메뉴 건너뛰기




Volumn 15, Issue 1, 2008, Pages 5-19

Potent anti-angiogenic motifs within the Alzheimer β-amyloid peptide

Author keywords

Alzheimer; Amyloid; Angiogenesis; Cancer

Indexed keywords

AMYLOID BETA PROTEIN; MATRIGEL;

EID: 39049128041     PISSN: 13506129     EISSN: 17442818     Source Type: Journal    
DOI: 10.1080/13506120701814723     Document Type: Article
Times cited : (17)

References (59)
  • 1
    • 0023037536 scopus 로고
    • Isolation and partial characterization of neurofibrillary tangles and amyloid plaque core in Alzheimer's disease: Immunohistological studies
    • Gorevic PD, Goni F, Pons-Estel B, Alvarez F, Peress NS, Frangione B. Isolation and partial characterization of neurofibrillary tangles and amyloid plaque core in Alzheimer's disease: immunohistological studies. J Neuropathol Exp Neurol 1986;45:647-664.
    • (1986) J Neuropathol Exp Neurol , vol.45 , pp. 647-664
    • Gorevic, P.D.1    Goni, F.2    Pons-Estel, B.3    Alvarez, F.4    Peress, N.S.5    Frangione, B.6
  • 2
    • 0022654027 scopus 로고
    • Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease
    • Selkoe DJ, Abraham CR, Podlisny MB, Duffy LK. Isolation of low-molecular-weight proteins from amyloid plaque fibers in Alzheimer's disease. J Neurochem 1986;46:1820-1834.
    • (1986) J Neurochem , vol.46 , pp. 1820-1834
    • Selkoe, D.J.1    Abraham, C.R.2    Podlisny, M.B.3    Duffy, L.K.4
  • 3
    • 0023275358 scopus 로고
    • Amyloid angiopathy of Alzheimer's disease: Amino acid composition and partial sequence of a 4,200-dalton peptide isolated from cortical microvessels
    • Pardridge WM, Vinters HV, Yang J, Eisenberg J, Choi TB, Tourtellotte WW, Huebner V, Shively JE. Amyloid angiopathy of Alzheimer's disease: amino acid composition and partial sequence of a 4,200-dalton peptide isolated from cortical microvessels. J Neurochem 1987;49:1394-1401.
    • (1987) J Neurochem , vol.49 , pp. 1394-1401
    • Pardridge, W.M.1    Vinters, H.V.2    Yang, J.3    Eisenberg, J.4    Choi, T.B.5    Tourtellotte, W.W.6    Huebner, V.7    Shively, J.E.8
  • 4
    • 14844327519 scopus 로고    scopus 로고
    • Prevalence and pathogenic role of cerebrovascular lesions in Alzheimer disease
    • Jellinger KA, Attems J. Prevalence and pathogenic role of cerebrovascular lesions in Alzheimer disease. J Neurol Sci 2005;229-230:37-41.
    • (2005) J Neurol Sci
    • Jellinger, K.A.1    Attems, J.2
  • 6
    • 13844298168 scopus 로고    scopus 로고
    • Pattern of cerebral hypoperfusion in Alzheimer disease and mild cognitive impairment measured with arterial spin-labeling MR imaging: Initial experience
    • Johnson NA, Jahng GH, Weiner MW, Miller BL, Chui HC, Jagust WJ, Gorno-Tempini ML, Schuff N. Pattern of cerebral hypoperfusion in Alzheimer disease and mild cognitive impairment measured with arterial spin-labeling MR imaging: initial experience. Radiology 2005;234:851-859.
    • (2005) Radiology , vol.234 , pp. 851-859
    • Johnson, N.A.1    Jahng, G.H.2    Weiner, M.W.3    Miller, B.L.4    Chui, H.C.5    Jagust, W.J.6    Gorno-Tempini, M.L.7    Schuff, N.8
  • 7
    • 2542455536 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy plays a direct role in the pathogenesis of Alzheimer's disease. Pro-CAA position statement
    • Nicoll JA, Yamada M, Frackowiak J, Mazur-Kolecka B, Weller RO. Cerebral amyloid angiopathy plays a direct role in the pathogenesis of Alzheimer's disease. Pro-CAA position statement. Neurobiol Aging 2004;25:589-597.
    • (2004) Neurobiol Aging , vol.25 , pp. 589-597
    • Nicoll, J.A.1    Yamada, M.2    Frackowiak, J.3    Mazur-Kolecka, B.4    Weller, R.O.5
  • 8
    • 1642472817 scopus 로고    scopus 로고
    • Nilvadipine antagonizes both Abeta vasoactivity in isolated arteries, and the reduced cerebral blood flow in APPsw transgenic mice
    • Paris D, Quadros A, Humphrey J, Patel N, Crescentini R, Crawford F, Mullan M. Nilvadipine antagonizes both Abeta vasoactivity in isolated arteries, and the reduced cerebral blood flow in APPsw transgenic mice. Brain Res 2004;999:53-61.
    • (2004) Brain Res , vol.999 , pp. 53-61
    • Paris, D.1    Quadros, A.2    Humphrey, J.3    Patel, N.4    Crescentini, R.5    Crawford, F.6    Mullan, M.7
  • 9
    • 0141457931 scopus 로고    scopus 로고
    • Age-dependent cerebrovascular abnormalities and blood flow disturbances in APP23 mice modeling Alzheimer's disease
    • Beckmann N, Schuler A, Mueggler T, Meyer EP, Wiederhold KH, Staufenbiel M, Krucker T. Age-dependent cerebrovascular abnormalities and blood flow disturbances in APP23 mice modeling Alzheimer's disease. J Neurosci 2003;23:8453-8459.
    • (2003) J Neurosci , vol.23 , pp. 8453-8459
    • Beckmann, N.1    Schuler, A.2    Mueggler, T.3    Meyer, E.P.4    Wiederhold, K.H.5    Staufenbiel, M.6    Krucker, T.7
  • 10
    • 0035047718 scopus 로고    scopus 로고
    • Cerebral microvascular pathology in aging and Alzheimer's disease
    • Farkas E, Luiten PG. Cerebral microvascular pathology in aging and Alzheimer's disease. Prog Neurobiol 2001;64:575-611.
    • (2001) Prog Neurobiol , vol.64 , pp. 575-611
    • Farkas, E.1    Luiten, P.G.2
  • 15
    • 10044245948 scopus 로고    scopus 로고
    • Physiological levels of amyloid peptides stimulate the angiogenic response through FGF-2
    • Cantara S, Donnini S, Morbidelli L, Giachetti A, Schulz R, Memo M, Ziche M. Physiological levels of amyloid peptides stimulate the angiogenic response through FGF-2. FASEB J 2004;18:1943-1945.
    • (2004) FASEB J , vol.18 , pp. 1943-1945
    • Cantara, S.1    Donnini, S.2    Morbidelli, L.3    Giachetti, A.4    Schulz, R.5    Memo, M.6    Ziche, M.7
  • 16
    • 4444322354 scopus 로고    scopus 로고
    • Do antiangiogenic protein fragments have amyloid properties?
    • Gebbink MF, Voest EE, Reijerkerk A. Do antiangiogenic protein fragments have amyloid properties? Blood 2004;104:1601-1605.
    • (2004) Blood , vol.104 , pp. 1601-1605
    • Gebbink, M.F.1    Voest, E.E.2    Reijerkerk, A.3
  • 17
    • 0034718157 scopus 로고    scopus 로고
    • Alzheimer's amyloid fibrils: Structure and assembly
    • Serpell LC. Alzheimer's amyloid fibrils: structure and assembly. Biochim Biophys Acta 2000;1502:16-30.
    • (2000) Biochim Biophys Acta , vol.1502 , pp. 16-30
    • Serpell, L.C.1
  • 20
    • 12844268491 scopus 로고    scopus 로고
    • Endostatin dramatically inhibits endothelial cell migration, vascular morphogenesis, and perivascular cell recruitment in vivo
    • Skovseth DK, Veuger MJ, Sorensen DR, De Angelis PM, Haraldsen G. Endostatin dramatically inhibits endothelial cell migration, vascular morphogenesis, and perivascular cell recruitment in vivo. Blood 2005;105:1044-1051.
    • (2005) Blood , vol.105 , pp. 1044-1051
    • Skovseth, D.K.1    Veuger, M.J.2    Sorensen, D.R.3    De Angelis, P.M.4    Haraldsen, G.5
  • 22
    • 0024584913 scopus 로고
    • Molecular modeling of protein glycosaminoglycan interactions
    • Cardin AD, Weintaub HJR. Molecular modeling of protein glycosaminoglycan interactions. Arteriosclerosis 1989;9:21-32.
    • (1989) Arteriosclerosis , vol.9 , pp. 21-32
    • Cardin, A.D.1    Weintaub, H.J.R.2
  • 23
    • 0029047722 scopus 로고
    • Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the beta-amyloid protein of Alzheimer's disease
    • Snow AD, Kinsella MG, Parks E, Sekiguchi RT, Miller JD, Kimata K, Wight TN. Differential binding of vascular cell-derived proteoglycans (perlecan, biglycan, decorin, and versican) to the beta-amyloid protein of Alzheimer's disease. Arch Biochem Biophys 1995;320:84-95.
    • (1995) Arch Biochem Biophys , vol.320 , pp. 84-95
    • Snow, A.D.1    Kinsella, M.G.2    Parks, E.3    Sekiguchi, R.T.4    Miller, J.D.5    Kimata, K.6    Wight, T.N.7
  • 24
    • 0033755865 scopus 로고    scopus 로고
    • Effect of amino-acid substitutions on Alzheimer's amyloid-beta peptide-glycosaminoglycan interactions
    • McLaurin J, Fraser PE. Effect of amino-acid substitutions on Alzheimer's amyloid-beta peptide-glycosaminoglycan interactions. Eur J Biochem 2000;267:6353-6361.
    • (2000) Eur J Biochem , vol.267 , pp. 6353-6361
    • McLaurin, J.1    Fraser, P.E.2
  • 25
    • 3042663370 scopus 로고    scopus 로고
    • Determination of dissociation constants for a heparin-binding domain of amyloid precursor protein and heparins or heparan sulfate by affinity capillary electrophoresis
    • McKeon J, Holland LA. Determination of dissociation constants for a heparin-binding domain of amyloid precursor protein and heparins or heparan sulfate by affinity capillary electrophoresis. Electrophoresis 2004;25:1243-1248.
    • (2004) Electrophoresis , vol.25 , pp. 1243-1248
    • McKeon, J.1    Holland, L.A.2
  • 26
    • 14744281839 scopus 로고    scopus 로고
    • Role of cell surface heparan sulfate proteoglycans in endothelial cell migration and mechanotransduction
    • Moon JJ, Matsumoto M, Patel S, Lee L, Guan JL, Li S. Role of cell surface heparan sulfate proteoglycans in endothelial cell migration and mechanotransduction. J Cell Physiol 2005;203:166-176.
    • (2005) J Cell Physiol , vol.203 , pp. 166-176
    • Moon, J.J.1    Matsumoto, M.2    Patel, S.3    Lee, L.4    Guan, J.L.5    Li, S.6
  • 27
    • 16244380777 scopus 로고    scopus 로고
    • Syndecans: New kids on the signaling block
    • Tkachenko E, Rhodes JM, Simons M. Syndecans: new kids on the signaling block. Circ Res 2005;96:488-500.
    • (2005) Circ Res , vol.96 , pp. 488-500
    • Tkachenko, E.1    Rhodes, J.M.2    Simons, M.3
  • 29
    • 0028278477 scopus 로고
    • Binding of heparan sulfate glycosaminoglycan to beta-amyloid peptide: Inhibition by potentially therapeutic polysulfated compounds
    • Leveugle B, Scanameo A, Ding W, Fillit H. Binding of heparan sulfate glycosaminoglycan to beta-amyloid peptide: inhibition by potentially therapeutic polysulfated compounds. Neuroreport 1994;5:1389-1392.
    • (1994) Neuroreport , vol.5 , pp. 1389-1392
    • Leveugle, B.1    Scanameo, A.2    Ding, W.3    Fillit, H.4
  • 30
    • 0036675368 scopus 로고    scopus 로고
    • Novel glycosaminoglycan precursors as anti-amyloid agents part II
    • Kisilevsky R, Szarek WA. Novel glycosaminoglycan precursors as anti-amyloid agents part II. J Mol Neurosci 2002;19:45-50.
    • (2002) J Mol Neurosci , vol.19 , pp. 45-50
    • Kisilevsky, R.1    Szarek, W.A.2
  • 34
    • 33644851439 scopus 로고    scopus 로고
    • The solvent protection of Alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy
    • Olofsson A, Sauer-Eriksson AE, Ohman A. The solvent protection of Alzheimer amyloid-beta-(1-42) fibrils as determined by solution NMR spectroscopy. J Biol Chem 2006;281:477-483.
    • (2006) J Biol Chem , vol.281 , pp. 477-483
    • Olofsson, A.1    Sauer-Eriksson, A.E.2    Ohman, A.3
  • 35
    • 32644475566 scopus 로고    scopus 로고
    • Alzheimer's amyloid beta-peptide (1-42) induces cell death in human neuroblastoma via bax/bcl-2 ratio increase: An intriguing role for methionine 35
    • Clementi ME, Pezzotti M, Orsini F, Sampaolese B, Mezzogori D, Grassi C, Giardina B, Misiti F. Alzheimer's amyloid beta-peptide (1-42) induces cell death in human neuroblastoma via bax/bcl-2 ratio increase: an intriguing role for methionine 35. Biochem Biophys Res Commun 2006;342:206-213.
    • (2006) Biochem Biophys Res Commun , vol.342 , pp. 206-213
    • Clementi, M.E.1    Pezzotti, M.2    Orsini, F.3    Sampaolese, B.4    Mezzogori, D.5    Grassi, C.6    Giardina, B.7    Misiti, F.8
  • 36
  • 37
    • 33747195017 scopus 로고    scopus 로고
    • An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity
    • Ferreiro E, Resende R, Costa R, Oliveira CR, Pereira CM. An endoplasmic-reticulum-specific apoptotic pathway is involved in prion and amyloid-beta peptides neurotoxicity. Neurobiol Dis 2006;23:669-678.
    • (2006) Neurobiol Dis , vol.23 , pp. 669-678
    • Ferreiro, E.1    Resende, R.2    Costa, R.3    Oliveira, C.R.4    Pereira, C.M.5
  • 38
    • 33645238970 scopus 로고    scopus 로고
    • Dissociation of ERK and Akt signaling in endothelial cell angiogenic responses to beta-amyloid
    • Magrane J, Christensen RA, Rosen KM, Veereshwarayya V, Querfurth HW. Dissociation of ERK and Akt signaling in endothelial cell angiogenic responses to beta-amyloid. Exp Cell Res 2006;312:996-1010.
    • (2006) Exp Cell Res , vol.312 , pp. 996-1010
    • Magrane, J.1    Christensen, R.A.2    Rosen, K.M.3    Veereshwarayya, V.4    Querfurth, H.W.5
  • 40
    • 0029704210 scopus 로고    scopus 로고
    • Interaction of angiogenic basic fibroblast growth factor with endothelial cell heparan sulfate proteoglycans. Biological implications in neovascularization
    • Rusnati M, Presta M. Interaction of angiogenic basic fibroblast growth factor with endothelial cell heparan sulfate proteoglycans. Biological implications in neovascularization. Int J Clin Lab Res 1996;26:15-23.
    • (1996) Int J Clin Lab Res , vol.26 , pp. 15-23
    • Rusnati, M.1    Presta, M.2
  • 42
    • 4544370585 scopus 로고    scopus 로고
    • Inhibition of endothelial cell tube formation by the low molecular weight heparin, tinzaparin, is mediated by tissue factor pathway inhibitor
    • Mousa SA, Mohamed S. Inhibition of endothelial cell tube formation by the low molecular weight heparin, tinzaparin, is mediated by tissue factor pathway inhibitor. Thromb Haemost 2004;92:627-633.
    • (2004) Thromb Haemost , vol.92 , pp. 627-633
    • Mousa, S.A.1    Mohamed, S.2
  • 43
    • 24744454378 scopus 로고    scopus 로고
    • Heparin regulates vascular endothelial growth factor165-dependent mitogenic activity, tube formation, and its receptor phosphorylation of human endothelial cells. Comparison of the effects of heparin and modified heparins
    • Ashikari-Hada S, Habuchi H, Kariya Y, Kimata K. Heparin regulates vascular endothelial growth factor165-dependent mitogenic activity, tube formation, and its receptor phosphorylation of human endothelial cells. Comparison of the effects of heparin and modified heparins. J Biol Chem 2005;280:31508-31515.
    • (2005) J Biol Chem , vol.280 , pp. 31508-31515
    • Ashikari-Hada, S.1    Habuchi, H.2    Kariya, Y.3    Kimata, K.4
  • 44
    • 33644830185 scopus 로고    scopus 로고
    • Low-molecular-weight heparins and angiogenesis
    • Norrby K. Low-molecular-weight heparins and angiogenesis. APMIS 2006;114:79-102.
    • (2006) APMIS , vol.114 , pp. 79-102
    • Norrby, K.1
  • 45
    • 16244376148 scopus 로고    scopus 로고
    • Specific interaction of VEGF165 with beta-amyloid, and its protective effect on beta-amyloid-induced neurotoxicity
    • Yang SP, Kwon BO, Gho YS, Chae CB. Specific interaction of VEGF165 with beta-amyloid, and its protective effect on beta-amyloid-induced neurotoxicity. J Neurochem 2005;93:118-127.
    • (2005) J Neurochem , vol.93 , pp. 118-127
    • Yang, S.P.1    Kwon, B.O.2    Gho, Y.S.3    Chae, C.B.4
  • 46
    • 0032741507 scopus 로고    scopus 로고
    • Common binding sites for beta-amyloid fibrils and fibroblast growth factor-2 in heparan sulfate from human cerebral cortex
    • Lindahl B, Westling C, Gimenez-Gallego G, Lindahl U, Salmivirta M. Common binding sites for beta-amyloid fibrils and fibroblast growth factor-2 in heparan sulfate from human cerebral cortex. J Biol Chem 1999;274:30631-30635.
    • (1999) J Biol Chem , vol.274 , pp. 30631-30635
    • Lindahl, B.1    Westling, C.2    Gimenez-Gallego, G.3    Lindahl, U.4    Salmivirta, M.5
  • 47
    • 0034904186 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans: Heavy hitters in the angiogenesis arena
    • Iozzo RV, San Antonio JD. Heparan sulfate proteoglycans: heavy hitters in the angiogenesis arena. J Clin Invest 2001;108:349-355.
    • (2001) J Clin Invest , vol.108 , pp. 349-355
    • Iozzo, R.V.1    San Antonio, J.D.2
  • 49
    • 28044442504 scopus 로고    scopus 로고
    • Enzymatic remodeling of heparan sulfate proteoglycans within the tumor microenvironment: Growth regulation and the prospect of new cancer therapies
    • Sanderson RD, Yang Y, Kelly T, Macleod V, Dai Y, Theus A. Enzymatic remodeling of heparan sulfate proteoglycans within the tumor microenvironment: Growth regulation and the prospect of new cancer therapies. J Cell Biochem 2005;96:897-905.
    • (2005) J Cell Biochem , vol.96 , pp. 897-905
    • Sanderson, R.D.1    Yang, Y.2    Kelly, T.3    Macleod, V.4    Dai, Y.5    Theus, A.6
  • 50
    • 0033026552 scopus 로고    scopus 로고
    • The sulfate moieties of glycosaminoglycans are critical for the enhancement of beta-amyloid protein fibril formation
    • Castillo GM, Lukito W, Wight TN, Snow AD. The sulfate moieties of glycosaminoglycans are critical for the enhancement of beta-amyloid protein fibril formation. J Neurochem 1999;72:1681-1687.
    • (1999) J Neurochem , vol.72 , pp. 1681-1687
    • Castillo, G.M.1    Lukito, W.2    Wight, T.N.3    Snow, A.D.4
  • 51
    • 0037022186 scopus 로고    scopus 로고
    • Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro
    • Cohlberg JA, Li J, Uversky VN, Fink AL. Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro. Biochemistry 2002;41:1502-1511.
    • (2002) Biochemistry , vol.41 , pp. 1502-1511
    • Cohlberg, J.A.1    Li, J.2    Uversky, V.N.3    Fink, A.L.4
  • 53
    • 0036167595 scopus 로고    scopus 로고
    • Increased intrathecal levels of the angiogenic factors VEGF and TGF-beta in Alzheimer's disease and vascular dementia
    • Tarkowski E, Issa R, Sjogren M, Wallin A, Blennow K, Tarkowski A, Kumar P. Increased intrathecal levels of the angiogenic factors VEGF and TGF-beta in Alzheimer's disease and vascular dementia. Neurobiol Aging 2002;23:237-243.
    • (2002) Neurobiol Aging , vol.23 , pp. 237-243
    • Tarkowski, E.1    Issa, R.2    Sjogren, M.3    Wallin, A.4    Blennow, K.5    Tarkowski, A.6    Kumar, P.7
  • 54
    • 0030721487 scopus 로고    scopus 로고
    • Brain microvascular changes in Alzheimer's disease and other dementias
    • Buee L, Hof PR, Delacourte A. Brain microvascular changes in Alzheimer's disease and other dementias. Ann NY Acad Sci 1997;826:7-24.
    • (1997) Ann NY Acad Sci , vol.826 , pp. 7-24
    • Buee, L.1    Hof, P.R.2    Delacourte, A.3
  • 55
    • 0034698943 scopus 로고    scopus 로고
    • Activation of MAP kinase (ERK-1/ERK-2), tyrosine kinase and VEGF in the human brain following acute ischaemic stroke
    • Slevin M, Krupinski J, Slowik A, Rubio F, Szczudlik A, Gaffney J. Activation of MAP kinase (ERK-1/ERK-2), tyrosine kinase and VEGF in the human brain following acute ischaemic stroke. Neuroreport 2000;11:2759-2764.
    • (2000) Neuroreport , vol.11 , pp. 2759-2764
    • Slevin, M.1    Krupinski, J.2    Slowik, A.3    Rubio, F.4    Szczudlik, A.5    Gaffney, J.6
  • 56
    • 10744225620 scopus 로고    scopus 로고
    • Vascular endothelial growth factor is increased in cerebrospinal fluid after traumatic brain injury in infants and children
    • Shore PM, Jackson EK, Wisniewski SR, Clark RS, Adelson PD, Kochanek PM. Vascular endothelial growth factor is increased in cerebrospinal fluid after traumatic brain injury in infants and children. Neurosurgery 2004;54:605-611.
    • (2004) Neurosurgery , vol.54 , pp. 605-611
    • Shore, P.M.1    Jackson, E.K.2    Wisniewski, S.R.3    Clark, R.S.4    Adelson, P.D.5    Kochanek, P.M.6
  • 58
    • 2542428253 scopus 로고    scopus 로고
    • Transient cerebral ischemia induces aberrant neuronal cell cycle re-entry and Alzheimer's disease-like tauopathy in female rats
    • Wen Y, Yang S, Liu R, Brun-Zinkernagel AM, Koulen P, Simpkins JW. Transient cerebral ischemia induces aberrant neuronal cell cycle re-entry and Alzheimer's disease-like tauopathy in female rats. J Biol Chem 2004;279:22684-22692.
    • (2004) J Biol Chem , vol.279 , pp. 22684-22692
    • Wen, Y.1    Yang, S.2    Liu, R.3    Brun-Zinkernagel, A.M.4    Koulen, P.5    Simpkins, J.W.6
  • 59
    • 17844385791 scopus 로고    scopus 로고
    • Interactions between Alzheimer's disease and cerebral ischemia - focus on inflammation
    • Koistinaho M, Koistinaho J. Interactions between Alzheimer's disease and cerebral ischemia - focus on inflammation. Brain Res Brain Res Rev 2005;48:240-250.
    • (2005) Brain Res Brain Res Rev , vol.48 , pp. 240-250
    • Koistinaho, M.1    Koistinaho, J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.