035794182 scopus 로고    scopus 로고
    • The β-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation
    • Minopoli, G. et al. The β-amyloid precursor protein functions as a cytosolic anchoring site that prevents Fe65 nuclear translocation. J. Biol. Chem. 276, 6545-6550 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 6545-6550
    • Minopoli, G.1
  • 105
    • 15844408798 scopus 로고    scopus 로고
    • APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein
    • Chow, N., Korenberg, J. R., Chen, X. N. & Neve, R. L. APP-BP1, a novel protein that binds to the carboxyl-terminal region of the amyloid precursor protein. J. Biol. Chem. 271, 11339-11346 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 11339-11346
    • Chow, N.1    Korenberg, J.R.2    Chen, X.N.3    Neve, R.L.4
  • 106
    • 0029805132 scopus 로고    scopus 로고
    • The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein
    • Borg, J. P., Ooi, J., Levy, E. & Margolis, B. The phosphotyrosine interaction domains of X11 and FE65 bind to distinct sites on the YENPTY motif of amyloid precursor protein. Mol. Cell. Biol. 16, 6229-6241 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 107
    • 0033599341 scopus 로고    scopus 로고
    • X11L2, a new member of the X11 protein family, interacts with Alzheimer's β-amyloid precursor protein
    • Tanahashi, H. & Tabira, T. X11L2, a new member of the X11 protein family, interacts with Alzheimer's β-amyloid precursor protein. Biochem. Biophys. Res. Commun. 255, 663-667 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.255 , pp. 663-667
    • Tanahashi, H.1    Tabira, T.2
  • 108
    • 0033198295 scopus 로고    scopus 로고
    • Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1
    • Homayouni, R., Rice, D. S., Sheldon, M. & Curran, T. Disabled-1 binds to the cytoplasmic domain of amyloid precursor-like protein 1. J. Neurosci. 19, 7507-7515 (1999).
    • (1999) J. Neurosci. , vol.19 , pp. 7507-7515
    • Homayouni, R.1    Rice, D.S.2    Sheldon, M.3    Curran, T.4
  • 109
    • 0033593480 scopus 로고    scopus 로고
    • Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein
    • Tomita, S. et al. Interaction of a neuron-specific protein containing PDZ domains with Alzheimer's amyloid precursor protein. J. Biol. Chem. 274, 2243-2254 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 2243-2254
    • Tomita, S.1
  • 110
    • 0035449943 scopus 로고    scopus 로고
    • C-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK
    • Matsuda, S. et al. c-Jun N-terminal kinase (JNK)-interacting protein-1b/islet-brain-1 scaffolds Alzheimer's amyloid precursor protein with JNK. J. Neurosci. 21, 6597-6607 (2001).
    • (2001) J. Neurosci. , vol.21 , pp. 6597-6607
    • Matsuda, S.1
  • 111
    • 0037053281 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the β-amyloid precursor protein cytoplasmic tail promotes interaction with Shc
    • Tarr, P. E., Roncarati, R., Pelicci, G., Pelicci, P. G. & D'Adamio, L. Tyrosine phosphorylation of the β-amyloid precursor protein cytoplasmic tail promotes interaction with Shc. J. Biol. Chem. 277, 16798-16804 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 16798-16804
    • Tarr, P.E.1    Roncarati, R.2    Pelicci, G.3    Pelicci, P.G.4    D'adamio, L.5
  • 112
    • 0037144497 scopus 로고    scopus 로고
    • Signal transduction through tyrosine- phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain
    • Russo, C. et al. Signal transduction through tyrosine- phosphorylated C-terminal fragments of amyloid precursor protein via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain. J. Biol. Chem. 277, 35282-35288 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 35282-35288
    • Russo, C.1
  • 113
    • 0035909901 scopus 로고    scopus 로고
    • The γ-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus
    • Gao, Y. & Pimplikar, S. W. The γ-secretase-cleaved C-terminal fragment of amyloid precursor protein mediates signaling to the nucleus. Proc. Natl Acad. Sci. USA 98, 14979-14984 (2001).
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 14979-14984
    • Gao, Y.1    Pimplikar, S.W.2
  • 114
    • 0032410747 scopus 로고    scopus 로고
    • PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein
    • Zheng, P., Eastman, J., Vande Pol, S. & Pimplikar, S. W. PAT1, a microtubule-interacting protein, recognizes the basolateral sorting signal of amyloid precursor protein. Proc. Natl Acad. Sci. USA 95, 14745-14750 (1998).
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 14745-14750
    • Zheng, P.1    Eastman, J.2    Vande Pol, S.3    Pimplikar, S.W.4
  • 115
    • 0037114010 scopus 로고    scopus 로고
    • Processing of β-amyloid precursor like protein-1 and -2 by γ-secretase regulates transcription
    • 12 September
    • Scheinfeld, M. H., Ghersi, E., Laky, K., Fowlkes, B. J. & D'Adamio, L. Processing of β-amyloid precursor like protein-1 and -2 by γ-secretase regulates transcription. J. Biol. Chem. 12 September 2002 (doi:10.1074/jbc.M208110200).
    • (2002) J. Biol. Chem.
    • Scheinfeld, M.H.1    Ghersi, E.2    Laky, K.3    Fowlkes, B.J.4    D'adamio, L.5
  • 116
    • 0037076398 scopus 로고    scopus 로고
    • The y-secretase-generated intracellular domain of β-amyloid precursor protein binds Numb and inhibits Notch signaling
    • Roncarati, R. et al. The y-secretase-generated intracellular domain of β-amyloid precursor protein binds Numb and inhibits Notch signaling. Proc. Natl Acad. Sci. USA 99, 7102-7107 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7102-7107
    • Roncarati, R.1
  • 117
    • 0037047434 scopus 로고    scopus 로고
    • The γ secretase-generated carboxyl-terminal domain of the amyloid precursor protein induces apoptosis via Tip60 in H4 cells
    • Kinoshita, A., Whelan, C. M., Berezovska, O. & Hyman, B. T. The γ secretase-generated carboxyl-terminal domain of the amyloid precursor protein induces apoptosis via Tip60 in H4 cells. J. Biol. Chem. 277, 28530-28536 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 28530-28536
    • Kinoshita, A.1    Whelan, C.M.2    Berezovska, O.3    Hyman, B.T.4
  • 118
    • 0034513572 scopus 로고    scopus 로고
    • Vitamin E supplementation prevents spatial learning deficits and dendritic alterations in aged apolipoprotein E-deficient mice
    • Veinbergs, I., Mallory, M., Sagara, Y. & Masliah, E. Vitamin E supplementation prevents spatial learning deficits and dendritic alterations in aged apolipoprotein E-deficient mice. Eur. J. Neurosci. 12, 4541-4546 (2000).
    • (2000) Eur. J. Neurosci , vol.12 , pp. 4541-4546
    • Veinbergs, I.1    Mallory, M.2    Sagara, Y.3    Masliah, E.4
  • 119
    • 0035223312 scopus 로고    scopus 로고
    • Apolipoprotein E and βA4-amyloid: Signals and effects
    • Ohm, T. G. et al. Apolipoprotein E and βA4-amyloid: signals and effects. Biochem. Soc. Symp. 67, 121-129 (2001).
    • (2001) Biochem. Soc. Symp , vol.67 , pp. 121-129
    • Ohm, T.G.1
  • 120
    • 0030300022 scopus 로고    scopus 로고
    • The 'nonamyloidogenic' p3 fragment (Amyloid β17-42) is a major constituent of Down's syndrome cerebellar preamyloid
    • Lalowski, M. et al. The 'nonamyloidogenic' p3 fragment (amyloid β17-42) is a major constituent of Down's syndrome cerebellar preamyloid. J. Biol. Chem. 271, 33623-33631 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 33623-33631
    • Lalowski, M.1
  • 121
    • 0031985080 scopus 로고    scopus 로고
    • N-terminal heterogeneity of parenchymal and cerebrovascular Aβ deposits
    • Tekirian, T. L. et al. N-terminal heterogeneity of parenchymal and cerebrovascular Aβ deposits. J. Neuropathol. Exp. Neurol. 57, 76-94 (1998).
    • (1998) J. Neuropathol. Exp. Neurol. , vol.57 , pp. 76-94
    • Tekirian, T.L.1
  • 122
    • 0033595706 scopus 로고    scopus 로고
    • β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE
    • Vassar, R. et al. β-Secretase cleavage of Alzheimer's amyloid precursor protein by the transmembrane aspartic protease BACE. Science 286, 735-741 (1999).
    • (1999) Science , vol.286 , pp. 735-741
    • Vassar, R.1
  • 123
    • 0037188528 scopus 로고    scopus 로고
    • Identification of a family of calcium sensors as protein ligands of inositol trisphosphate receptor Ca2+ release channels
    • 2+ release channels. Proc. Natl Acad. Sci. USA 99, 7711-7716 (2002).
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 7711-7716
    • Yang, J.1
  • 125
    • 0029658406 scopus 로고    scopus 로고
    • Elementary events of InsP3- induced Ca2+ liberation in Xenopus oocytes: Hot spots, puffs and blips
    • 2+ liberation in Xenopus oocytes: hot spots, puffs and blips. Cell Calcium 20, 105-121 (1996).
    • (1996) Cell Calcium , vol.20 , pp. 105-121
    • Parker, I.1    Choi, J.2    Yao, Y.3
  • 126
    • 0028913955 scopus 로고
    • Quantal puffs of intracellular Ca2+ evoked by inositol trisphosphate in Xenopus oocytes
    • 2+ evoked by inositol trisphosphate in Xenopus oocytes. J. Physiol. (Lond.) 482, 533-553 (1995).
    • (1995) J. Physiol. (Lond.) , vol.482 , pp. 533-553
    • Yao, Y.1    Choi, J.2    Parker, I.3
  • 128
    • 0034979346 scopus 로고    scopus 로고
    • Subcellular mechanisms of presenilin-mediated enhancement of calcium signaling
    • Leissring, M. A., LaFerla, F. M., Callamaras, N. & Parker, I. Subcellular mechanisms of presenilin-mediated enhancement of calcium signaling. Neurobiol. Dis. 8, 469-478 (2001).
    • (2001) Neurobiol. Dis. , vol.8 , pp. 469-478
    • Leissring, M.A.1    Laferla, F.M.2    Callamaras, N.3    Parker, I.4
  • 129
    • 0030891662 scopus 로고    scopus 로고
    • Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide
    • Guo, Q. et al. Alzheimer's PS-1 mutation perturbs calcium homeostasis and sensitizes PC12 cells to death induced by amyloid β-peptide. Neuroreport 8, 379-383 (1996).
    • (1996) Neuroreport , vol.8 , pp. 379-383
    • Guo, Q.1
  • 130
    • 0032972922 scopus 로고    scopus 로고
    • Altered calcium homeostasis and mitochondrial dysfunction in cortical synaptic compartments of presenilin-1 mutant mice
    • Begley, J. G., Duan, W., Chan, S., Duff, K. & Mattson, M. P. Altered calcium homeostasis and mitochondrial dysfunction in cortical synaptic compartments of presenilin-1 mutant mice. J. Neurochem. 72, 1030-1039 (1999).
    • (1999) J. Neurochem , vol.72 , pp. 1030-1039
    • Begley, J.G.1    Duan, W.2    Chan, S.3    Duff, K.4    Mattson, M.P.5
  • 131
    • 0033009194 scopus 로고    scopus 로고
    • Increased vulnerability of hippocampal neurons from presenilin-1 mutant knock-in mice to amyloid β-peptide toxicity: Central roles of superoxide production and caspase activation
    • Guo, Q. et al. Increased vulnerability of hippocampal neurons from presenilin-1 mutant knock-in mice to amyloid β-peptide toxicity: central roles of superoxide production and caspase activation. J. Neurochem. 72, 1019-1029 (1999).
    • (1999) J. Neurochem. , vol.72 , pp. 1019-1029
    • Guo, Q.1
  • 133
    • 0023198092 scopus 로고
    • Diminished mitogen-induced calcium uptake by lymphocytes from Alzheimer patients
    • Gibson, G. E., Nielsen, P., Sherman, K. A. & Blass, J. P. Diminished mitogen-induced calcium uptake by lymphocytes from Alzheimer patients. Biol. Psychiatry 22, 1079-1086 (1987).
    • (1987) Biol. Psychiatry , vol.22 , pp. 1079-1086
    • Gibson, G.E.1    Nielsen, P.2    Sherman, K.A.3    Blass, J.P.4
  • 134
    • 0029787370 scopus 로고    scopus 로고
    • Calcium responses in human fibroblasts: A diagnostic molecular profile for Alzheimer's disease
    • Hirashima, N. et al. Calcium responses in human fibroblasts: a diagnostic molecular profile for Alzheimer's disease. Neurobiol. Aging 17, 549-555 (1996).
    • (1996) Neurobiol. Aging , vol.17 , pp. 549-555
    • Hirashima, N.1
  • 135
    • 0023037796 scopus 로고
    • Cytosolic free calcium and cell spreading decrease in fibroblasts from aged and Alzheimer donors
    • Peterson, C., Ratan, R. R., Shelanski, M. L. & Goldman, J. E. Cytosolic free calcium and cell spreading decrease in fibroblasts from aged and Alzheimer donors. Proc. Natl Acad. Sci. USA 83, 7999-8001 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 7999-8001
    • Peterson, C.1    Ratan, R.R.2    Shelanski, M.L.3    Goldman, J.E.4
  • 136
    • 0022001659 scopus 로고
    • Altered calcium uptake in cultured skin fibroblasts from patients with Alzheimer's disease
    • Peterson, C., Gibson, G. E. & Blass, J. P. Altered calcium uptake in cultured skin fibroblasts from patients with Alzheimer's disease. N. Engl. J. Med. 312, 1063-1065 (1985).
    • (1985) N. Engl. J. Med. , vol.312 , pp. 1063-1065
    • Peterson, C.1    Gibson, G.E.2    Blass, J.P.3
  • 137
    • 0343050763 scopus 로고
    • Alterations in calcium content and biochemical processes in cultured skin fibroblasts from aged and Alzheimer donors
    • Peterson, C. & Goldman, J. E. Alterations in calcium content and biochemical processes in cultured skin fibroblasts from aged and Alzheimer donors. Proc. Natl Acad. Sci. USA 83, 2758-2762 (1986).
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , pp. 2758-2762
    • Peterson, C.1    Goldman, J.E.2
  • 138
    • 0024156569 scopus 로고
    • Altered response of fibroblasts from aged and Alzheimer donors to drugs that elevate cytosolic free calcium
    • Peterson, C., Ratan, R. R., Shelanski, M. L. & Goldman, J. E. Altered response of fibroblasts from aged and Alzheimer donors to drugs that elevate cytosolic free calcium. Neurobiol. Aging 9, 261-266 (1988).
    • (1988) Neurobiol. Aging , vol.9 , pp. 261-266
    • Peterson, C.1    Ratan, R.R.2    Shelanski, M.L.3    Goldman, J.E.4
  • 139
    • 0024949896 scopus 로고
    • Changes in calcium homeostasis during aging and Alzheimer's disease
    • Peterson, C., Ratan, R., Shelanski, M. & Goldman, J. Changes in calcium homeostasis during aging and Alzheimer's disease. Ann. NY Acad. Sci. 568, 262-270 (1989).
    • (1989) Ann. NY Acad. Sci. , vol.568 , pp. 262-270
    • Peterson, C.1    Ratan, R.2    Shelanski, M.3    Goldman, J.4
  • 140
    • 0028814411 scopus 로고
    • Cell-cycle-dependent abnormal calcium response in fibroblasts from patients with familial Alzheimer's disease
    • Tatebayashi, Y. et al. Cell-cycle-dependent abnormal calcium response in fibroblasts from patients with familial Alzheimer's disease. Dementia 6, 9-16 (1995).
    • (1995) Dementia , vol.6 , pp. 9-16
    • Tatebayashi, Y.1
  • 141
    • 0030917601 scopus 로고    scopus 로고
    • Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid β-peptide: Involvement of calcium and oxyradicals
    • Guo, Q. et al. Alzheimer's presenilin mutation sensitizes neural cells to apoptosis induced by trophic factor withdrawal and amyloid β-peptide: involvement of calcium and oxyradicals. J. Neurosci. 17, 4212-4222 (1997).
    • (1997) J. Neurosci. , vol.17 , pp. 4212-4222
    • Guo, Q.1
  • 142
    • 0345055313 scopus 로고    scopus 로고
    • Increased sensitivity to mitochondrial toxin- induced apoptosis in neural cells expressing mutant presenilin-1 is linked to perturbed calcium homeostasis and enhanced oxyradical production
    • Keller, J. N., Guo, Q., Holtsberg, F. W., Bruce-Keller, A. J. & Mattson, M. P. Increased sensitivity to mitochondrial toxin- induced apoptosis in neural cells expressing mutant presenilin-1 is linked to perturbed calcium homeostasis and enhanced oxyradical production. J. Neurosci. 18, 4439-4450 (1998).
    • (1998) J. Neurosci. , vol.18 , pp. 4439-4450
    • Keller, J.N.1    Guo, Q.2    Holtsberg, F.W.3    Bruce-Keller, A.J.4    Mattson, M.P.5
  • 143
    • 0032100541 scopus 로고    scopus 로고
    • Presenilin-1 mutation alters NGF-induced neurite outgrowth, calcium homeostasis, and transcription factor (AP-1) activation in PC12 cells
    • Furukawa, K., Guo, Q., Schellenberg, G. D. & Mattson, M. P. Presenilin-1 mutation alters NGF-induced neurite outgrowth, calcium homeostasis, and transcription factor (AP-1) activation in PC12 cells. J. Neurosci. Res. 52, 618-624 (1998).
    • (1998) J. Neurosci. Res , vol.52 , pp. 618-624
    • Furukawa, K.1    Guo, Q.2    Schellenberg, G.D.3    Mattson, M.P.4
  • 144
    • 0035477406 scopus 로고    scopus 로고
    • Caspase cleavage of exon 9 deleted presenilin-1 is an early event in apoptosis induced by calcium ionophore A 23187 in SH-SY5Y neuroblastoma cells
    • Popescu, B. O. et al. Caspase cleavage of exon 9 deleted presenilin-1 is an early event in apoptosis induced by calcium ionophore A 23187 in SH-SY5Y neuroblastoma cells. J. Neurosci. Res. 66, 122-134 (2001).
    • (2001) J. Neurosci. Res , vol.66 , pp. 122-134
    • Popescu, B.O.1
  • 145
    • 0035853828 scopus 로고    scopus 로고
    • Mutant presenilins disturb neuronal calcium homeostasis in the brain of transgenic mice, decreasing the threshold for excitotoxicity and facilitating long-term potentiation
    • Schneider, I. et al. Mutant presenilins disturb neuronal calcium homeostasis in the brain of transgenic mice, decreasing the threshold for excitotoxicity and facilitating long-term potentiation. J. Biol. Chem. 276, 11539-11544 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 11539-11544
    • Schneider, I.1


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