메뉴 건너뛰기




Volumn 8, Issue 6, 2013, Pages

Characterization of the Oligomerization and Aggregation of Human Serum Amyloid A

Author keywords

[No Author keywords available]

Indexed keywords

ISOPROTEIN; METHIONINE; SERUM AMYLOID A;

EID: 84878657649     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0064974     Document Type: Article
Times cited : (29)

References (48)
  • 1
    • 0036176146 scopus 로고    scopus 로고
    • Pathology, diagnosis and pathogenesis of AA amyloidosis
    • Rocken C, Shakespeare A, (2002) Pathology, diagnosis and pathogenesis of AA amyloidosis. Virchows Archiv 440: 111-122.
    • (2002) Virchows Archiv , vol.440 , pp. 111-122
    • Rocken, C.1    Shakespeare, A.2
  • 2
    • 0033569982 scopus 로고    scopus 로고
    • Serum amyloid A, the major vertebrate acute-phase reactant
    • Uhlar CM, Whitehead AS, (1999) Serum amyloid A, the major vertebrate acute-phase reactant. European Journal of Biochemistry 265: 501-523.
    • (1999) European Journal of Biochemistry , vol.265 , pp. 501-523
    • Uhlar, C.M.1    Whitehead, A.S.2
  • 3
    • 0033988643 scopus 로고    scopus 로고
    • Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states
    • Urieli-Shoval S, Linke RP, Matzner Y, (2000) Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states. Current Opinion in Hematology 7: 64-69.
    • (2000) Current Opinion in Hematology , vol.7 , pp. 64-69
    • Urieli-Shoval, S.1    Linke, R.P.2    Matzner, Y.3
  • 4
    • 0023755881 scopus 로고
    • Direct Evidence for Circulating ApoSAA as the Precursor of Tissue AA Amyloid Deposits
    • Tape C, Tan R, Nesheim M, Kisilevsky R, (1988) Direct Evidence for Circulating ApoSAA as the Precursor of Tissue AA Amyloid Deposits. Scandinavian Journal of Immunology 28: 317-324.
    • (1988) Scandinavian Journal of Immunology , vol.28 , pp. 317-324
    • Tape, C.1    Tan, R.2    Nesheim, M.3    Kisilevsky, R.4
  • 5
    • 0035822274 scopus 로고    scopus 로고
    • Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein
    • Gillmore JD, Lovat LB, Persey MR, Pepys MB, Hawkins PN, (2001) Amyloid load and clinical outcome in AA amyloidosis in relation to circulating concentration of serum amyloid A protein. Lancet 358: 24-29.
    • (2001) Lancet , vol.358 , pp. 24-29
    • Gillmore, J.D.1    Lovat, L.B.2    Persey, M.R.3    Pepys, M.B.4    Hawkins, P.N.5
  • 6
    • 0021051914 scopus 로고
    • Serum Amyloid A Protein Concentration in Rheumatoid-Arthritis and Its Role in Monitoring Disease-Activity
    • Chambers RE, Macfarlane DG, Whicher JT, Dieppe PA, (1983) Serum Amyloid A Protein Concentration in Rheumatoid-Arthritis and Its Role in Monitoring Disease-Activity. Annals of the Rheumatic Diseases 42: 665-667.
    • (1983) Annals of the Rheumatic Diseases , vol.42 , pp. 665-667
    • Chambers, R.E.1    Macfarlane, D.G.2    Whicher, J.T.3    Dieppe, P.A.4
  • 9
    • 0026647903 scopus 로고
    • Serum Amyloid A Changes High-Density-Lipoproteins Cellular Affinity - a Clue to Serum Amyloid-as Principal Function
    • Kisilevsky R, Subrahmanyan L, (1992) Serum Amyloid A Changes High-Density-Lipoproteins Cellular Affinity- a Clue to Serum Amyloid-as Principal Function. Laboratory Investigation 66: 778-785.
    • (1992) Laboratory Investigation , vol.66 , pp. 778-785
    • Kisilevsky, R.1    Subrahmanyan, L.2
  • 10
    • 0036016553 scopus 로고    scopus 로고
    • Acute phase serum amyloid A, cholesterol metabolism, and cardiovascular disease
    • Kisilevsky R, Tam SP, (2002) Acute phase serum amyloid A, cholesterol metabolism, and cardiovascular disease. Pediatric Pathology & Molecular Medicine 21: 291-305.
    • (2002) Pediatric Pathology & Molecular Medicine , vol.21 , pp. 291-305
    • Kisilevsky, R.1    Tam, S.P.2
  • 11
    • 0036737704 scopus 로고    scopus 로고
    • Promoting export of macrophage cholesterol: the physiological role of a major acute-phase protein, serum amyloid A 2.1
    • Tam SP, Flexman A, Hulme J, Kisilevsky R, (2002) Promoting export of macrophage cholesterol: the physiological role of a major acute-phase protein, serum amyloid A 2.1. Journal of Lipid Research 43: 1410-1420.
    • (2002) Journal of Lipid Research , vol.43 , pp. 1410-1420
    • Tam, S.P.1    Flexman, A.2    Hulme, J.3    Kisilevsky, R.4
  • 13
    • 0027977021 scopus 로고
    • Evolution of the Serum Amyloid-a (Saa) Protein Superfamily
    • Uhlar CM, Burgess CJ, Sharp PM, Whitehead AS, (1994) Evolution of the Serum Amyloid-a (Saa) Protein Superfamily. Genomics 19: 228-235.
    • (1994) Genomics , vol.19 , pp. 228-235
    • Uhlar, C.M.1    Burgess, C.J.2    Sharp, P.M.3    Whitehead, A.S.4
  • 14
    • 0027424029 scopus 로고
    • Serum Amyloid A (SAA) - an Acute-Phase Protein and Apolipoprotein
    • Malle E, Steinmetz A, Raynes JG, (1993) Serum Amyloid A (SAA)- an Acute-Phase Protein and Apolipoprotein. Atherosclerosis 102: 131-146.
    • (1993) Atherosclerosis , vol.102 , pp. 131-146
    • Malle, E.1    Steinmetz, A.2    Raynes, J.G.3
  • 18
    • 0020476110 scopus 로고
    • Amino-Acid-Sequence of Amyloid-Related Apoprotein (Aposaa1) from Human High-Density Lipoprotein
    • Parmelee DC, Titani K, Ericsson LH, Eriksen N, Benditt EP, et al. (1982) Amino-Acid-Sequence of Amyloid-Related Apoprotein (Aposaa1) from Human High-Density Lipoprotein. Biochemistry 21: 3298-3303.
    • (1982) Biochemistry , vol.21 , pp. 3298-3303
    • Parmelee, D.C.1    Titani, K.2    Ericsson, L.H.3    Eriksen, N.4    Benditt, E.P.5
  • 19
    • 79960386345 scopus 로고    scopus 로고
    • Serum Amyloid A Activates the NLRP3 Inflammasome and Promotes Th17 Allergic Asthma in Mice
    • Ather JL, Ckless K, Martin R, Foley KL, Suratt BT, et al. (2011) Serum Amyloid A Activates the NLRP3 Inflammasome and Promotes Th17 Allergic Asthma in Mice. Journal of Immunology 187: 64-73.
    • (2011) Journal of Immunology , vol.187 , pp. 64-73
    • Ather, J.L.1    Ckless, K.2    Martin, R.3    Foley, K.L.4    Suratt, B.T.5
  • 24
    • 84857198063 scopus 로고    scopus 로고
    • Acute-phase serum amyloid A: Perspectives on its physiological and pathological roles
    • Kisilevsky R, Manley PN, (2012) Acute-phase serum amyloid A: Perspectives on its physiological and pathological roles. Amyloid-Journal of Protein Folding Disorders 19: 5-14.
    • (2012) Amyloid-Journal of Protein Folding Disorders , vol.19 , pp. 5-14
    • Kisilevsky, R.1    Manley, P.N.2
  • 25
    • 23044449398 scopus 로고    scopus 로고
    • Amyloid ion channels: a common structural link for protein-misfolding disease
    • Quist A, Doudevski I, Lin H, Azimova R, Ng D, et al. (2005) Amyloid ion channels: a common structural link for protein-misfolding disease. Proc Natl Acad Sci U S A 102: 10427-10432.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 10427-10432
    • Quist, A.1    Doudevski, I.2    Lin, H.3    Azimova, R.4    Ng, D.5
  • 27
    • 0032933232 scopus 로고    scopus 로고
    • Expression of serum amyloid A protein in the absence of the acute phase response does not reduce HDL cholesterol or apoA-I levels in human apoA-I transgenic mice
    • Hosoai H, Webb NR, Glick JM, Tietge UJF, Purdom MS, et al. (1999) Expression of serum amyloid A protein in the absence of the acute phase response does not reduce HDL cholesterol or apoA-I levels in human apoA-I transgenic mice. Journal of Lipid Research 40: 648-653.
    • (1999) Journal of Lipid Research , vol.40 , pp. 648-653
    • Hosoai, H.1    Webb, N.R.2    Glick, J.M.3    Tietge, U.J.F.4    Purdom, M.S.5
  • 29
    • 47949085624 scopus 로고    scopus 로고
    • Cutting edge: TLR2 is a functional receptor for acute-phase serum amyloid A
    • Cheng N, He R, Tian J, Ye PP, Ye RD, (2008) Cutting edge: TLR2 is a functional receptor for acute-phase serum amyloid A. Journal of Immunology. 181: 22-26.
    • (2008) Journal of Immunology , vol.181 , pp. 22-26
    • Cheng, N.1    He, R.2    Tian, J.3    Ye, P.P.4    Ye, R.D.5
  • 30
    • 58849134296 scopus 로고    scopus 로고
    • Serum amyloid A induces G-CSF expression and neutrophilia via Toll-like receptor 2
    • He RL, Zhou J, Hanson CZ, Chen J, Cheng N, et al. (2009) Serum amyloid A induces G-CSF expression and neutrophilia via Toll-like receptor 2. Blood 113: 429-437.
    • (2009) Blood , vol.113 , pp. 429-437
    • He, R.L.1    Zhou, J.2    Hanson, C.Z.3    Chen, J.4    Cheng, N.5
  • 31
    • 84859592416 scopus 로고    scopus 로고
    • Influence of the Carboxy Terminus of Serum Amyloid A on Protein Oligomerization, Misfolding, and Fibril Formation
    • Patke S, Maheshwari R, Litt J, Srinivasan S, Aguilera JJ, et al. (2012) Influence of the Carboxy Terminus of Serum Amyloid A on Protein Oligomerization, Misfolding, and Fibril Formation. Biochemistry 51: 3092-3099.
    • (2012) Biochemistry , vol.51 , pp. 3092-3099
    • Patke, S.1    Maheshwari, R.2    Litt, J.3    Srinivasan, S.4    Aguilera, J.J.5
  • 32
    • 84873878454 scopus 로고    scopus 로고
    • Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2
    • Srinivasan S, Patke S, Wang Y, Ye Z, Litt J, et al. (2013) Pathogenic serum amyloid A 1.1 shows a long oligomer-rich fibrillation lag phase contrary to the highly amyloidogenic non-pathogenic SAA2.2. J Biol Chem 288: 2744-2755.
    • (2013) J Biol Chem , vol.288 , pp. 2744-2755
    • Srinivasan, S.1    Patke, S.2    Wang, Y.3    Ye, Z.4    Litt, J.5
  • 33
    • 0142247606 scopus 로고    scopus 로고
    • pH-dependent amyloid and protofibril formation by the ABri peptide of familial British dementia
    • Srinivasan R, Jones EM, Liu K, Ghiso J, Marchant RE, et al. (2003) pH-dependent amyloid and protofibril formation by the ABri peptide of familial British dementia. J Mol Biol 333: 1003-1023.
    • (2003) J Mol Biol , vol.333 , pp. 1003-1023
    • Srinivasan, R.1    Jones, E.M.2    Liu, K.3    Ghiso, J.4    Marchant, R.E.5
  • 36
    • 22244492326 scopus 로고    scopus 로고
    • Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer
    • Wang LM, Colon W, (2005) Urea-induced denaturation of apolipoprotein serum amyloid A reveals marginal stability of hexamer. Protein Science 14: 1811-1817.
    • (2005) Protein Science , vol.14 , pp. 1811-1817
    • Wang, L.M.1    Colon, W.2
  • 37
    • 27144480726 scopus 로고    scopus 로고
    • From hexamer to amyloid: Marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature
    • Wang LM, Lashuel HA, Colon W, (2005) From hexamer to amyloid: Marginal stability of apolipoprotein SAA2.2 leads to in vitro fibril formation at physiological temperature. Amyloid-Journal of Protein Folding Disorders 12: 139-148.
    • (2005) Amyloid-Journal of Protein Folding Disorders , vol.12 , pp. 139-148
    • Wang, L.M.1    Lashuel, H.A.2    Colon, W.3
  • 38
    • 80054969302 scopus 로고    scopus 로고
    • Inflammation Protein SAA2.2 Spontaneously Forms Marginally Stable Amyloid Fibrils at Physiological Temperature
    • Ye ZQ, Poueymiroy DB, Aguilera JJ, Srinivasan S, Wang Y, et al. (2011) Inflammation Protein SAA2.2 Spontaneously Forms Marginally Stable Amyloid Fibrils at Physiological Temperature. Biochemistry 50: 9184-9191.
    • (2011) Biochemistry , vol.50 , pp. 9184-9191
    • Ye, Z.Q.1    Poueymiroy, D.B.2    Aguilera, J.J.3    Srinivasan, S.4    Wang, Y.5
  • 39
    • 0027502784 scopus 로고
    • Thioflavine-T Interaction with Synthetic Alzheimers-Disease Beta-Amyloid Peptides - Detection of Amyloid Aggregation in Solution
    • Levine H, (1993) Thioflavine-T Interaction with Synthetic Alzheimers-Disease Beta-Amyloid Peptides- Detection of Amyloid Aggregation in Solution. Protein Science 2: 404-410.
    • (1993) Protein Science , vol.2 , pp. 404-410
    • Levine, H.1
  • 40
    • 0032899322 scopus 로고    scopus 로고
    • Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay
    • Klunk WE, Jacob RF, Mason RP, (1999) Quantifying amyloid beta-peptide (Abeta) aggregation using the Congo red-Abeta (CR-abeta) spectrophotometric assay. Anal Biochem 266: 66-76.
    • (1999) Anal Biochem , vol.266 , pp. 66-76
    • Klunk, W.E.1    Jacob, R.F.2    Mason, R.P.3
  • 41
    • 0024212706 scopus 로고
    • Circular-dichroism studies on two murine serum amyloid A proteins
    • McCubbin WD, Kay CM, Narindrasorasak S, Kisilevsky R, (1988) Circular-dichroism studies on two murine serum amyloid A proteins. Biochem J 256: 775-783.
    • (1988) Biochem J , vol.256 , pp. 775-783
    • McCubbin, W.D.1    Kay, C.M.2    Narindrasorasak, S.3    Kisilevsky, R.4
  • 42
    • 77949889842 scopus 로고    scopus 로고
    • Conformations within Soluble Oligomers and Insoluble Aggregates Revealed by Resonance Energy Transfer
    • Digambaranath JL, Dang LA, Dembinska M, Vasyluk A, Finke JM, (2010) Conformations within Soluble Oligomers and Insoluble Aggregates Revealed by Resonance Energy Transfer. Biopolymers 93: 299-317.
    • (2010) Biopolymers , vol.93 , pp. 299-317
    • Digambaranath, J.L.1    Dang, L.A.2    Dembinska, M.3    Vasyluk, A.4    Finke, J.M.5
  • 43
    • 0242668337 scopus 로고    scopus 로고
    • Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis
    • Kayed R, Head E, Thompson JL, McIntire TM, Milton SC, et al. (2003) Common structure of soluble amyloid oligomers implies common mechanism of pathogenesis. Science 300: 486-489.
    • (2003) Science , vol.300 , pp. 486-489
    • Kayed, R.1    Head, E.2    Thompson, J.L.3    McIntire, T.M.4    Milton, S.C.5
  • 44
    • 36749078121 scopus 로고    scopus 로고
    • Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers
    • Kayed R, Head E, Sarsoza F, Saing T, Cotman CW, et al. (2007) Fibril specific, conformation dependent antibodies recognize a generic epitope common to amyloid fibrils and fibrillar oligomers that is absent in prefibrillar oligomers. Molecular Neurodegeneration 2: 18.
    • (2007) Molecular Neurodegeneration , vol.2 , pp. 18
    • Kayed, R.1    Head, E.2    Sarsoza, F.3    Saing, T.4    Cotman, C.W.5
  • 46
    • 0029777342 scopus 로고    scopus 로고
    • Expression of recombinant human serum amyloid A in mammalian cells and demonstration of the region necessary for high-density lipoprotein binding and amyloid fibril formation by site-directed mutagenesis
    • Patel H, Bramall J, Waters H, De Beer MC, Woo P, (1996) Expression of recombinant human serum amyloid A in mammalian cells and demonstration of the region necessary for high-density lipoprotein binding and amyloid fibril formation by site-directed mutagenesis. Biochem J 318 (Pt 3): 1041-1049.
    • (1996) Biochem J , vol.318 , Issue.PT 3 , pp. 1041-1049
    • Patel, H.1    Bramall, J.2    Waters, H.3    De Beer, M.C.4    Woo, P.5
  • 47
    • 34248165082 scopus 로고    scopus 로고
    • Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A
    • Wang LM, Colon W, (2007) Effect of zinc, copper, and calcium on the structure and stability of serum amyloid A. Biochemistry. 46: 5562-5569.
    • (2007) Biochemistry , vol.46 , pp. 5562-5569
    • Wang, L.M.1    Colon, W.2
  • 48
    • 84864105671 scopus 로고    scopus 로고
    • Heparan Sulfate Dissociates Serum Amyloid A (SAA) from Acute-phase High-density Lipoprotein, Promoting SAA Aggregation
    • Noborn F, Ancsin JB, Ubhayasekera W, Kisilevsk R, Li JP, (2012) Heparan Sulfate Dissociates Serum Amyloid A (SAA) from Acute-phase High-density Lipoprotein, Promoting SAA Aggregation. Journal of Biological Chemistry 287: 25669-25677.
    • (2012) Journal of Biological Chemistry , vol.287 , pp. 25669-25677
    • Noborn, F.1    Ancsin, J.B.2    Ubhayasekera, W.3    Kisilevsk, R.4    Li, J.P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.