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Volumn 155, Issue 1, 1999, Pages 123-133

A cell culture system for the study of amyloid pathogenesis: Amyloid formation by peritoneal macrophages cultured with recombinant serum amyloid A

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID; AMYLOID A PROTEIN; RECOMBINANT PROTEIN;

EID: 0033021099     PISSN: 00029440     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0002-9440(10)65107-3     Document Type: Article
Times cited : (66)

References (55)
  • 1
    • 0000375747 scopus 로고
    • The major proteins of human and monkey amyloid substance: Common properties including unusual N-terminal amino acid sequences
    • Benditt EP, Eriksen N, Hermodsen MA, Ericsson LH: The major proteins of human and monkey amyloid substance: common properties including unusual N-terminal amino acid sequences. FEBS Lett 1971, 19:169-173
    • (1971) FEBS Lett , vol.19 , pp. 169-173
    • Benditt, E.P.1    Eriksen, N.2    Hermodsen, M.A.3    Ericsson, L.H.4
  • 2
    • 0015419122 scopus 로고
    • The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils
    • Levin M, Franklin EC, Frangione B, Pras M: The amino acid sequence of a major nonimmunoglobulin component of some amyloid fibrils. J Clin Invest 1972, 51:2773-2776
    • (1972) J Clin Invest , vol.51 , pp. 2773-2776
    • Levin, M.1    Franklin, E.C.2    Frangione, B.3    Pras, M.4
  • 3
    • 0021909988 scopus 로고
    • Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo
    • Husebekk A, Skogen B, Husby G, Marhaug G: Transformation of amyloid precursor SAA to protein AA and incorporation in amyloid fibrils in vivo. Scand J Immunol 1985, 21:283-287
    • (1985) Scand J Immunol , vol.21 , pp. 283-287
    • Husebekk, A.1    Skogen, B.2    Husby, G.3    Marhaug, G.4
  • 5
    • 0018889041 scopus 로고
    • Synthesis and secretion of serum amyloid A (SAA) by hepatocytes in mice treated with casein
    • Benson MD, Kleiner E: Synthesis and secretion of serum amyloid A (SAA) by hepatocytes in mice treated with casein. J Immunol 1980, 124:495-499
    • (1980) J Immunol , vol.124 , pp. 495-499
    • Benson, M.D.1    Kleiner, E.2
  • 6
    • 0020457016 scopus 로고
    • Secretion of serum amyloid protein and assembly of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture
    • Hoffman JS, Benditt EP: Secretion of serum amyloid protein and assembly of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture. J Biol Chem 1982, 257:10518-10522
    • (1982) J Biol Chem , vol.257 , pp. 10518-10522
    • Hoffman, J.S.1    Benditt, E.P.2
  • 7
    • 0345299157 scopus 로고
    • Amyloid protein SAA is associated with high density lipoprotein from human serum
    • Benditt EP, Eriksen N: Amyloid protein SAA is associated with high density lipoprotein from human serum. Proc Natl Acad Sci USA 1977, 74:4025-4028
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 4025-4028
    • Benditt, E.P.1    Eriksen, N.2
  • 8
    • 0018187709 scopus 로고
    • Changes in human serum amyloid A and C-reactive protein following etiocholanlolone-induced inflammation
    • McAdam KPW, Elin RJ, Sipe JD, Wolff SM: Changes in human serum amyloid A and C-reactive protein following etiocholanlolone-induced inflammation. J Clin Invest 1978, 61:390-394
    • (1978) J Clin Invest , vol.61 , pp. 390-394
    • McAdam, K.P.W.1    Elin, R.J.2    Sipe, J.D.3    Wolff, S.M.4
  • 9
    • 0022966771 scopus 로고
    • Transcriptional regulation of serum amyloid A gene expression
    • Lowell CA, Stearman RS, Morrow JF: Transcriptional regulation of serum amyloid A gene expression. J Biol Chem 1986, 261 8453-8461
    • (1986) J Biol Chem , vol.261 , pp. 8453-8461
    • Lowell, C.A.1    Stearman, R.S.2    Morrow, J.F.3
  • 11
    • 0016287131 scopus 로고
    • Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods
    • Cooper JH: Selective amyloid staining as a function of amyloid composition and structure. Histochemical analysis of the alkaline Congo red, standardized toluidine blue, and iodine methods. Lab Invest 1974, 31:232-238
    • (1974) Lab Invest , vol.31 , pp. 232-238
    • Cooper, J.H.1
  • 12
    • 0019153066 scopus 로고
    • Amyloid deposits and amyloidois. The β-fibrilloses
    • Glenner GG: Amyloid deposits and amyloidois. The β-fibrilloses. N Engl J Med 1980, 302:1283-1292, 1333-1343
    • (1980) N Engl J Med , vol.302 , pp. 1283-1292
    • Glenner, G.G.1
  • 13
    • 0021883883 scopus 로고
    • Amyloidosis and rheumatoid arthritis
    • Husby G: Amyloidosis and rheumatoid arthritis. Clin Exp Rheumatol 1985, 3:173-180
    • (1985) Clin Exp Rheumatol , vol.3 , pp. 173-180
    • Husby, G.1
  • 14
    • 0001999309 scopus 로고
    • Amyloidosis
    • Edited by CR Scriver, AL Beaudet, WS Sly, D Valle. New York, McGraw-Hill
    • Benson MD: Amyloidosis. The Metabolic and Molecular Bases of Inherited Disease, ed 7. Edited by CR Scriver, AL Beaudet, WS Sly, D Valle. New York, McGraw-Hill, 1995, pp 4159-4191
    • (1995) The Metabolic and Molecular Bases of Inherited Disease, Ed 7 , pp. 4159-4191
    • Benson, M.D.1
  • 15
    • 0017411543 scopus 로고
    • Murine amyloid protein AA in casein-induced experimental amyloidosis
    • Skinner M, Shirahama JT, Benson MD, Cohen AS: Murine amyloid protein AA in casein-induced experimental amyloidosis. Lab Invest 1977, 36:420-427
    • (1977) Lab Invest , vol.36 , pp. 420-427
    • Skinner, M.1    Shirahama, J.T.2    Benson, M.D.3    Cohen, A.S.4
  • 16
    • 0018308853 scopus 로고
    • The effect of a liver protein synthesis inhibitor on plasma SAA levels in a model of accelerated amyloid deposition
    • Kisilevsky R, Benson MD, Axelrad MA, Boudreau L: The effect of a liver protein synthesis inhibitor on plasma SAA levels in a model of accelerated amyloid deposition. Lab Invest 1979, 41:206-210
    • (1979) Lab Invest , vol.41 , pp. 206-210
    • Kisilevsky, R.1    Benson, M.D.2    Axelrad, M.A.3    Boudreau, L.4
  • 17
    • 0030221863 scopus 로고    scopus 로고
    • Animal model for the pathogenesis of reactive amyloidosis
    • Ali-Khan Z, Li W, Chan SL: Animal model for the pathogenesis of reactive amyloidosis. Parasitol Today 1996, 12:297-302
    • (1996) Parasitol Today , vol.12 , pp. 297-302
    • Ali-Khan, Z.1    Li, W.2    Chan, S.L.3
  • 20
    • 0344088095 scopus 로고
    • Complete primary structures of two major murine serum amyloid A proteins deduced from cDNA sequences
    • Yamamoto K-I, Migita S: Complete primary structures of two major murine serum amyloid A proteins deduced from cDNA sequences. Proc Natl Acad Sci USA 1985, 82:2915-2919
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2915-2919
    • Yamamoto, K.-I.1    Migita, S.2
  • 21
    • 0023868491 scopus 로고
    • Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual
    • Dwulet FE, Wallace DK, Benson MD: Amino acid structures of multiple forms of amyloid-related serum protein SAA from a single individual. Biochemistry 1988, 27:1677-1682
    • (1988) Biochemistry , vol.27 , pp. 1677-1682
    • Dwulet, F.E.1    Wallace, D.K.2    Benson, M.D.3
  • 22
    • 0024346219 scopus 로고
    • The primary structure of equine serum amyloid A (SAA) protein
    • Sletten K, Husebekk A, Husby G: The primary structure of equine serum amyloid A (SAA) protein. Scand J Immunol 1989, 30:117-122
    • (1989) Scand J Immunol , vol.30 , pp. 117-122
    • Sletten, K.1    Husebekk, A.2    Husby, G.3
  • 23
    • 0025357636 scopus 로고
    • Mink serum amyloid A protein. Expression and primary sequence based on cDNA sequences
    • Marhaug G, Husby G, Dowton SB: Mink serum amyloid A protein. Expression and primary sequence based on cDNA sequences. J Biol Chem 1990, 265:10049-10054
    • (1990) J Biol Chem , vol.265 , pp. 10049-10054
    • Marhaug, G.1    Husby, G.2    Dowton, S.B.3
  • 25
    • 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, 26:709-716
    • (1987) Scand J Immunol , vol.26 , pp. 709-716
    • Shiroo, M.1    Kawahara, E.2    Nakanishi, I.3    Migita, S.4
  • 28
    • 0017817736 scopus 로고
    • Biochemical evidence for the biphasic development of experimental amyloidosis
    • Sipe JD, McAdam KPWJ, Uchino F: Biochemical evidence for the biphasic development of experimental amyloidosis. Lab Invest 1978, 38:110-114
    • (1978) Lab Invest , vol.38 , pp. 110-114
    • Sipe, J.D.1    McAdam, K.P.W.J.2    Uchino, F.3
  • 31
  • 32
    • 0027959216 scopus 로고
    • 2-fibrils to AA-fibrils in amyloid fibrillogenesis: In vivo observations in murine spleen using anti-SAA and anti-AA antibodies
    • 2-fibrils to AA-fibrils in amyloid fibrillogenesis: in vivo observations in murine spleen using anti-SAA and anti-AA antibodies. J Pathol (Lond) 1994, 173:127-134
    • (1994) J Pathol (Lond) , vol.173 , pp. 127-134
    • Arai, K.1    Miura, K.2    Baba, S.3    Shirasawa, H.4
  • 36
    • 0031044289 scopus 로고    scopus 로고
    • Differential plasma clearance of murine acute phase serum amyloid A proteins SAA1 and SAA2
    • Kluve-Beckerman B, Yamada T, Hardwick J, Liepnieks JJ, Benson MD: Differential plasma clearance of murine acute phase serum amyloid A proteins SAA1 and SAA2. Biochem J 1997, 322:663-669
    • (1997) Biochem J , vol.322 , pp. 663-669
    • Kluve-Beckerman, B.1    Yamada, T.2    Hardwick, J.3    Liepnieks, J.J.4    Benson, M.D.5
  • 38
    • 0030989257 scopus 로고    scopus 로고
    • In situ trypan blue staining of monolayer cell cultures for permanent fixation and mounting
    • Perry SW, Epstein LG, Gelbard HA: In situ trypan blue staining of monolayer cell cultures for permanent fixation and mounting. BioTechniques 1997, 22:1020-1024
    • (1997) BioTechniques , vol.22 , pp. 1020-1024
    • Perry, S.W.1    Epstein, L.G.2    Gelbard, H.A.3
  • 39
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa
    • Schagger H, von Jagow G: Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range of 1 to 100 kDa. Anal Biochem 1987, 166:368-379
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schagger, H.1    Von Jagow, G.2
  • 40
    • 0027422071 scopus 로고
    • Recombinant murine serum amyloid A from baculovirus-infected insect cells: Purification and characterization
    • Kluve-Beckerman B, Song M, Benson MD, Liepnieks, JJ: Recombinant murine serum amyloid A from baculovirus-infected insect cells: purification and characterization. Biochim Biophys Acta 1993, 1182: 303-310
    • (1993) Biochim Biophys Acta , vol.1182 , pp. 303-310
    • Kluve-Beckerman, B.1    Song, M.2    Benson, M.D.3    Liepnieks, J.J.4
  • 41
    • 0029960572 scopus 로고    scopus 로고
    • Accelerated amyloid deposition in mice treated with the aspartic protease inhibitor, pepstatin
    • Yamada T, Liepnieks JJ, Benson MD, Kluve-Beckerman B: Accelerated amyloid deposition in mice treated with the aspartic protease inhibitor, pepstatin. J Immunol 1996, 157:901-907
    • (1996) J Immunol , vol.157 , pp. 901-907
    • Yamada, T.1    Liepnieks, J.J.2    Benson, M.D.3    Kluve-Beckerman, B.4
  • 42
    • 0030908095 scopus 로고    scopus 로고
    • Models of amyloid seeding in Alzheimer's disease and scrapie: Mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins
    • Harper JD, Lansbury PT: Models of amyloid seeding in Alzheimer's disease and scrapie: mechanistic truths and physiological consequences of the time-dependent solubility of amyloid proteins. Annu Rev Biochem 1997, 66:385-407
    • (1997) Annu Rev Biochem , vol.66 , pp. 385-407
    • Harper, J.D.1    Lansbury, P.T.2
  • 43
    • 9044229145 scopus 로고    scopus 로고
    • On the nucleation and growth of amyloid β-protein fibrils: Detection of nuclei and quantitation of rate constants
    • Lomakin A, Chung DS, Benedek GB, Kirschner DA, Teplow DB: On the nucleation and growth of amyloid β-protein fibrils: detection of nuclei and quantitation of rate constants. Proc Natl Acad Sci USA 1996, 93:1125-1129
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 1125-1129
    • Lomakin, A.1    Chung, D.S.2    Benedek, G.B.3    Kirschner, D.A.4    Teplow, D.B.5
  • 44
    • 0030684085 scopus 로고    scopus 로고
    • Aβ amyloidogenesis: Unique, or variation on a systemic theme?
    • Kisilevsky R, Fraser PE: Aβ amyloidogenesis: unique, or variation on a systemic theme? Crit Rev Biochem Mol Biol 1997, 32:361-404
    • (1997) Crit Rev Biochem Mol Biol , vol.32 , pp. 361-404
    • Kisilevsky, R.1    Fraser, P.E.2
  • 45
    • 0026555175 scopus 로고
    • The N-terminal segment of protein AA determines its fibrillogenic property
    • Westermark GT, Engstrom U, Westermark P: The N-terminal segment of protein AA determines its fibrillogenic property. Biochem Biophys Res Commun 1992, 182:27-33
    • (1992) Biochem Biophys Res Commun , vol.182 , pp. 27-33
    • Westermark, G.T.1    Engstrom, U.2    Westermark, P.3
  • 46
    • 0031833147 scopus 로고    scopus 로고
    • SAA) donors by murine macrophages of four different mouse strains
    • SAA) donors by murine macrophages of four different mouse strains. Virchows Arch 1998, 432:547-555
    • (1998) Virchows Arch , vol.432 , pp. 547-555
    • Rocken, C.1    Kisilevsky, R.2
  • 47
    • 0026647903 scopus 로고
    • Serum amyloid A changes high density lipoprotein's cellular affinity. A clue to serum amyloid A's principal function
    • Kisilevsky R, Subrahmanyan L: Serum amyloid A changes high density lipoprotein's cellular affinity. A clue to serum amyloid A's principal function. Lab Invest 1992, 66:778-785
    • (1992) Lab Invest , vol.66 , pp. 778-785
    • Kisilevsky, R.1    Subrahmanyan, L.2
  • 48
    • 0016803424 scopus 로고
    • Intralysosomal formation of amyloid fibrils
    • Shirahama TS, Cohen AS: Intralysosomal formation of amyloid fibrils. Am J Pathol 1975, 81:101-116
    • (1975) Am J Pathol , vol.81 , pp. 101-116
    • Shirahama, T.S.1    Cohen, A.S.2
  • 49
    • 0027258525 scopus 로고
    • The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: Implications for the pathogenesis of Alzheimer's disease
    • Jarrett JT, Berger EP, Lansbury PT: The carboxy terminus of the β amyloid protein is critical for the seeding of amyloid formation: implications for the pathogenesis of Alzheimer's disease. Biochemistry 1993, 32:4693-4697
    • (1993) Biochemistry , vol.32 , pp. 4693-4697
    • Jarrett, J.T.1    Berger, E.P.2    Lansbury, P.T.3
  • 50
    • 0030030956 scopus 로고    scopus 로고
    • First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro
    • Naiki H, Nakakuki K: First-order kinetic model of Alzheimer's β-amyloid fibril extension in vitro. Lab Invest 1996, 74:374-383
    • (1996) Lab Invest , vol.74 , pp. 374-383
    • Naiki, H.1    Nakakuki, K.2
  • 51
    • 0025905155 scopus 로고
    • Fibril amyloid enhancing factor (FAEF)-accelerated amyloidosis in the hamster is not dependent on serine esterase activity and mononuclear phagocytosis
    • Niewold TA, Gruys E, Kisilevsky R, Shirahama TS: Fibril amyloid enhancing factor (FAEF)-accelerated amyloidosis in the hamster is not dependent on serine esterase activity and mononuclear phagocytosis. Scand J Immunol 1991, 34:101-107
    • (1991) Scand J Immunol , vol.34 , pp. 101-107
    • Niewold, T.A.1    Gruys, E.2    Kisilevsky, R.3    Shirahama, T.S.4
  • 53
    • 0001632706 scopus 로고
    • Does amyloid enhancing factor (AEF) exist? Is AEF a single biological entity?
    • Kisilevsky R, Gruys E, Shirahama T: Does amyloid enhancing factor (AEF) exist? Is AEF a single biological entity? Amyloid Int J Exp Clin Invest 1995, 2:128-134
    • (1995) Amyloid Int J Exp Clin Invest , vol.2 , pp. 128-134
    • Kisilevsky, R.1    Gruys, E.2    Shirahama, T.3
  • 54
    • 0029013897 scopus 로고
    • In vitro degradation of serum amyloid A by cathepsin d and other acid proteases: Possible protection against amyloid fibril formation
    • Yamada T, Kluve-Beckerman B, Liepnieks JJ, Benson MD: In vitro degradation of serum amyloid A by cathepsin D and other acid proteases: possible protection against amyloid fibril formation. Scand J Immunol 1995, 41:570-574
    • (1995) Scand J Immunol , vol.41 , pp. 570-574
    • Yamada, T.1    Kluve-Beckerman, B.2    Liepnieks, J.J.3    Benson, M.D.4
  • 55
    • 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 M, 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, 318:1041-1049
    • (1996) Biochem J , vol.318 , pp. 1041-1049
    • Patel, H.1    Bramall, J.2    Waters, H.3    De Beer, M.4    Woo, P.5


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