메뉴 건너뛰기




Volumn 287, Issue 33, 2012, Pages 28163-28168

Human serum albumin can regulate amyloid-β peptide fiber growth in the brain interstitium: Implications for Alzheimer disease

Author keywords

[No Author keywords available]

Indexed keywords

ALZHEIMER DISEASE; AMYLOID FIBERS; BLOOD PLASMA; EXTRACELLULAR ACCUMULATIONS; FIBRIL GROWTH; FIBRILLIZATION; HUMAN SERUM ALBUMINS; LAG-TIME; NEURODEGENERATIVE DISORDERS; PEPTIDE FIBERS; PERIPHERAL TISSUE;

EID: 84865007775     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.C112.360800     Document Type: Article
Times cited : (136)

References (32)
  • 1
    • 0037135111 scopus 로고    scopus 로고
    • The amyloid hypothesis of Alzheimer disease: Progress and problems on the road to therapeutics
    • Hardy, J., and Selkoe, D. J. (2002) The amyloid hypothesis of Alzheimer disease: progress and problems on the road to therapeutics. Science 297, 353-356
    • (2002) Science , vol.297 , pp. 353-356
    • Hardy, J.1    Selkoe, D.J.2
  • 3
    • 80054084612 scopus 로고    scopus 로고
    • Quantitation of amyloid-β peptides Aβ(1-38), Aβ(1-40), and Aβ(1-42) in human cerebrospinal fluid by ultra-performance liquid chromatography-tandem mass spectrometry
    • Lame, M. E., Chambers, E. E., and Blatnik, M. (2011) Quantitation of amyloid-β peptides Aβ(1-38), Aβ(1-40), and Aβ(1-42) in human cerebrospinal fluid by ultra-performance liquid chromatography-tandem mass spectrometry. Anal. Biochem. 419, 133-139
    • (2011) Anal. Biochem. , vol.419 , pp. 133-139
    • Lame, M.E.1    Chambers, E.E.2    Blatnik, M.3
  • 6
    • 0028227096 scopus 로고
    • Structure of serum albumin
    • Carter, D. C., and Ho, J. X. (1994) Structure of serum albumin. Adv. Protein Chem. 45, 153-203
    • (1994) Adv. Protein Chem. , vol.45 , pp. 153-203
    • Carter, D.C.1    Ho, J.X.2
  • 7
    • 0018663461 scopus 로고
    • Application of fluoroimmunoassay to cerebrospinal fluid immunoglobulin G and albumin
    • Stevens, R. W., Elmendorf, D., Gourlay, M., Stroebel, E., and Gaafar, H. A. (1979) Application of fluoroimmunoassay to cerebrospinal fluid immunoglobulin G and albumin. J. Clin. Microbiol. 10, 346-350
    • (1979) J. Clin. Microbiol. , vol.10 , pp. 346-350
    • Stevens, R.W.1    Elmendorf, D.2    Gourlay, M.3    Stroebel, E.4    Gaafar, H.A.5
  • 9
    • 0033522988 scopus 로고    scopus 로고
    • Endogenous proteins controlling amyloid-β peptide polymerization: Possible implications for β-amyloid formation in the central nervous system and in peripheral tissues
    • Bohrmann, B., Tjernberg, L., Kuner, P., Poli, S., Levet-Trafit, B., Näslund, J., Richards, G., Huber, W., Döbeli, H., and Nordstedt, C. (1999) Endogenous proteins controlling amyloid-β peptide polymerization: possible implications for β-amyloid formation in the central nervous system and in peripheral tissues. J. Biol. Chem. 274, 15990-15995
    • (1999) J. Biol. Chem. , vol.274 , pp. 15990-15995
    • Bohrmann, B.1    Tjernberg, L.2    Kuner, P.3    Poli, S.4    Levet-Trafit, B.5    Näslund, J.6    Richards, G.7    Huber, W.8    Döbeli, H.9    Nordstedt, C.10
  • 10
    • 34247204257 scopus 로고    scopus 로고
    • Understanding the molecular basis for the inhibition of the Alzheimer Aβ-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation NMR spectroscopy
    • Milojevic, J., Esposito, V., Das, R., and Melacini, G. (2007) Understanding the molecular basis for the inhibition of the Alzheimer Aβ-peptide oligomerization by human serum albumin using saturation transfer difference and off-resonance relaxation NMR spectroscopy. J. Am. Chem. Soc. 129, 4282-4290
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 4282-4290
    • Milojevic, J.1    Esposito, V.2    Das, R.3    Melacini, G.4
  • 11
    • 78651245383 scopus 로고    scopus 로고
    • Stoichiometry and affinity of the human serum albumin-Alzheimer Aβ peptide interactions
    • Milojevic, J., and Melacini, G. (2011) Stoichiometry and affinity of the human serum albumin-Alzheimer Aβ peptide interactions. Biophys. J. 100, 183-192
    • (2011) Biophys. J. , vol.100 , pp. 183-192
    • Milojevic, J.1    Melacini, G.2
  • 12
    • 72249108028 scopus 로고    scopus 로고
    • Human serum albumin inhibits Aβ fibrillization through a "monomer-competitor" mechanism
    • Milojevic, J., Raditsis, A., and Melacini, G. (2009) Human serum albumin inhibits Aβ fibrillization through a "monomer-competitor" mechanism. Biophys. J. 97, 2585-2594
    • (2009) Biophys. J. , vol.97 , pp. 2585-2594
    • Milojevic, J.1    Raditsis, A.2    Melacini, G.3
  • 13
    • 66149099335 scopus 로고    scopus 로고
    • Soluble aggregates of the amyloid-β peptide are trapped by serum albumin to enhance amyloid-β activation of endothelial cells
    • Reyes Barcelo, A. A., Gonzalez-Velasquez, F. J., and Moss, M. A. (2009) Soluble aggregates of the amyloid-β peptide are trapped by serum albumin to enhance amyloid-β activation of endothelial cells. J. Biol. Eng. 3, 5-12
    • (2009) J. Biol. Eng. , vol.3 , pp. 5-12
    • Reyes Barcelo, A.A.1    Gonzalez-Velasquez, F.J.2    Moss, M.A.3
  • 14
    • 0035941201 scopus 로고    scopus 로고
    • Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein: A possible molecular NK between Parkinson disease and heavy metal exposure
    • Uversky, V. N., Li, J., and Fink, A. L. (2001) Metal-triggered structural transformations, aggregation, and fibrillation of human α-synuclein: a possible molecular NK between Parkinson disease and heavy metal exposure. J. Biol. Chem. 276, 44284-44296
    • (2001) J. Biol. Chem. , vol.276 , pp. 44284-44296
    • Uversky, V.N.1    Li, J.2    Fink, A.L.3
  • 15
    • 61349201380 scopus 로고    scopus 로고
    • Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers
    • Laurén, J., Gimbel, D. A., Nygaard, H. B., Gilbert, J. W., and Strittmatter, S. M. (2009) Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers. Nature 457, 1128-1132
    • (2009) Nature , vol.457 , pp. 1128-1132
    • Laurén, J.1    Gimbel, D.A.2    Nygaard, H.B.3    Gilbert, J.W.4    Strittmatter, S.M.5
  • 17
    • 77951177586 scopus 로고    scopus 로고
    • Identification of hot regions of the Aβ-IAPP interaction interface as high-affinity binding sites in both cross- and self-association
    • Andreetto, E., Yan, L. M., Tatarek-Nossol, M., Velkova, A., Frank, R., and Kapurniotu, A. (2010) Identification of hot regions of the Aβ-IAPP interaction interface as high-affinity binding sites in both cross- and self-association. Angew. Chem. Int. Ed. Engl. 49, 3081-3085
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 3081-3085
    • Andreetto, E.1    Yan, L.M.2    Tatarek-Nossol, M.3    Velkova, A.4    Frank, R.5    Kapurniotu, A.6
  • 19
    • 0023899417 scopus 로고
    • Isolation and characterization of amyloid P component from Alzheimer disease and other types of cerebral amyloidosis
    • Coria, F., Castaño, E., Prelli, F., Larrondo-Lillo, M., van Duinen, S., Shelanski, M. L., and Frangione, B. (1988) Isolation and characterization of amyloid P component from Alzheimer disease and other types of cerebral amyloidosis. Lab. Invest. 58, 454-458
    • (1988) Lab. Invest. , vol.58 , pp. 454-458
    • Coria, F.1    Castaño, E.2    Prelli, F.3    Larrondo-Lillo, M.4    Van Duinen, S.5    Shelanski, M.L.6    Frangione, B.7
  • 20
    • 0031683467 scopus 로고    scopus 로고
    • Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites
    • Curry, S., Mandelkow, H., Brick, P., and Franks, N. (1998) Crystal structure of human serum albumin complexed with fatty acid reveals an asymmetric distribution of binding sites. Nat. Struct. Biol. 5, 827-835
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 827-835
    • Curry, S.1    Mandelkow, H.2    Brick, P.3    Franks, N.4
  • 21
    • 85022776230 scopus 로고
    • Direct detection of albumin in human blood plasma by proton NMR spectroscopy. Complexation of nickel2+
    • Patel, S. U., Sadler, P. J., Tucker, A., and Viles, J. H. (1993) Direct detection of albumin in human blood plasma by proton NMR spectroscopy. Complexation of nickel2+. J. Am. Chem. Soc. 115, 9285-9286
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 9285-9286
    • Patel, S.U.1    Sadler, P.J.2    Tucker, A.3    Viles, J.H.4
  • 22
    • 78650650375 scopus 로고    scopus 로고
    • Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-β from Alzheimer disease
    • Sarell, C. J., Wilkinson, S. R., and Viles, J. H. (2010) Substoichiometric levels of Cu2+ ions accelerate the kinetics of fiber formation and promote cell toxicity of amyloid-β from Alzheimer disease. J. Biol. Chem. 285, 41533-41540
    • (2010) J. Biol. Chem. , vol.285 , pp. 41533-41540
    • Sarell, C.J.1    Wilkinson, S.R.2    Viles, J.H.3
  • 24
    • 84864532442 scopus 로고    scopus 로고
    • Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and Prion disease
    • in press
    • Viles, J. H. (2012) Metal ions and amyloid fiber formation in neurodegenerative diseases. Copper, zinc and iron in Alzheimer's, Parkinson's and Prion disease. Coord. Chem. Rev., in press
    • (2012) Coord. Chem. Rev.
    • Viles, J.H.1
  • 25
    • 75649136954 scopus 로고    scopus 로고
    • Copper transfer from Cu-Aβ to human serum albumin inhibits aggregation, radical production and reduces Aβ toxicity
    • Perrone, L., Mothes, E., Vignes, M., Mockel, A., Figueroa, C., Miquel, M. C., Maddelein, M. L., and Faller, P. (2010) Copper transfer from Cu-Aβ to human serum albumin inhibits aggregation, radical production and reduces Aβ toxicity. ChemBioChem 11, 110-118
    • (2010) ChemBioChem , vol.11 , pp. 110-118
    • Perrone, L.1    Mothes, E.2    Vignes, M.3    Mockel, A.4    Figueroa, C.5    Miquel, M.C.6    Maddelein, M.L.7    Faller, P.8
  • 26
    • 34547492662 scopus 로고
    • Studies of blood-brain-barrier permeability and of intrathecal IgG synthesis in patients with Alzheimer's Disease and multi-infarct dementia
    • Licastro, F., Morini, M. C., Davis, L. J., Biagi, R., Prete, L., and Savorani, G. (1993) Studies of blood-brain-barrier permeability and of intrathecal IgG synthesis in patients with Alzheimer's Disease and multi-infarct dementia. Adv. Biosci. 87, 283-284
    • (1993) Adv. Biosci. , vol.87 , pp. 283-284
    • Licastro, F.1    Morini, M.C.2    Davis, L.J.3    Biagi, R.4    Prete, L.5    Savorani, G.6
  • 27
    • 0020632398 scopus 로고
    • Interpretation of cerebrospinal fluid protein assays in various neurologic diseases
    • Christenson, R. H., Behlmer, P., Howard, J. F., Jr., Winfield, J. B., and Silverman, L. M. (1983) Interpretation of cerebrospinal fluid protein assays in various neurologic diseases. Clin. Chem. 29, 1028-1030
    • (1983) Clin. Chem. , vol.29 , pp. 1028-1030
    • Christenson, R.H.1    Behlmer, P.2    Howard Jr., J.F.3    Winfield, J.B.4    Silverman, L.M.5
  • 28
    • 0022973995 scopus 로고
    • Serum amyloid A protein, albumin, and prealbumin in Alzheimer disease and in demented patients with Down syndrome
    • Elovaara, I., Maury, C. P., and Palo, J. (1986) Serum amyloid A protein, albumin, and prealbumin in Alzheimer disease and in demented patients with Down syndrome. Acta Neurol. Scand. 74, 245-250
    • (1986) Acta Neurol. Scand. , vol.74 , pp. 245-250
    • Elovaara, I.1    Maury, C.P.2    Palo, J.3
  • 29
    • 0023191678 scopus 로고
    • Serum and cerebrospinal fluid proteins and the blood-brain barrier in Alzheimer disease and multi-infarct dementia
    • Elovaara, I., Palo, J., Erkinjuntti, T., and Sulkava, R. (1987) Serum and cerebrospinal fluid proteins and the blood-brain barrier in Alzheimer disease and multi-infarct dementia. Eur. Neurol. 26, 229-234
    • (1987) Eur. Neurol. , vol.26 , pp. 229-234
    • Elovaara, I.1    Palo, J.2    Erkinjuntti, T.3    Sulkava, R.4
  • 32
    • 0031961832 scopus 로고    scopus 로고
    • Cerebrovascular accumulation and increased blood-brain barrier permeability to circulating Alzheimer amyloid-β peptide in aged squirrel monkey with cerebral amyloid angiopathy
    • Mackic, J. B., Weiss, M. H., Miao, W., Kirkman, E., Ghiso, J., Calero, M., Bading, J., Frangione, B., and Zlokovic, B. V. (1998) Cerebrovascular accumulation and increased blood-brain barrier permeability to circulating Alzheimer amyloid-β peptide in aged squirrel monkey with cerebral amyloid angiopathy. J. Neurochem. 70, 210-215
    • (1998) J. Neurochem. , vol.70 , pp. 210-215
    • Mackic, J.B.1    Weiss, M.H.2    Miao, W.3    Kirkman, E.4    Ghiso, J.5    Calero, M.6    Bading, J.7    Frangione, B.8    Zlokovic, B.V.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.