메뉴 건너뛰기




Volumn 21, Issue 1, 2000, Pages 35-49

Mechanisms of amyloidosis and the proteins involved;Mecanismes de l'amylose et proteines impliquees

Author keywords

Amyloidosis; Classification; Physiopathology

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID P COMPONENT; APOLIPOPROTEIN E; BETA 2 MICROGLOBULIN; GLYCOSAMINOGLYCAN; SERUM AMYLOID A;

EID: 0033972329     PISSN: 02488663     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0248-8663(00)87227-6     Document Type: Article
Times cited : (8)

References (117)
  • 1
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidosis - the β-fibrilloses I
    • Glenner GG. Amyloid deposits and amyloidosis - the β-fibrilloses I. N Engl J Med 1980 ; 302 : 1283-92.
    • (1980) N Engl J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 2
    • 0019496124 scopus 로고
    • The basis of the staining of amyloid fibers: Their physicochemical nature and the mechanisms of their dye-substrate interaction
    • Glenner GG. The basis of the staining of amyloid fibers: Their physicochemical nature and the mechanisms of their dye-substrate interaction. Prog Histochem Cytochem 1981 ; 13 : 1-37
    • (1981) Prog Histochem Cytochem , vol.13 , pp. 1-37
    • Glenner, G.G.1
  • 3
    • 0022911274 scopus 로고
    • Secondary structure prediction of human SAA1: Presumptive identification of calcium and lipid binding sites
    • Turnell W, Sarra R, Glover ID, Baum JO, Caspi D, Baltz ML, et al. Secondary structure prediction of human SAA1: Presumptive identification of calcium and lipid binding sites. Mol Biol Med 1986 ; 3 : 387-407.
    • (1986) Mol Biol Med , vol.3 , pp. 387-407
    • Turnell, W.1    Sarra, R.2    Glover, I.D.3    Baum, J.O.4    Caspi, D.5    Baltz, M.L.6
  • 5
    • 0019788234 scopus 로고
    • Degradation of amyloid proteins by different serine proteases
    • Skogen B, Natvig JB. Degradation of amyloid proteins by different serine proteases. Scand J Immunol 1981 ; 14 : 389-96.
    • (1981) Scand J Immunol , vol.14 , pp. 389-396
    • Skogen, B.1    Natvig, J.B.2
  • 6
    • 0015219685 scopus 로고
    • Amyloid fibril proteins: Proof of homology with immunoglobulin light chains by sequence analyses
    • Glenner GG, Terry W, Harada M, Isersky C, Page D. Amyloid fibril proteins: Proof of homology with immunoglobulin light chains by sequence analyses. Science 1971 ; 172 : 1150-1.
    • (1971) Science , vol.172 , pp. 1150-1151
    • Glenner, G.G.1    Terry, W.2    Harada, M.3    Isersky, C.4    Page, D.5
  • 9
    • 0015256234 scopus 로고
    • Immunoglobulins and amyloidosis: An immunologic study of sixty-two patients with biopsy-proved disease
    • Cathcart ES, Ritchie RF, Cohen AS, Brandt K. Immunoglobulins and amyloidosis: An immunologic study of sixty-two patients with biopsy-proved disease. Am J Med 1972 ; 52 : 93-101.
    • (1972) Am J Med , vol.52 , pp. 93-101
    • Cathcart, E.S.1    Ritchie, R.F.2    Cohen, A.S.3    Brandt, K.4
  • 10
    • 0019951737 scopus 로고
    • Bences-Jonces proteins and light chains of immunoglobulins: Preferential association of the lambda VI subgroup of human light chains with amyloidosis AL (lambda)
    • Solomon A, Frangione B, Franklin EC. Bences-Jonces proteins and light chains of immunoglobulins: Preferential association of the lambda VI subgroup of human light chains with amyloidosis AL (lambda). J Clin Invest 1982 ; 70 : 453-60.
    • (1982) J Clin Invest , vol.70 , pp. 453-460
    • Solomon, A.1    Frangione, B.2    Franklin, E.C.3
  • 11
    • 0015419122 scopus 로고
    • The amino acid sequence of a major non immunoglobulin component of some amyloid fibrils
    • Levin M, Franklin EC, Frangione B, Pras M. The amino acid sequence of a major non immunoglobulin component of some amyloid fibrils. J Clin Invest 1972 ; 51 : 2773-6.
    • (1972) J Clin Invest , vol.51 , pp. 2773-2776
    • Levin, M.1    Franklin, E.C.2    Frangione, B.3    Pras, M.4
  • 12
    • 0017114947 scopus 로고
    • Isolation and partial characterization of SAA - An amyloid-related protein from human serum
    • Rosenthal CJ, Franklin EC, Frangione B, Greenspan J. Isolation and partial characterization of SAA - An amyloid-related protein from human serum. J Immunol 1976 ; 116 : 1415-8.
    • (1976) J Immunol , vol.116 , pp. 1415-1418
    • Rosenthal, C.J.1    Franklin, E.C.2    Frangione, B.3    Greenspan, J.4
  • 13
    • 0015846635 scopus 로고
    • Immunologic studies of the major nonimmunoglobulin protein of amyloid. Identification and partial characterization of a related serum component
    • Levin M, Pras M, Franklin EC. Immunologic studies of the major nonimmunoglobulin protein of amyloid. Identification and partial characterization of a related serum component. J Exp Med 1973 ; 138 : 373-80.
    • (1973) J Exp Med , vol.138 , pp. 373-380
    • Levin, M.1    Pras, M.2    Franklin, E.C.3
  • 16
    • 0019969508 scopus 로고
    • Serum amyloid A protein concentration in inflammatory diseases and its relationship to the incidence of reactive systemic amyloidosis
    • de Beer FC, Mallga RK, Fagan EA, Lanham JG, Hugues GRV, Pepys MB. Serum amyloid A protein concentration in inflammatory diseases and its relationship to the incidence of reactive systemic amyloidosis. Lancet 1982 ; ii : 231-4.
    • (1982) Lancet , vol.2 , pp. 231-234
    • De Beer, F.C.1    Mallga, R.K.2    Fagan, E.A.3    Lanham, J.G.4    Hugues, G.R.V.5    Pepys, M.B.6
  • 17
    • 0025257454 scopus 로고
    • L'apolipoprotéine sérique amyloïde A (apo SAA): Implication dans l'inflammation et dans les modifications des lipoprotéines
    • Saïle R, Fruchart JC. L'apolipoprotéine sérique amyloïde A (apo SAA): Implication dans l'inflammation et dans les modifications des lipoprotéines. Ann Biol Clin 1990 ; 48 : 77-85.
    • (1990) Ann Biol Clin , vol.48 , pp. 77-85
    • Saïle, R.1    Fruchart, J.C.2
  • 18
    • 0023719605 scopus 로고
    • Enzyme linked immunosorbent assay for serum amyloid A apolipoprotein with use of specific antibodies against synthetic peptides
    • Saïle R, Delpierre C, Puchois P, Hocke G, Cachera C, Gesquière JC, et al. Enzyme linked immunosorbent assay for serum amyloid A apolipoprotein with use of specific antibodies against synthetic peptides. Clin Chem 1988 ; 34 : 1767-71.
    • (1988) Clin Chem , vol.34 , pp. 1767-1771
    • Saïle, R.1    Delpierre, C.2    Puchois, P.3    Hocke, G.4    Cachera, C.5    Gesquière, J.C.6
  • 19
    • 0024463068 scopus 로고
    • Antipeptide antibodies discriminate between different SAA proteins in human plasma
    • Saïle R, Hocke G, Tartar A, Fruchart JC, Steinmetz A. Antipeptide antibodies discriminate between different SAA proteins in human plasma. Biochim Biophys Acta 1989 ; 992 : 407-8.
    • (1989) Biochim Biophys Acta , vol.992 , pp. 407-408
    • Saïle, R.1    Hocke, G.2    Tartar, A.3    Fruchart, J.C.4    Steinmetz, A.5
  • 21
    • 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 FC, Woo P. 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 1996 ; 318 : 1041-9.
    • (1996) Biochem J , vol.318 , pp. 1041-1049
    • Patel, H.1    Bramall, J.2    Waters, H.3    De Beer, F.C.4    Woo, P.5
  • 22
    • 0024552713 scopus 로고
    • Analyse quantitative des apolipoprotéines et des particules lipoprotéiniques chez les traumatisés crâniens
    • Kabbaj O, Saïle R, Ghalim N, Parra HJ, Puchois P, Fruchart JC, et al. Analyse quantitative des apolipoprotéines et des particules lipoprotéiniques chez les traumatisés crâniens. Ann Biol Clin 1989 ; 47 : 35-40.
    • (1989) Ann Biol Clin , vol.47 , pp. 35-40
    • Kabbaj, O.1    Saïle, R.2    Ghalim, N.3    Parra, H.J.4    Puchois, P.5    Fruchart, J.C.6
  • 24
    • 84942558618 scopus 로고
    • Variations in apolipoproteins serum amyloid A, A-I, A-II and C-III in severely head injured patients
    • Saïle R, Kabbaj O, Visvikis S, Steinmetz J, Steinmetz A, Ferard G, et al. Variations in apolipoproteins serum amyloid A, A-I, A-II and C-III in severely head injured patients. J Clin Chem Clin Biochem 1990 ; 28 : 519-25.
    • (1990) J Clin Chem Clin Biochem , vol.28 , pp. 519-525
    • Saïle, R.1    Kabbaj, O.2    Visvikis, S.3    Steinmetz, J.4    Steinmetz, A.5    Ferard, G.6
  • 25
    • 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 UJ, Purdom MS, de Beer FC, et al. 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. J Lipid Res 1999 ; 40 : 648-53.
    • (1999) J Lipid Res , vol.40 , pp. 648-653
    • Hosoai, H.1    Webb, N.R.2    Glick, J.M.3    Tietge, U.J.4    Purdom, M.S.5    De Beer, F.C.6
  • 27
    • 0019519109 scopus 로고
    • Aggravation foudroyante d'amylose rénale après chirurgie. Trois observations
    • Jacquot C, D'Auzac C, Loirat P, Bariety J. Aggravation foudroyante d'amylose rénale après chirurgie. Trois observations. Nouv Presse Méd 1981 ; 10 : 3389-95.
    • (1981) Nouv Presse Méd , vol.10 , pp. 3389-3395
    • Jacquot, C.1    D'Auzac, C.2    Loirat, P.3    Bariety, J.4
  • 28
    • 0029812540 scopus 로고    scopus 로고
    • Increased circulation serum amyloid A protein derivatives in rheumatoid arthritis patients with secondary amyloidosis
    • Migita K, Eguchi K, Tsukada T, Kawabe Y, Takashima H, Mine M, et al. Increased circulation serum amyloid A protein derivatives in rheumatoid arthritis patients with secondary amyloidosis. Lab Invest 1996 ; 75 : 371-5.
    • (1996) Lab Invest , vol.75 , pp. 371-375
    • Migita, K.1    Eguchi, K.2    Tsukada, T.3    Kawabe, Y.4    Takashima, H.5    Mine, M.6
  • 29
    • 0019996811 scopus 로고
    • Mechanism of reduced amyloid-A-degrading activity in serum of patients with secondary amyloidosis
    • Maury CPJ, Teppo AM. Mechanism of reduced amyloid-A-degrading activity in serum of patients with secondary amyloidosis. Lancet 1982 ; ii : 234-7.
    • (1982) Lancet , vol.2 , pp. 234-237
    • Maury, C.P.J.1    Teppo, A.M.2
  • 31
    • 0023511345 scopus 로고
    • Specific deposition of serum amyloid A protein 2 in the mouse
    • Shiroo M, Kawahara E, Nakanishi I, Migita S. Specific deposition of serum amyloid A protein 2 in the mouse. Scand J Immunol 1987 ; 26 : 709-16.
    • (1987) Scand J Immunol , vol.26 , pp. 709-716
    • Shiroo, M.1    Kawahara, E.2    Nakanishi, I.3    Migita, S.4
  • 32
    • 0030929756 scopus 로고    scopus 로고
    • Degradation of amyloid A precursor protein SAA by macrophage cell lines obtained from amyloid resistant and susceptible strains of mice
    • Ham D, Caouras V, Radzioch D, Gervais F. Degradation of amyloid A precursor protein SAA by macrophage cell lines obtained from amyloid resistant and susceptible strains of mice. Scand J Immunol 1997 ; 45 : 354-60.
    • (1997) Scand J Immunol , vol.45 , pp. 354-360
    • Ham, D.1    Caouras, V.2    Radzioch, D.3    Gervais, F.4
  • 33
    • 0020332411 scopus 로고
    • The role of interleukin 1 in acute phase serum amyloid A (SAA) and serum amyloid P (SAP) biosynthetis
    • Sipe JD, Vogel SN, Sztein MB, Skinner M, Cohen AS. The role of interleukin 1 in acute phase serum amyloid A (SAA) and serum amyloid P (SAP) biosynthetis. Ann N Y Acad Sci 1982 ; 389 : 137-49.
    • (1982) Ann N Y Acad Sci , vol.389 , pp. 137-149
    • Sipe, J.D.1    Vogel, S.N.2    Sztein, M.B.3    Skinner, M.4    Cohen, A.S.5
  • 34
    • 0023779948 scopus 로고
    • The effect of interleukin-1, interleukin-6 and its interelationship on the synthetis of serum amyloid A and C-reactive protein in primary cultures of adult human hepatocytes
    • Moshage HJ, Roelofs HMJ, Van Pelt JF, Hazenberg BPC, Van Leeuwen MA, Limburg PC, et al. The effect of interleukin-1, interleukin-6 and its interelationship on the synthetis of serum amyloid A and C-reactive protein in primary cultures of adult human hepatocytes. Biochem Biophys Res Commun 1988 ; 155 : 112-7.
    • (1988) Biochem Biophys Res Commun , vol.155 , pp. 112-117
    • Moshage, H.J.1    Roelofs, H.M.J.2    Van Pelt, J.F.3    Hazenberg, B.P.C.4    Van Leeuwen, M.A.5    Limburg, P.C.6
  • 35
    • 0029100030 scopus 로고
    • A novel biologic function of serum amyloid A. Induction of lymphocyte migration and adhesion
    • Xu L, Badolato R, Murphy WJ, Longo DL, Anver M, Hale S, et al. A novel biologic function of serum amyloid A. Induction of lymphocyte migration and adhesion. J Immunol 1995 ; 155 : 1184-90.
    • (1995) J Immunol , vol.155 , pp. 1184-1190
    • Xu, L.1    Badolato, R.2    Murphy, W.J.3    Longo, D.L.4    Anver, M.5    Hale, S.6
  • 36
    • 0020045084 scopus 로고
    • SAA suppression of immune response in vitro: Evidence for an effect on T cell-macrophage interaction
    • Aldo-Benson MA, Benson MD. SAA suppression of immune response in vitro: Evidence for an effect on T cell-macrophage interaction. J Immunol 1982 ; 128 : 2390-2.
    • (1982) J Immunol , vol.128 , pp. 2390-2392
    • Aldo-Benson, M.A.1    Benson, M.D.2
  • 37
    • 0029910905 scopus 로고    scopus 로고
    • Amino terminal region of acute phase, but not constitutive, serum amyloid A (apoSAA) specifically binds and transports cholesterol into aortic smooth muscle and HepG2 cells
    • Liang JS, Schreiber BM, Salmona M, Phillip G, Gonnerman WA, de Beer FC, et al. Amino terminal region of acute phase, but not constitutive, serum amyloid A (apoSAA) specifically binds and transports cholesterol into aortic smooth muscle and HepG2 cells. J Lipid Res 1996 ; 37 : 2109-16.
    • (1996) J Lipid Res , vol.37 , pp. 2109-2116
    • Liang, J.S.1    Schreiber, B.M.2    Salmona, M.3    Phillip, G.4    Gonnerman, W.A.5    De Beer, F.C.6
  • 38
    • 0002696182 scopus 로고
    • Amyloidosis
    • In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. New York: McGram-Hill
    • Benson MD, Wallace MR. Amyloidosis. In: Scriver CR, Beaudet AL, Sly WS, Valle D, eds. The Metabolic Basis of Inherited Disease, Ed 6, vol 2. New York: McGram-Hill; 1989. p. 2439.
    • (1989) The Metabolic Basis of Inherited Disease, Ed 6 , vol.2 , pp. 2439
    • Benson, M.D.1    Wallace, M.R.2
  • 39
    • 0020697241 scopus 로고
    • Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin
    • Pras M, Prelli F, Franklin EL, Frangione B. Primary structure of an amyloid prealbumin variant in familial polyneuropathy of Jewish origin. Proc Natl Acad Sci 1983 ; 80 : 539-42.
    • (1983) Proc Natl Acad Sci , vol.80 , pp. 539-542
    • Pras, M.1    Prelli, F.2    Franklin, E.L.3    Frangione, B.4
  • 40
    • 0021012829 scopus 로고
    • Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy
    • Tawara S, Nakazato M, Kangawa K, Matsuo H, Araki S. Identification of amyloid prealbumin variant in familial amyloidotic polyneuropathy (Japanese type). Biochem Biophys Res Commun 1983 ; 116 : 880-8.
    • (1983) Biochem Biophys Res Commun , vol.116 , pp. 880-888
    • Tawara, S.1    Nakazato, M.2    Kangawa, K.3    Matsuo, H.4    Araki, S.5
  • 41
    • 0003351753 scopus 로고
    • Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin
    • Dwulet FE, Benson MD. Primary structure of an amyloid prealbumin and its plasma precursor in a heredofamilial polyneuropathy of Swedish origin. Proc Natl Acad Sci 1984 ; 81 : 694-8.
    • (1984) Proc Natl Acad Sci , vol.81 , pp. 694-698
    • Dwulet, F.E.1    Benson, M.D.2
  • 42
    • 0021266985 scopus 로고
    • Amyloid fibril protein in familial amyloid polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin)
    • Saraiva MJM, Birken S, Costa PP, Goodman DS. Amyloid fibril protein in familial amyloid polyneuropathy, Portuguese type. Definition of molecular abnormality in transthyretin (prealbumin). J Clin Invest 1984 ; 74 : 104-19.
    • (1984) J Clin Invest , vol.74 , pp. 104-119
    • Saraiva, M.J.M.1    Birken, S.2    Costa, P.P.3    Goodman, D.S.4
  • 43
    • 0022472793 scopus 로고
    • Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis
    • Wallace MR, Dwulet FE, Conneally PM, Benson MD. Biochemical and molecular genetic characterization of a new variant prealbumin associated with hereditary amyloidosis. J Clin Invest 1986 ; 78 : 6-12.
    • (1986) J Clin Invest , vol.78 , pp. 6-12
    • Wallace, M.R.1    Dwulet, F.E.2    Conneally, P.M.3    Benson, M.D.4
  • 44
    • 0023019098 scopus 로고
    • Characterization of transthyretin (prealbumin) variant associated with familial amyloid polyneuropathy type II
    • Indiana/Swiss
    • Dwulet FE, Benson MD. Characterization of transthyretin (prealbumin) variant associated with familial amyloid polyneuropathy type II (Indiana/Swiss). J Clin Invest 1986 ; 78 : 880-6.
    • (1986) J Clin Invest , vol.78 , pp. 880-886
    • Dwulet, F.E.1    Benson, M.D.2
  • 45
    • 0022760013 scopus 로고
    • Structure of the mutant prealbumin gene responsible for familial amyloidotic polyneuropathy
    • Yoshioka K, Sasaki H, Yoshioka N, Furuya H, Harada T, Kito S, et al. Structure of the mutant prealbumin gene responsible for familial amyloidotic polyneuropathy. Mol Biol Med 1986 ; 3 : 319-28.
    • (1986) Mol Biol Med , vol.3 , pp. 319-328
    • Yoshioka, K.1    Sasaki, H.2    Yoshioka, N.3    Furuya, H.4    Harada, T.5    Kito, S.6
  • 46
    • 0030830019 scopus 로고    scopus 로고
    • Transtyretin quaternary ane tertiary structural changes facilitate misassembly into amyloid
    • Kelly JW, Colon W, Lai Z, Lashuel HA, McCulloch J, McCutchen SL, et al. Transtyretin quaternary ane tertiary structural changes facilitate misassembly into amyloid. Adv Protein Chem 1997 ; 50 : 161-81.
    • (1997) Adv Protein Chem , vol.50 , pp. 161-181
    • Kelly, J.W.1    Colon, W.2    Lai, Z.3    Lashuel, H.A.4    McCulloch, J.5    McCutchen, S.L.6
  • 49
    • 0021256895 scopus 로고
    • Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein
    • Glenner GG, Wong CW. Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984 ; 120 : 885-90.
    • (1984) Biochem Biophys Res Commun , vol.120 , pp. 885-890
    • Glenner, G.G.1    Wong, C.W.2
  • 50
    • 0021207461 scopus 로고
    • Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein
    • Glenner GG, Wong CW. Alzheimer's disease and Down's syndrome: Sharing of a unique cerebrovascular amyloid fibril protein. Biochem Biophys Res Commun 1984 ; 122 : 1131-5.
    • (1984) Biochem Biophys Res Commun , vol.122 , pp. 1131-1135
    • Glenner, G.G.1    Wong, C.W.2
  • 52
    • 0023105114 scopus 로고
    • The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor
    • Kang J, Lemaire H-G, Unterbeck A, Salbaum JM, Masters CL, Grzeschik KH, et al. The precursor of Alzheimer's disease amyloid A4 protein resembles a cell-surface receptor. Nature 1987 ; 325 : 733-6.
    • (1987) Nature , vol.325 , pp. 733-736
    • Kang, J.1    Lemaire, H.-G.2    Unterbeck, A.3    Salbaum, J.M.4    Masters, C.L.5    Grzeschik, K.H.6
  • 53
    • 0023132387 scopus 로고
    • Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease
    • Goldgaber D, Lerman MI, McBride OW, Saffiotti U, Gajdusek DC. Characterization and chromosomal localization of a cDNA encoding brain amyloid of Alzheimer's disease. Science 1987 ; 234 : 877-80.
    • (1987) Science , vol.234 , pp. 877-880
    • Goldgaber, D.1    Lerman, M.I.2    McBride, O.W.3    Saffiotti, U.4    Gajdusek, D.C.5
  • 54
    • 0023189941 scopus 로고
    • The genetic defect in familial Alzheimer's disease is not tightly linked to the amyloid β-protein gene
    • Tanzi RE, St George-Hyslop PH, Haines JL, Polinsky RJ, Nee L, Foncin JF, et al. The genetic defect in familial Alzheimer's disease is not tightly linked to the amyloid β-protein gene. Nature 1987 ; 329 : 156-7.
    • (1987) Nature , vol.329 , pp. 156-157
    • Tanzi, R.E.1    St. George-Hyslop, P.H.2    Haines, J.L.3    Polinsky, R.J.4    Nee, L.5    Foncin, J.F.6
  • 55
    • 0023118252 scopus 로고
    • Conservation of brain amyloid proteins in aged mammals and humans with Alzheimer's disease
    • Selkoe DJ, Bell DS, Podlisny MB, Price DL, Cork LC. Conservation of brain amyloid proteins in aged mammals and humans with Alzheimer's disease. Science 1987 ; 235 : 873-6.
    • (1987) Science , vol.235 , pp. 873-876
    • Selkoe, D.J.1    Bell, D.S.2    Podlisny, M.B.3    Price, D.L.4    Cork, L.C.5
  • 57
    • 0030778933 scopus 로고    scopus 로고
    • The role of amyloid in the pathogenesis of Alzheimer's disease
    • Verbbek MM, Ruiter DJ, de Maal RM. The role of amyloid in the pathogenesis of Alzheimer's disease. Biol Chem 1997 ; 378 : 937-50.
    • (1997) Biol Chem , vol.378 , pp. 937-950
    • Verbbek, M.M.1    Ruiter, D.J.2    De Maal, R.M.3
  • 58
    • 0027447286 scopus 로고
    • Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state
    • Pike CJ, Burdick D, Walencewicz AJ, Glabe CG, Cotman CW. Neurodegeneration induced by β-amyloid peptides in vitro: The role of peptide assembly state. J Neurosci 1993 ; 13 : 1676-87.
    • (1993) J Neurosci , vol.13 , pp. 1676-1687
    • Pike, C.J.1    Burdick, D.2    Walencewicz, A.J.3    Glabe, C.G.4    Cotman, C.W.5
  • 59
    • 0031226585 scopus 로고    scopus 로고
    • New insights into the neuropathology and cell biology of Alzheimer's disease
    • Weldon DT, Maggio JE, Mantyh PW. New insights into the neuropathology and cell biology of Alzheimer's disease. Geriatrics 1997 ; 52 : S13-6.
    • (1997) Geriatrics , vol.52
    • Weldon, D.T.1    Maggio, J.E.2    Mantyh, P.W.3
  • 60
    • 0023870043 scopus 로고
    • A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors
    • Ponte P, Gonzalez-DeWhitt P, Miller J, Hsu D, Greenberg B. A new A4 amyloid mRNA contains a domain homologous to serine proteinase inhibitors. Nature (London) 1988 ; 331 : 525-7.
    • (1988) Nature (London) , vol.331 , pp. 525-527
    • Ponte, P.1    Gonzalez-DeWhitt, P.2    Miller, J.3    Hsu, D.4    Greenberg, B.5
  • 61
    • 0023838532 scopus 로고
    • 1-antichymotrypsin in the brain amyloid deposits of Alzeimer's disease
    • 1-antichymotrypsin in the brain amyloid deposits of Alzeimer's disease. Cell 1988 ; 52 : 487-501.
    • (1988) Cell , vol.52 , pp. 487-501
    • Abraham, C.R.1    Selkoe, D.J.2    Potter, H.3
  • 62
    • 0022435132 scopus 로고
    • Image reconstruction of the Alzheimer paired helical filament
    • Crowther RA, Wischik CM. Image reconstruction of the Alzheimer paired helical filament. Embo J 1985 ; 4 : 3661-5.
    • (1985) Embo J , vol.4 , pp. 3661-3665
    • Crowther, R.A.1    Wischik, C.M.2
  • 63
    • 0021796959 scopus 로고
    • Subunit structure of paired helical filaments in Alzeimer's disease
    • Wischik CM, Crowther RA, Stewart M, Roth M. Subunit structure of paired helical filaments in Alzeimer's disease. J Cell Biol 1985 ; 100 : 1905-12.
    • (1985) J Cell Biol , vol.100 , pp. 1905-1912
    • Wischik, C.M.1    Crowther, R.A.2    Stewart, M.3    Roth, M.4
  • 64
    • 0022341791 scopus 로고
    • Amyloidosis of a possible new type in patients receiving long-term hemodialysis
    • Morita T, Suzuki M, Kamimura A, Hirasawa Y. Amyloidosis of a possible new type in patients receiving long-term hemodialysis. Arch Pathol Lab Med 1985 ; 109 : 1029-32.
    • (1985) Arch Pathol Lab Med , vol.109 , pp. 1029-1032
    • Morita, T.1    Suzuki, M.2    Kamimura, A.3    Hirasawa, Y.4
  • 69
    • 0024448641 scopus 로고
    • Lysine-specific cleavage of β2M in amyloid deposits associated with hemodialysis
    • Linke RP, Hampl H, Lobeck H, Ritz E, Bommer J, Waldherr R, et al. Lysine-specific cleavage of β2M in amyloid deposits associated with hemodialysis. Kidney Int 1989 ; 36 : 675-81.
    • (1989) Kidney Int , vol.36 , pp. 675-681
    • Linke, R.P.1    Hampl, H.2    Lobeck, H.3    Ritz, E.4    Bommer, J.5    Waldherr, R.6
  • 70
    • 0024595476 scopus 로고
    • Amyloid syndromes associated with hemodialysis
    • Kleinman KS, Coburn JW. Amyloid syndromes associated with hemodialysis. Kidney Int 1989 ; 35 : 567-75.
    • (1989) Kidney Int , vol.35 , pp. 567-575
    • Kleinman, K.S.1    Coburn, J.W.2
  • 71
    • 0022545359 scopus 로고
    • Haemodialysis versus CAPD: Equal predisposition to amyloidosis?
    • Ballardie FW, Kerr DNS, Tennent G, Pepys MB. Haemodialysis versus CAPD: Equal predisposition to amyloidosis? Lancet 1986 ; i : 795-6.
    • (1986) Lancet , vol.1 , pp. 795-796
    • Ballardie, F.W.1    Kerr, D.N.S.2    Tennent, G.3    Pepys, M.B.4
  • 73
    • 0023628870 scopus 로고
    • Amyloid deposition in systemic organs in long-term hemodialysis patients
    • Ogawa H, Saito A, Hirabayashi N, Hara K. Amyloid deposition in systemic organs in long-term hemodialysis patients. Clin Nephrol 1987 ; 28 : 199-204.
    • (1987) Clin Nephrol , vol.28 , pp. 199-204
    • Ogawa, H.1    Saito, A.2    Hirabayashi, N.3    Hara, K.4
  • 74
    • 0013919085 scopus 로고
    • Mucopolysaccharides of whole human spleens in generalized amyloidosis
    • Bitter T, Muir H. Mucopolysaccharides of whole human spleens in generalized amyloidosis. J Clin Invest 1966 ; 45 : 963-75.
    • (1966) J Clin Invest , vol.45 , pp. 963-975
    • Bitter, T.1    Muir, H.2
  • 75
    • 0023128689 scopus 로고
    • Sulfated glycosaminoglycans: A common constituent of all amyloids?
    • Snow AD, Willmer J, Kisilevsky R. Sulfated glycosaminoglycans: A common constituent of all amyloids? Lab Invest 1987 ; 56 : 120-3.
    • (1987) Lab Invest , vol.56 , pp. 120-123
    • Snow, A.D.1    Willmer, J.2    Kisilevsky, R.3
  • 76
    • 0014428207 scopus 로고
    • Association of acid mucopolysaccharides with isolated amyloid fibrils
    • Pennock CA. Association of acid mucopolysaccharides with isolated amyloid fibrils. Nature 1968 ; 217 : 753-4.
    • (1968) Nature , vol.217 , pp. 753-754
    • Pennock, C.A.1
  • 77
    • 4243236803 scopus 로고
    • An intimate ultrastructural association between sulphated proteoglycans and AA amyloid fibrils
    • Snow AD, Kisilevsky R. An intimate ultrastructural association between sulphated proteoglycans and AA amyloid fibrils. Lab Invest 1987 ; 56 : 75A.
    • (1987) Lab Invest , vol.56
    • Snow, A.D.1    Kisilevsky, R.2
  • 78
    • 0022004144 scopus 로고
    • Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis: A histochemical study
    • Snow AD, Kisilevsky R. Temporal relationship between glycosaminoglycan accumulation and amyloid deposition during experimental amyloidosis: A histochemical study. Lab Invest 1985 ; 53 : 37-44.
    • (1985) Lab Invest , vol.53 , pp. 37-44
    • Snow, A.D.1    Kisilevsky, R.2
  • 79
    • 0033548474 scopus 로고    scopus 로고
    • The heparin/heparan sulfate-binding site on apo-serum amyloid A. Implications for the therapeutic intervention of amyloidosis
    • Ancsin JB, Kisilevsky R. The heparin/heparan sulfate-binding site on apo-serum amyloid A. Implications for the therapeutic intervention of amyloidosis. J Biol Chem 1999 ; 274 : 7172-81.
    • (1999) J Biol Chem , vol.274 , pp. 7172-7181
    • Ancsin, J.B.1    Kisilevsky, R.2
  • 80
    • 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 : 1681-7.
    • (1999) J Neurochem , vol.72 , pp. 1681-1687
    • Castillo, G.M.1    Lukito, W.2    Wight, T.N.3    Snow, A.D.4
  • 81
    • 0027407565 scopus 로고
    • Apolipoprotein E: High-avidity binding to β-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease
    • Strittmatter WJ, Saunders AM, Schmechel D, Pericak-Vance M, Enghild J, Salvesen G, et al. Apolipoprotein E: High-avidity binding to β-amyloid and increased frequency of type 4 allele in late-onset familial Alzheimer disease. Proc Natl Acad Sci USA 1993 ; 90 : 177-81.
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 177-181
    • Strittmatter, W.J.1    Saunders, A.M.2    Schmechel, D.3    Pericak-Vance, M.4    Enghild, J.5    Salvesen, G.6
  • 82
    • 0028178047 scopus 로고
    • Apolipoprotein E, E4 allele as a major risk factor for sporadic early and late-onset forms of Alzheimer's disease: Analysis of the 19q13.2 chromosomal region
    • Chartier-Harlin MC, Parfitt M, Legrain S, Pérez-Tur J, Brousseau T, Evans A, et al. Apolipoprotein E, E4 allele as a major risk factor for sporadic early and late-onset forms of Alzheimer's disease: Analysis of the 19q13.2 chromosomal region. Hum Mol Genet 1994 ; 3 : 569-74.
    • (1994) Hum Mol Genet , vol.3 , pp. 569-574
    • Chartier-Harlin, M.C.1    Parfitt, M.2    Legrain, S.3    Pérez-Tur, J.4    Brousseau, T.5    Evans, A.6
  • 84
    • 0029151238 scopus 로고
    • Apolipoprotein E carboxyl-terminal fragments are complexed to amyloids A and L. Implications for amyloidogenesis and Alzheimer's disease
    • Castano EM, Prelli F, Pras M, Frangione B. Apolipoprotein E carboxyl-terminal fragments are complexed to amyloids A and L. Implications for amyloidogenesis and Alzheimer's disease. J Biol Chem 1995 ; 270 : 17610-5.
    • (1995) J Biol Chem , vol.270 , pp. 17610-17615
    • Castano, E.M.1    Prelli, F.2    Pras, M.3    Frangione, B.4
  • 86
    • 0020478765 scopus 로고
    • Abnormal lipoprotein receptor-binding activity of the human E apoprotein due to Cysteine-Arginine interchange at a single site
    • Weisgraber KH, Innerarity TL, Mahley RW. Abnormal lipoprotein receptor-binding activity of the human E apoprotein due to Cysteine-Arginine interchange at a single site. J Biol Chem 1982 ; 257 : 2518-21.
    • (1982) J Biol Chem , vol.257 , pp. 2518-2521
    • Weisgraber, K.H.1    Innerarity, T.L.2    Mahley, R.W.3
  • 87
    • 0032891220 scopus 로고    scopus 로고
    • Cerebral amyloid angiopathy in Alzheimer disease associated with apolipoprotein E4 and cortical neuron loss
    • Zarow C, Zaias B, Lyness SA, Chui H. Cerebral amyloid angiopathy in Alzheimer disease associated with apolipoprotein E4 and cortical neuron loss. Alzheimer Dis Assoc Disord 1999 ; 13 : 1-8.
    • (1999) Alzheimer Dis Assoc Disord , vol.13 , pp. 1-8
    • Zarow, C.1    Zaias, B.2    Lyness, S.A.3    Chui, H.4
  • 89
    • 0020971452 scopus 로고
    • Acute phase proteins with special reference to C-reactive protein and related proteins (pentraxins) and serum amyloid A protein
    • Pepys MB, Baltz ML. Acute phase proteins with special reference to C-reactive protein and related proteins (pentraxins) and serum amyloid A protein. Adv Immunol 1983 ; 34 : 141-212.
    • (1983) Adv Immunol , vol.34 , pp. 141-212
    • Pepys, M.B.1    Baltz, M.L.2
  • 91
    • 0022397513 scopus 로고
    • The primary structure of human tissue amyloid P component from a patient with primary idiopathie amyloidosis
    • Prelli F, Pras M, Frangione B. The primary structure of human tissue amyloid P component from a patient with primary idiopathie amyloidosis. J Biol Chem 1985 ; 260 : 12895-8.
    • (1985) J Biol Chem , vol.260 , pp. 12895-12898
    • Prelli, F.1    Pras, M.2    Frangione, B.3
  • 92
    • 0018169127 scopus 로고
    • Human plasma P component: Isolation and characterization
    • Thompson AR, Enfield DL. Human plasma P component: Isolation and characterization. Biochemistry 1978 ; 17 : 4304-11.
    • (1978) Biochemistry , vol.17 , pp. 4304-4311
    • Thompson, A.R.1    Enfield, D.L.2
  • 94
    • 0021365253 scopus 로고
    • Binding specificity of serum amyloid P component for the pyruvate acetal of galactose
    • Hind CRK, Collins PM, Renn D, Cook RB, Caspi D, Baltz ML, et al. Binding specificity of serum amyloid P component for the pyruvate acetal of galactose. J Exp Med 1984 ; 59 : 1058-69.
    • (1984) J Exp Med , vol.59 , pp. 1058-1069
    • Hind, C.R.K.1    Collins, P.M.2    Renn, D.3    Cook, R.B.4    Caspi, D.5    Baltz, M.L.6
  • 97
    • 0017872572 scopus 로고
    • Analogues in other mammals and in fish of human plasma proteins, C-reactive protein and amyloid P-component
    • Pepys MB, Dash AC, Fletcher TC, Richardson N, Munn EA, Feinstein A. Analogues in other mammals and in fish of human plasma proteins, C-reactive protein and amyloid P-component. Nature (London) 1978 ; 273 : 168-70.
    • (1978) Nature (London) , vol.273 , pp. 168-170
    • Pepys, M.B.1    Dash, A.C.2    Fletcher, T.C.3    Richardson, N.4    Munn, E.A.5    Feinstein, A.6
  • 98
    • 0023617937 scopus 로고
    • Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum
    • Pepys MB, Butler PJG. Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum. Biochem Biophys Res Commun 1987 ; 148 : 308-13.
    • (1987) Biochem Biophys Res Commun , vol.148 , pp. 308-313
    • Pepys, M.B.1    Butler, P.J.G.2
  • 99
    • 0021674860 scopus 로고
    • Appearance of serum amyloid protein in high-density lipoproteins of rabbits subjected to relatively mild stimuli
    • Moon EA, MacKinnon AM, Barter PJ. Appearance of serum amyloid protein in high-density lipoproteins of rabbits subjected to relatively mild stimuli. Biochim Biophys Acta 1984 ; 796 : 354-8.
    • (1984) Biochim Biophys Acta , vol.796 , pp. 354-358
    • Moon, E.A.1    MacKinnon, A.M.2    Barter, P.J.3
  • 101
    • 23444442507 scopus 로고
    • Interaction between serum amyloid P component and C4b-binding protein associated with inhibition of factor I-mediated C4b degradation
    • Garcia de Frutos P, Dahlback B. Interaction between serum amyloid P component and C4b-binding protein associated with inhibition of factor I-mediated C4b degradation. J Immunol 1994 ; 152 : 2430-7.
    • (1994) J Immunol , vol.152 , pp. 2430-2437
    • De Garcia Frutos, P.1    Dahlback, B.2
  • 103
    • 0018425762 scopus 로고
    • Serum amyloid P-component is an acute phase reactant in the mouse
    • Pepys MB, Baltz M, Gomer K, Davies AJS, Doenhoff M. Serum amyloid P-component is an acute phase reactant in the mouse. Nature 1979 ; 278 : 259-62.
    • (1979) Nature , vol.278 , pp. 259-262
    • Pepys, M.B.1    Baltz, M.2    Gomer, K.3    Davies, A.J.S.4    Doenhoff, M.5
  • 104
    • 0018941792 scopus 로고
    • Amyloid P-component in mice injected with casein identification in amyloid deposits and in the cytoplasm of hepatocytes
    • Baltz ML, Dyck RF, Pepys MB. Amyloid P-component in mice injected with casein identification in amyloid deposits and in the cytoplasm of hepatocytes. Immunology 1980 ; 41 : 59-66.
    • (1980) Immunology , vol.41 , pp. 59-66
    • Baltz, M.L.1    Dyck, R.F.2    Pepys, M.B.3
  • 105
  • 106
    • 0023262545 scopus 로고
    • A genetic marker for systemic amyloidosis in juvenile arthritis
    • Woo P, O'Brien J, Robson M, Ansel B. A genetic marker for systemic amyloidosis in juvenile arthritis. Lancet 1987 ; ii : 767-9.
    • (1987) Lancet , vol.2 , pp. 767-769
    • Woo, P.1    O'Brien, J.2    Robson, M.3    Ansel, B.4
  • 107
    • 0025752708 scopus 로고
    • Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis
    • Hawkins PN, Tennent GA, Woo P, Pepys MB. Studies in vivo and in vitro of serum amyloid P component in normals and in a patient with AA amyloidosis. Clin Exp Immunol 1991 ; 84 : 308-16.
    • (1991) Clin Exp Immunol , vol.84 , pp. 308-316
    • Hawkins, P.N.1    Tennent, G.A.2    Woo, P.3    Pepys, M.B.4
  • 109
    • 0019199344 scopus 로고
    • Amyloid P-component is a constitutent of normal human glomerular basement membrane
    • Dyck RF, Lockwood M, Kershaw M, Mc Hugh N, Duance VC, Baltz ML, et al. Amyloid P-component is a constitutent of normal human glomerular basement membrane. J Exp Med 1980 ; 152 : 1162-74.
    • (1980) J Exp Med , vol.152 , pp. 1162-1174
    • Dyck, R.F.1    Lockwood, M.2    Kershaw, M.3    Mc Hugh, N.4    Duance, V.C.5    Baltz, M.L.6
  • 110
    • 0019832756 scopus 로고
    • Amyloid P-component is located on elastic fibre microfibrils of normal human tissues
    • Breathnach SM, Melrose SM, Bhogal B, de Beer FC, Dyck RF, Tennent G, et al. Amyloid P-component is located on elastic fibre microfibrils of normal human tissues. Nature 1981 ; 293 : 652-4.
    • (1981) Nature , vol.293 , pp. 652-654
    • Breathnach, S.M.1    Melrose, S.M.2    Bhogal, B.3    De Beer, F.C.4    Dyck, R.F.5    Tennent, G.6
  • 111
    • 0021210903 scopus 로고
    • Specific chemical dissociation of fibrillar and non-fibrillar components of amyloid deposits
    • Hind CRK, Collins PM, Caspi D, Baltz ML, Pepys MB. Specific chemical dissociation of fibrillar and non-fibrillar components of amyloid deposits. Lancet 1984 ; ii : 376-8.
    • (1984) Lancet , vol.2 , pp. 376-378
    • Hind, C.R.K.1    Collins, P.M.2    Caspi, D.3    Baltz, M.L.4    Pepys, M.B.5
  • 113
    • 0025694826 scopus 로고
    • Metabolic studies of radioiodinated serum amyloid P component in normal subjects and patients with systemic amyloidosis
    • Hawkins PN, Wootton R, Pepys MB. Metabolic studies of radioiodinated serum amyloid P component in normal subjects and patients with systemic amyloidosis. J Clin Invest 1990 ; 86 : 1862-9.
    • (1990) J Clin Invest , vol.86 , pp. 1862-1869
    • Hawkins, P.N.1    Wootton, R.2    Pepys, M.B.3
  • 114
    • 0018717327 scopus 로고
    • Serum amyloid P-component levels in amyloidosis, connective tissue diseases, infections and malignancy as compared to normal serum
    • Skinner M, Vaitukaitis JL, Cohen AS, Benson MD. Serum amyloid P-component levels in amyloidosis, connective tissue diseases, infections and malignancy as compared to normal serum. J Lab Clin Med 1979 ; 97 : 633-8.
    • (1979) J Lab Clin Med , vol.97 , pp. 633-638
    • Skinner, M.1    Vaitukaitis, J.L.2    Cohen, A.S.3    Benson, M.D.4
  • 116
    • 0028246095 scopus 로고
    • Concentration of serum amyloid P component in the CSF as a possible marker of cerebral amyloid deposits in Alzheimer's disease
    • Hawkins PN, Rossor MN, Gallimore JR, Miller B, Moore EG, Pepys MB. Concentration of serum amyloid P component in the CSF as a possible marker of cerebral amyloid deposits in Alzheimer's disease. Biochem Biophys Res Commun 1994 ; 201 : 722-6.
    • (1994) Biochem Biophys Res Commun , vol.201 , pp. 722-726
    • Hawkins, P.N.1    Rossor, M.N.2    Gallimore, J.R.3    Miller, B.4    Moore, E.G.5    Pepys, M.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.