메뉴 건너뛰기




Volumn 48, Issue 3, 1998, Pages 241-247

Catabolism of lipid-free recombinant apolipoprotein serum amyloid A by mouse macrophages in vitro results in removal of the amyloid fibril-forming amino terminus

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID A PROTEIN; APOLIPOPROTEIN; RECOMBINANT PROTEIN;

EID: 0031694813     PISSN: 03009475     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1365-3083.1998.00384.x     Document Type: Article
Times cited : (10)

References (38)
  • 1
    • 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;61:390-4.
    • (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
  • 2
    • 0017265742 scopus 로고
    • Amyloid-treated serum protein SAA in endotoxin-induced amyloidosis in the mink
    • Anders RF, Nordstoga K, Natvig JB, Husby G. Amyloid-treated serum protein SAA in endotoxin-induced amyloidosis in the mink. J Exp Med 1976;143:678-86.
    • (1976) J Exp Med , vol.143 , pp. 678-686
    • Anders, R.F.1    Nordstoga, K.2    Natvig, J.B.3    Husby, G.4
  • 3
    • 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;51:2773-9.
    • (1972) J Clin Invest , vol.51 , pp. 2773-2779
    • Levin, M.1    Franklin, E.C.2    Frangione, B.3    Pras, M.4
  • 4
    • 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;21:263-8.
    • (1985) Scand J Immunol , vol.21 , pp. 263-268
    • Husebekk, A.1    Skogen, B.2    Husby, G.3    Marhaug, G.4
  • 5
    • 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 Comm 1992;182:27-33.
    • (1992) Biochem Biophys Res Comm , vol.182 , pp. 27-33
    • Westermark, G.T.1    Engstrom, U.2    Westermark, P.3
  • 7
    • 0000452490 scopus 로고
    • During AA amyloidogenesis is proteolytic attack on serum amyloid A a pre- or post-fibrillogenic event?
    • Kisilevsky R, Narindrasorasak S, Tape C, Tan R, Boudreau L. During AA amyloidogenesis is proteolytic attack on serum amyloid A a pre- or post-fibrillogenic event? Amyloid 1994;1:174-83.
    • (1994) Amyloid , vol.1 , pp. 174-183
    • Kisilevsky, R.1    Narindrasorasak, S.2    Tape, C.3    Tan, R.4    Boudreau, L.5
  • 8
    • 0018074981 scopus 로고
    • Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes
    • Lavie G, Zucker-Franklin D, Franklin EC. Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes. J Exp Med 1978;148:1020-31.
    • (1978) J Exp Med , vol.148 , pp. 1020-1031
    • Lavie, G.1    Zucker-Franklin, D.2    Franklin, E.C.3
  • 9
    • 0018958580 scopus 로고
    • Elastase-type proteases on the surface of human blood monocyte: Possible role in amyloid formation
    • Lavie G, Zucker-Franklin D, Franklin EC. Elastase-type proteases on the surface of human blood monocyte: Possible role in amyloid formation. J Immunol 1980;125:175-80.
    • (1980) J Immunol , vol.125 , pp. 175-180
    • Lavie, G.1    Zucker-Franklin, D.2    Franklin, E.C.3
  • 10
    • 0019862162 scopus 로고
    • Demonstration of membrane bound proteolytic activity on the surface of mononuclear leukocytes
    • Zucker-Franklin D, Lavie G, Franklin EC. Demonstration of membrane bound proteolytic activity on the surface of mononuclear leukocytes. J Histochem Cytochem 1981;29:451-6.
    • (1981) J Histochem Cytochem , vol.29 , pp. 451-456
    • Zucker-Franklin, D.1    Lavie, G.2    Franklin, E.C.3
  • 12
    • 0019962346 scopus 로고
    • The degradation of serum amyloid A protein by activated polymorphonuclear leukocytes: Participation of granulocytic elastase
    • Silverman SL, Cathcart ES, Skinner MS, Cohen AS. The degradation of serum amyloid A protein by activated polymorphonuclear leukocytes: participation of granulocytic elastase. Immunol 1982;46: 737-44.
    • (1982) Immunol , vol.46 , pp. 737-744
    • Silverman, S.L.1    Cathcart, E.S.2    Skinner, M.S.3    Cohen, A.S.4
  • 13
    • 0018836856 scopus 로고
    • Degradation of protein SAA to an AA-like fragment by enzymes of monocytic origin
    • Skogen B, Thorsteinsson L, Natvig JB. Degradation of protein SAA to an AA-like fragment by enzymes of monocytic origin. Scand J Immunol 1980;11:533-40.
    • (1980) Scand J Immunol , vol.11 , pp. 533-540
    • Skogen, B.1    Thorsteinsson, L.2    Natvig, J.B.3
  • 14
    • 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;14:391-8.
    • (1981) Scand J Immunol , vol.14 , pp. 391-398
    • Skogen, B.1    Natvig, J.B.2
  • 15
    • 0021249294 scopus 로고
    • Degradation of serum amyloid A and apolipoproteins by serum proteases
    • Bausserman LL, Herbert PN. Degradation of serum amyloid A and apolipoproteins by serum proteases. Biochem 1984;23:2241-5.
    • (1984) Biochem , vol.23 , pp. 2241-2245
    • Bausserman, L.L.1    Herbert, P.N.2
  • 16
    • 0029762733 scopus 로고    scopus 로고
    • Degradation of serum amyloid A in amyloid-susceptible and amyloid-resistant mouse strains
    • Elliott-Bryant R, Liang J-S, Sipe JD, Cathcart ES. Degradation of serum amyloid A in amyloid-susceptible and amyloid-resistant mouse strains. Scand J Immunol 1996;44:223-8.
    • (1996) Scand J Immunol , vol.44 , pp. 223-228
    • Elliott-Bryant, R.1    Liang, J.-S.2    Sipe, J.D.3    Cathcart, E.S.4
  • 17
    • 0343561039 scopus 로고
    • In vitro clearance of HDL associated SAA by resident peritoneal cells from CBA/J mice
    • Kisilevsky R, Benson MD, Frangione B, Gauldie J, Muckle T, Young ID, eds. New York: Parthenon Press
    • Elliott-Bryant R, Sipe JD, Gonnerman WA, Newcombe DS, Cathcart ES. In vitro clearance of HDL associated SAA by resident peritoneal cells from CBA/J mice. In: Kisilevsky R, Benson MD, Frangione B, Gauldie J, Muckle T, Young ID, eds. Amyloid and Amyloidosis 1993. New York: Parthenon Press, 1994:119-21.
    • (1994) Amyloid and Amyloidosis 1993 , pp. 119-121
    • Elliott-Bryant, R.1    Sipe, J.D.2    Gonnerman, W.A.3    Newcombe, D.S.4    Cathcart, E.S.5
  • 18
    • 0030751036 scopus 로고    scopus 로고
    • An in vitro cellular system for generation of AA amyloid
    • Palm M, Holm Nielsen E, Svehag S-E. An in vitro cellular system for generation of AA amyloid. APMIS 1997;105:603-8.
    • (1997) APMIS , vol.105 , pp. 603-608
    • Palm, M.1    Holm Nielsen, E.2    Svehag, S.-E.3
  • 19
    • 0020457015 scopus 로고
    • Changes in high density lipoprotein content following endotoxin administration in the mouse: Formation of serum amyloid protein-rich subtractions
    • Hoffman JS, Benditt EP. Changes in high density lipoprotein content following endotoxin administration in the mouse: formation of serum amyloid protein-rich subtractions. J Biol Chem 1982;257: 10510-7.
    • (1982) J Biol Chem , vol.257 , pp. 10510-10517
    • Hoffman, J.S.1    Benditt, E.P.2
  • 20
    • 0022972443 scopus 로고
    • In vitro proteolysis of human plasma low density lipoproteins by an elastase released from human blood polymorphonuclear cells
    • Polacek D, Byrne RE, Fless GM, Scanu AM. In vitro proteolysis of human plasma low density lipoproteins by an elastase released from human blood polymorphonuclear cells. J Biol Chem 1986;261: 2057-63.
    • (1986) J Biol Chem , vol.261 , pp. 2057-2063
    • Polacek, D.1    Byrne, R.E.2    Fless, G.M.3    Scanu, A.M.4
  • 22
    • 0019943055 scopus 로고
    • A serum AA-like protein as a common constituent of secondary amyloid fibrils
    • Westermark P, Sletten K, A serum AA-like protein as a common constituent of secondary amyloid fibrils. Clin Exp Immunol 1982; 49:725-31.
    • (1982) Clin Exp Immunol , vol.49 , pp. 725-731
    • Westermark, P.1    Sletten, K.2
  • 23
    • 0027959216 scopus 로고
    • Transformation from SAA2-tibrils to AA-fibrils in amyloid librillogenesis: In vivo observations in murine spleen using anti-SAA and anti-AA antibodies
    • Arai K, Miura K, Baba S, Shirasawa H. Transformation from SAA2-tibrils to AA-fibrils in amyloid librillogenesis: in vivo observations in murine spleen using anti-SAA and anti-AA antibodies. J Pathol 1994;173:127-34.
    • (1994) J Pathol , vol.173 , pp. 127-134
    • Arai, K.1    Miura, K.2    Baba, S.3    Shirasawa, H.4
  • 26
    • 0025273159 scopus 로고
    • Apolipoprotein A-1 and apolipoprotein SAA half-lives during acute inflammation and amyloidogenesis
    • Tape C, Kisilevsky R. Apolipoprotein A-1 and apolipoprotein SAA half-lives during acute inflammation and amyloidogenesis. Biochem Biophys Acta 1990;1043:295-300.
    • (1990) Biochem Biophys Acta , vol.1043 , pp. 295-300
    • Tape, C.1    Kisilevsky, R.2
  • 28
    • 0025891978 scopus 로고
    • Serum amyloid A (SAA3) produced by rabbit synovial fibroblasts treated with phorbol esters or interleukin I induces synthesis of collagenase and is neutralized with specific antiserum
    • Mitchell TI, Coon CI, Brinckerhoff CE. Serum amyloid A (SAA3) produced by rabbit synovial fibroblasts treated with phorbol esters or interleukin I induces synthesis of collagenase and is neutralized with specific antiserum. J Clin Invest 1995;87:1177-85.
    • (1995) J Clin Invest , vol.87 , pp. 1177-1185
    • Mitchell, T.I.1    Coon, C.I.2    Brinckerhoff, C.E.3
  • 29
    • 0027417158 scopus 로고
    • The acute phase reactant serum amyloid A (SAA3) is a novel substrate for degradation by the metalloproteinases collagenase and stromelysin
    • Mitchell TI, Jeffrey JJ, Palmitier RD, Brinckerhoff CE. The acute phase reactant serum amyloid A (SAA3) is a novel substrate for degradation by the metalloproteinases collagenase and stromelysin. Biochim Biophys Acta 1993;1156:245-54.
    • (1993) Biochim Biophys Acta , vol.1156 , pp. 245-254
    • Mitchell, T.I.1    Jeffrey, J.J.2    Palmitier, R.D.3    Brinckerhoff, C.E.4
  • 30
    • 0030847776 scopus 로고    scopus 로고
    • Interleukin-1 induces apolipoprotein serum amyloid A3 (apoSAA3) synthesis and secretion by cultured neonatal rabbit aotic smooth muscle muscle cells
    • Kumon Y, Sipe JD, Brinckerhoff CE, Schreiber BM. Interleukin-1 (induces apolipoprotein serum amyloid A3 (apoSAA3) synthesis and secretion by cultured neonatal rabbit aotic smooth muscle muscle cells. Scand J Immunol 1997;46:284-91.
    • (1997) Scand J Immunol , vol.46 , pp. 284-291
    • Kumon, Y.1    Sipe, J.D.2    Brinckerhoff, C.E.3    Schreiber, B.M.4
  • 31
    • 0023613158 scopus 로고
    • Primary structure of amyloid fibril protein AA in azocasein-induced amyloidosis of CBA/J mice
    • Dwulet FE, Benson MD. Primary structure of amyloid fibril protein AA in azocasein-induced amyloidosis of CBA/J mice. J Lab Clin Med 1987;110:322-9.
    • (1987) J Lab Clin Med , vol.110 , pp. 322-329
    • Dwulet, F.E.1    Benson, M.D.2
  • 33
    • 0031260287 scopus 로고    scopus 로고
    • Apolipoprotein E and apolipoprotein A-1 knock-out mice readily develop amyloid A protein amyloidosis
    • Elliott-Bryant R, Cathcart ES. Apolipoprotein E and apolipoprotein A-1 knock-out mice readily develop amyloid A protein amyloidosis. Clin Immunol Immunopathol 1997;85:104-8.
    • (1997) Clin Immunol Immunopathol , vol.85 , pp. 104-108
    • Elliott-Bryant, R.1    Cathcart, E.S.2
  • 35
    • 0030870625 scopus 로고    scopus 로고
    • Adenoviral vector-mediated overexpression of serum amyloid a on apoA-1-deficient mice
    • Webb NR, de Beer MC, van der Westhuzen DR et al. Adenoviral vector-mediated overexpression of serum amyloid A on apoA-1-deficient mice. J Lipid Res 1997;38:1583-90.
    • (1997) J Lipid Res , vol.38 , pp. 1583-1590
    • Webb, N.R.1    De Beer, M.C.2    Van Der Westhuzen, D.R.3
  • 36
    • 0021800324 scopus 로고
    • Impaired Kupffer cell function precedes development of secondary amyloidosis
    • Fuks A, Zucker-Franklin D. Impaired Kupffer cell function precedes development of secondary amyloidosis. J Exp Med 1985;148: 1013-28.
    • (1985) J Exp Med , vol.148 , pp. 1013-1028
    • Fuks, A.1    Zucker-Franklin, D.2
  • 37
    • 7144239825 scopus 로고
    • In vitro uptake of HDL-SAA by tissue macrophages during the development of AA amyloidosis in mice
    • Herbert L, Janousek J, Gervais F. In vitro uptake of HDL-SAA by tissue macrophages during the development of AA amyloidosis in mice. Amyloid 1995;2:251-6.
    • (1995) Amyloid , vol.2 , pp. 251-256
    • Herbert, L.1    Janousek, J.2    Gervais, F.3
  • 38
    • 0029777342 scopus 로고    scopus 로고
    • Expression of recombinant human serum amyloid A in mamalian 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 Beers MC, Woo P. Expression of recombinant human serum amyloid A in mamalian 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 Beers, M.C.4    Woo, P.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.