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Volumn 29, Issue 46, 2009, Pages 14451-14462

Amyloid precursor protein mediates a tyrosine kinase-dependent activation response in endothelial cells

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID PRECURSOR PROTEIN; BETA SECRETASE; CYCLOOXYGENASE 2; PHOSPHOPROTEIN; PROTEIN ANTIBODY; PROTEIN TYROSINE KINASE; VASCULAR CELL ADHESION MOLECULE 1;

EID: 70949083202     PISSN: 02706474     EISSN: 15292401     Source Type: Journal    
DOI: 10.1523/JNEUROSCI.3107-09.2009     Document Type: Article
Times cited : (31)

References (47)
  • 1
    • 0742306942 scopus 로고    scopus 로고
    • Only cerebral capillary amyloid angiopathy correlates with Alzheimer pathology - A pilot study
    • DOI 10.1007/s00401-003-0796-9
    • Attems J, Jellinger KA (2004) Only cerebral capillary amyloid angiopathy correlates with Alzheimer pathology: a pilot study. Acta Neuropathol 107:83-90. (Pubitemid 38159295)
    • (2004) Acta Neuropathologica , vol.107 , Issue.2 , pp. 83-90
    • Attems, J.1    Jellinger, K.A.2
  • 2
    • 1842739274 scopus 로고    scopus 로고
    • Amyloid beta peptide 1-42 highly correlates with capillary cerebral amyloid angiopathy and Alzheimer disease pathology
    • DOI 10.1007/s00401-004-0822-6
    • Attems J, Lintner F, Jellinger KA (2004) Amyloid beta peptide 1-42 highly correlates with capillary cerebral amyloid angiopathy and Alzheimer disease pathology. Acta Neuropathol 107:283-291. (Pubitemid 38477354)
    • (2004) Acta Neuropathologica , vol.107 , Issue.4 , pp. 283-291
    • Attems, J.1    Lintner, F.2    Jellinger, K.A.3
  • 3
    • 77956894555 scopus 로고    scopus 로고
    • Amyloid precursor protein mediates monocyte adhesion in AD tissue and apoE(-)/(-) mice
    • Advance online publication. Retrieved December 4, 2008. doi: 10.1016/j.neurobiolaging.2008.10.013
    • Austin SA, Combs CK (2008) Amyloid precursor protein mediates monocyte adhesion in AD tissue and apoE(-)/(-) mice. Neurobiol Aging. Advance online publication. Retrieved December 4, 2008. doi: 10.1016/j.neurobiolaging.2008.10. 013.
    • (2008) Neurobiol Aging
    • Austin, S.A.1    Combs, C.K.2
  • 5
    • 0028181159 scopus 로고
    • Glial beta-amyloid precursor protein: Expression in the dentate gyrus after entorhinal cortex lesion
    • Banati RB, Gehrmann J, Kreutzberg GW (1994) Glial beta-amyloid precursor protein: expression in the dentate gyrus after entorhinal cortex lesion. Neuroreport 5:1359-1361. (Pubitemid 24219232)
    • (1994) NeuroReport , vol.5 , Issue.11 , pp. 1359-1361
    • Banati, R.B.1    Gehrmann, J.2    Kreutzberg, G.W.3
  • 6
    • 0030030005 scopus 로고    scopus 로고
    • Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I
    • Beher D, Hesse L, Masters CL, Multhaup G (1996) Regulation of amyloid protein precursor (APP) binding to collagen and mapping of the binding sites on APP and collagen type I. J Biol Chem 271:1613-1620.
    • (1996) J Biol Chem , vol.271 , pp. 1613-1620
    • Beher, D.1    Hesse, L.2    Masters, C.L.3    Multhaup, G.4
  • 7
    • 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 JP, Ooi J, Levy E, Margolis B (1996) 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) Mol Cell Biol , vol.16 , pp. 6229-6241
    • Borg, J.P.1    Ooi, J.2    Levy, E.3    Margolis, B.4
  • 8
    • 0033527637 scopus 로고    scopus 로고
    • Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells
    • Chung H, Brazil MI, Soe TT, Maxfield FR (1999) Uptake, degradation, and release of fibrillar and soluble forms of Alzheimer's amyloid beta-peptide by microglial cells. J Biol Chem 274:32301-32308. (Pubitemid 129503830)
    • (1999) Journal of Biological Chemistry , vol.274 , Issue.45 , pp. 32301-32308
    • Chung, H.1    Brazil, M.I.2    Soe, T.T.3    Maxfield, F.R.4
  • 11
    • 0037701180 scopus 로고    scopus 로고
    • Beta-amyloid peptide-induced blood-brain barrier disruption facilitates T-cell entry into the rat brain
    • DOI 10.1078/0065-1281-00696
    • Farkas IG, Czigner A, Farkas E, Dobó E, Soó s K, Penke B, Endrész V, Mihá ly A (2003) Beta-amyloid peptide-induced blood-brain barrier disruption facilitates T-cell entry into the rat brain. Acta Histochem 105:115-125. (Pubitemid 36734149)
    • (2003) Acta Histochemica , vol.105 , Issue.2 , pp. 115-125
    • Farkas, I.G.1    Czigner, A.2    Farkas, E.3    Dobo, E.4    Soos, K.5    Penke, B.6    Endresz, V.7    Mihaly, A.8
  • 13
    • 0026452028 scopus 로고
    • Expression of amyloid precursor protein mRNAs in endothelial, neuronal and glial cells: Modulation by interleukin-1
    • Forloni G, Demicheli F, Giorgi S, Bendotti C, Angeretti N (1992) Expression of amyloid precursor protein mRNAs in endothelial, neuronal and glial cells: modulation by interleukin-1. Brain Res Mol Brain Res 16:128-134.
    • (1992) Brain Res Mol Brain Res , vol.16 , pp. 128-134
    • Forloni, G.1    Demicheli, F.2    Giorgi, S.3    Bendotti, C.4    Angeretti, N.5
  • 15
    • 37349003744 scopus 로고    scopus 로고
    • Soluble aggregates of the amyloidbeta protein activate endothelial monolayers for adhesion and subsequent transmigration of monocyte cells
    • Gonzalez-Velasquez FJ, Moss MA (2008) Soluble aggregates of the amyloidbeta protein activate endothelial monolayers for adhesion and subsequent transmigration of monocyte cells. J Neurochem 104:500-513.
    • (2008) J Neurochem , vol.104 , pp. 500-513
    • Gonzalez-Velasquez, F.J.1    Moss, M.A.2
  • 16
    • 67649366042 scopus 로고    scopus 로고
    • Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers
    • Gralle M, Botelho MG, Wouters FS (2009) Neuroprotective secreted amyloid precursor protein acts by disrupting amyloid precursor protein dimers. J Biol Chem 284:15016-15025.
    • (2009) J Biol Chem , vol.284 , pp. 15016-15025
    • Gralle, M.1    Botelho, M.G.2    Wouters, F.S.3
  • 18
    • 0033066680 scopus 로고    scopus 로고
    • The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids
    • Howell BW, Lanier LM, Frank R, Gertler FB, Cooper JA (1999) The disabled 1 phosphotyrosine-binding domain binds to the internalization signals of transmembrane glycoproteins and to phospholipids. Mol Cell Biol 19:5179-5188. (Pubitemid 29289556)
    • (1999) Molecular and Cellular Biology , vol.19 , Issue.7 , pp. 5179-5188
    • Howell, B.W.1    Lanier, L.M.2    Frank, R.3    Gertler, F.B.4    Cooper, J.A.5
  • 20
    • 0032534611 scopus 로고    scopus 로고
    • Endothelial cell dysfunction in response to intracellular overexpression of amyloid precursor protein
    • DOI 10.1002/(SICI)1097-4547(19981215)54:6<828::AID-JNR11>3.0.CO;2-M
    • Jahroudi N, Kitney J, Greenberger JS, Bowser R (1998) Endothelial cell dysfunction in response to intracellular overexpression of amyloid precursor protein. J Neurosci Res 54:828-839. (Pubitemid 28544384)
    • (1998) Journal of Neuroscience Research , vol.54 , Issue.6 , pp. 828-839
    • Jahroudi, N.1    Kitney, J.2    Greenberger, J.S.3    Bowser, R.4
  • 21
    • 0028171524 scopus 로고
    • Increased beta-amyloid release and levels of amyloid precursor protein (APP) in fibroblast cell lines from family members of the Swedish Alzheimer's disease APP670/671 mutation
    • DOI 10.1016/0014-5793(94)01137-0
    • Johnston JA, Cowburn RF, Norgren S, Wiehager B, Venizelos N, Winblad B, Vigo-Pelfrey C, Schenk D, Lannfelt L, O'Neill C (1994) Increased beta-amyloid release and levels of amyloid precursor protein (APP) in fibroblast cell lines from family members with the Swedish Alzheimer's disease APP670/671 mutation. FEBS Lett 354:274-278. (Pubitemid 2164744)
    • (1994) FEBS Letters , vol.354 , Issue.3 , pp. 274-278
    • Johnston, J.A.1    Cowburn, R.F.2    Norgren, S.3    Wiehager, B.4    Venizelos, N.5    Winblad, B.6    Vigo-Pelfrey, C.7    Schenk, D.8    Lannfelt, L.9    O'Neill, C.10
  • 22
    • 0037468159 scopus 로고    scopus 로고
    • c-Src inhibitor PP1 is non-competitive against ATP
    • DOI 10.1016/S0014-5793(03)00069-3
    • Karni R, Mizrachi S, Reiss-Sklan E, Gazit A, Livnah O, Levitzki A (2003) The pp60c-Src inhibitor PP1 is non-competitive against ATP. FEBS Lett 537:47-52. (Pubitemid 36246674)
    • (2003) FEBS Letters , vol.537 , Issue.1-3 , pp. 47-52
    • Karni, R.1    Mizrachi, S.2    Reiss-Sklan, E.3    Gazit, A.4    Livnah, O.5    Levitzki, A.6
  • 25
    • 0345602771 scopus 로고    scopus 로고
    • Amyloid beta Protein Toxicity Mediated by the Formation of Amyloid-beta Protein Precursor Complexes
    • DOI 10.1002/ana.10761
    • Lu DC, Shaked GM, Masliah E, Bredesen DE, Koo EH (2003) Amyloid beta protein toxicity mediated by the formation of amyloid-beta protein precursor complexes. Ann Neurol 54:781-789. (Pubitemid 37504953)
    • (2003) Annals of Neurology , vol.54 , Issue.6 , pp. 781-789
    • Lu, D.C.1    Shaked, G.M.2    Masliah, E.3    Bredesen, D.E.4    Koo, E.H.5
  • 26
    • 0023369786 scopus 로고
    • Isolation of rat aortic endothelial cells by primary explant techniques and their phenotypic modulation by defined substrata
    • McGuire PG, Orkin RW (1987) Isolation of rat aortic endothelial cells by primary explant techniques and their phenotypic modulation by defined substrata. Lab Invest 57:94-105.
    • (1987) Lab Invest , vol.57 , pp. 94-105
    • McGuire, P.G.1    Orkin, R.W.2
  • 27
    • 33749064224 scopus 로고    scopus 로고
    • Concanavalin A, but not glycated albumin, increases subendothelial deposition of von Willebrand factor in vitro
    • Nizheradze K (2006) Concanavalin A, but not glycated albumin, increases subendothelial deposition of von Willebrand factor in vitro. Endothelium 13:245-248.
    • (2006) Endothelium , vol.13 , pp. 245-248
    • Nizheradze, K.1
  • 28
    • 0034940552 scopus 로고    scopus 로고
    • Physiological levels of beta-amyloid induce cerebral vessel dysfunction and reduce endothelial nitric oxide production
    • DOI 10.1179/016164101101198758
    • Price JM, Chi X, Hellermann G, Sutton ET (2001) Physiological levels of beta-amyloid induce cerebral vessel dysfunction and reduce endothelial nitric oxide production. Neurol Res 23:506-512. (Pubitemid 32642784)
    • (2001) Neurological Research , vol.23 , Issue.5 , pp. 506-512
    • Price, J.M.1    Chi, X.2    Hellermann, G.3    Sutton, E.T.4
  • 29
    • 0027976942 scopus 로고
    • Atherosclerosis in mice lacking apo E. Evaluation of lesional development and progression
    • Reddick RL, Zhang SH, Maeda N (1994) Atherosclerosis in mice lacking apo E. Evaluation of lesional development and progression. Arterioscler Thromb 14:141-147.
    • (1994) Arterioscler Thromb , vol.14 , pp. 141-147
    • Reddick, R.L.1    Zhang, S.H.2    Maeda, N.3
  • 31
    • 0036959694 scopus 로고    scopus 로고
    • Signal transduction through tyrosine-phosphorylated carboxy-terminal fragments of APP via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain
    • Russo C, Dolcini V, Salis S, Venezia V, Violani E, Carlo P, Zambrano N, Russo T, Schettini G (2002) Signal transduction through tyrosine-phosphorylated carboxy-terminal fragments of APP via an enhanced interaction with Shc/Grb2 adaptor proteins in reactive astrocytes of Alzheimer's disease brain. Ann N Y Acad Sci 973:323-333. (Pubitemid 36125030)
    • (2002) Annals of the New York Academy of Sciences , vol.973 , pp. 323-333
    • Russo, C.1    Dolcini, V.2    Salis, S.3    Venezia, V.4    Violani, E.5    Carlo, P.6    Zambrano, N.7    Russo, T.8    Schettini, G.9
  • 32
    • 0036462590 scopus 로고    scopus 로고
    • 2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP)
    • DOI 10.1074/jbc.M108357200
    • Scheinfeld MH, Roncarati R, Vito P, Lopez PA, Abdallah M, D'Adamio L (2002) Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid precursor protein (APP). J Biol Chem 277:3767-3775. (Pubitemid 34953251)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.5 , pp. 3767-3775
    • Scheinfeld, M.H.1    Roncarati, R.2    Vito, P.3    Lopez, P.A.4    Abdallah, M.5    D'Adamio, L.6
  • 34
    • 0025151436 scopus 로고
    • The amyloid beta-protein precursor is localized in smooth muscle cells of leptomeningeal vessels
    • DOI 10.1016/0006-8993(90)90665-X
    • Shoji M, Hirai S, Harigaya Y, Kawarabayashi T, Yamaguchi H (1990) The amyloid beta-protein precursor is localized in smooth muscle cells of leptomeningeal vessels. Brain Res 530:113-116. (Pubitemid 20348585)
    • (1990) Brain Research , vol.530 , Issue.1 , pp. 113-116
    • Shoji, M.1    Hirai, S.2    Harigaya, Y.3    Kawarabayashi, T.4    Yamaguchi, H.5
  • 36
    • 1842689293 scopus 로고    scopus 로고
    • Amyloid precursor protein mediates proinflammatory activation of monocytic lineage cells
    • Sondag CM, Combs CK (2004) Amyloid precursor protein mediates proinflammatory activation of monocytic lineage cells. J Biol Chem 279:14456-14463.
    • (2004) J Biol Chem , vol.279 , pp. 14456-14463
    • Sondag, C.M.1    Combs, C.K.2
  • 37
    • 0017088029 scopus 로고
    • Lymphocyte homing into lymph nodes: In vitro demonstration of the selective affinity of recirculating lymphocytes for high-endothelial venules
    • Stamper HB Jr, Woodruff JJ (1976) Lymphocyte homing into lymph nodes: in vitro demonstration of the selective affinity of recirculating lymphocytes for high-endothelial venules. J Exp Med 144:828-833.
    • (1976) J Exp Med , vol.144 , pp. 828-833
    • Stamper Jr., H.B.1    Woodruff, J.J.2
  • 38
    • 0029670094 scopus 로고    scopus 로고
    • beta-Amyloid-mediated vasoactivity and vascular endothelial damage
    • DOI 10.1038/380168a0
    • Thomas T, Thomas G, McLendon C, Sutton T, Mullan M (1996) beta-Amyloid-mediated vasoactivity and vascular endothelial damage. Nature 380:168-171. (Pubitemid 26085884)
    • (1996) Nature , vol.380 , Issue.6570 , pp. 168-171
    • Thomas, T.1    Thomas, G.2    McLendon, C.3    Sutton, T.4    Mullan, M.5
  • 40
    • 9644254334 scopus 로고    scopus 로고
    • Amyloid precursor protein expression in circulating monocytes and brain macrophages from patients with HIV-associated cognitive impairment
    • DOI 10.1016/j.jneuroim.2004.08.035, PII S016557280400339X
    • Vehmas A, Lieu J, Pardo CA, McArthur JC, Gartner S (2004) Amyloid precursor protein expression in circulating monocytes and brain macrophages from patients with HIV-associated cognitive impairment. J Neuroimmunol 157:99-110. (Pubitemid 39576643)
    • (2004) Journal of Neuroimmunology , vol.157 , Issue.1-2 SPEC. ISS , pp. 99-110
    • Vehmas, A.1    Lieu, J.2    Pardo, C.A.3    McArthur, J.C.4    Gartner, S.5
  • 41
    • 4544302611 scopus 로고    scopus 로고
    • Apoptotic cell death influences the signaling activity of the amyloid precursor protein through ShcA and Grb2 adaptor proteins in neuroblastoma SH-SY5Y cells
    • DOI 10.1111/j.1471-4159.2004.02618.x
    • Venezia V, Russo C, Repetto E, Salis S, Dolcini V, Genova F, Nizzari M, Mueller U, Schettini G (2004) Apoptotic cell death influences the signaling activity of the amyloid precursor protein through ShcA and Grb2 adaptor proteins in neuroblastoma SH-SY5Y cells. J Neurochem 90:1359-1370. (Pubitemid 39223640)
    • (2004) Journal of Neurochemistry , vol.90 , Issue.6 , pp. 1359-1370
    • Venezia, V.1    Russo, C.2    Repetto, E.3    Salis, S.4    Dolcini, V.5    Genova, F.6    Nizzari, M.7    Mueller, U.8    Schettini, G.9
  • 42
    • 0034720732 scopus 로고    scopus 로고
    • Fibrillar amyloid beta-protein binds protease nexin-2/amyloid beta-protein precursor: Stimulation of its inhibition of coagulation factor XIa
    • Wagner MR, Keane DM, Melchor JP, Auspaker KR, Van Nostrand WE (2000) Fibrillar amyloid beta-protein binds protease nexin-2/amyloid beta-protein precursor: stimulation of its inhibition of coagulation factor XIa. Biochemistry 39:7420-7427.
    • (2000) Biochemistry , vol.39 , pp. 7420-7427
    • Wagner, M.R.1    Keane, D.M.2    Melchor, J.P.3    Auspaker, K.R.4    Van Nostrand, W.E.5
  • 43
    • 4143105782 scopus 로고    scopus 로고
    • The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain
    • DOI 10.1016/j.molcel.2004.06.037, PII S109727650400379X
    • Wang Y, Ha Y (2004) The X-ray structure of an antiparallel dimer of the human amyloid precursor protein E2 domain. Mol Cell 15:343-353. (Pubitemid 39092751)
    • (2004) Molecular Cell , vol.15 , Issue.3 , pp. 343-353
    • Wang, Y.1    Ha, Y.2
  • 44
    • 0028863251 scopus 로고
    • Affinity purification of proteoglycans that bind to the amyloid protein precursor of Alzheimer's disease
    • Williamson TG, Nurcombe V, Beyreuther K, Masters CL, Small DH (1995) Affinity purification of proteoglycans that bind to the amyloid protein precursor of Alzheimer's disease. J Neurochem 65:2201-2208.
    • (1995) J Neurochem , vol.65 , pp. 2201-2208
    • Williamson, T.G.1    Nurcombe, V.2    Beyreuther, K.3    Masters, C.L.4    Small, D.H.5
  • 46
    • 0026753096 scopus 로고
    • Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer's disease. An immunoelectron microscopic study
    • Yamaguchi H, Yamazaki T, Lemere CA, Frosch MP, Selkoe DJ (1992) Beta amyloid is focally deposited within the outer basement membrane in the amyloid angiopathy of Alzheimer's disease. An immunoelectron microscopic study. Am J Pathol 141:249-259.
    • (1992) Am J Pathol , vol.141 , pp. 249-259
    • Yamaguchi, H.1    Yamazaki, T.2    Lemere, C.A.3    Frosch, M.P.4    Selkoe, D.J.5
  • 47
    • 0033152210 scopus 로고    scopus 로고
    • Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors
    • Zhu X, Kim JL, Newcomb JR, Rose PE, Stover DR, Toledo LM, Zhao H, Morgenstern KA (1999) Structural analysis of the lymphocyte-specific kinase Lck in complex with non-selective and Src family selective kinase inhibitors. Structure 7:651-661.
    • (1999) Structure , vol.7 , pp. 651-661
    • Zhu, X.1    Kim, J.L.2    Newcomb, J.R.3    Rose, P.E.4    Stover, D.R.5    Toledo, L.M.6    Zhao, H.7    Morgenstern, K.A.8


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