메뉴 건너뛰기




Volumn 7, Issue 1, 2000, Pages 64-69

Expression and function of serum amyloid A, a major acute-phase protein, in normal and disease states

Author keywords

[No Author keywords available]

Indexed keywords

ACUTE PHASE PROTEIN; SERUM AMYLOID A;

EID: 0033988643     PISSN: 10656251     EISSN: None     Source Type: Journal    
DOI: 10.1097/00062752-200001000-00012     Document Type: Review
Times cited : (392)

References (71)
  • 1
    • 0000211440 scopus 로고
    • Amyloid: Extraction and preliminary characterization of some proteins
    • 1 Benditt EP, Lagunoff D, Eriksen N, Iseri OA: Amyloid: extraction and preliminary characterization of some proteins. Arch Pathol 1962, 74:323-330.
    • (1962) Arch Pathol , vol.74 , pp. 323-330
    • Benditt, E.P.1    Lagunoff, D.2    Eriksen, N.3    Iseri, O.A.4
  • 2
    • 0013881710 scopus 로고
    • Amyloid III: A protein related to the subunit structure of human amyloid fibrils
    • 2 Benditt EP, Eriksen N: Amyloid III: a protein related to the subunit structure of human amyloid fibrils. Proc Natl Acad Sci U S A 1966, 55:308-316.
    • (1966) Proc Natl Acad Sci U S A , vol.55 , pp. 308-316
    • Benditt, E.P.1    Eriksen, N.2
  • 3
    • 0015846635 scopus 로고
    • Immunologic studies of the major nonimmunoglobulin protein of amyloid: Identification and partial characterization of a related serum component
    • 3 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, 132:373-380.
    • (1973) J Exp Med , vol.132 , pp. 373-380
    • Levin, M.1    Pras, M.2    Franklin, E.C.3
  • 4
    • 0016686588 scopus 로고
    • Isolation of a low molecular weight serum component antigenically related to an amyloid fibril protein of unknown origin
    • 4 Linke RP, Sipe JD, Pollock PS, Ignaczak TF, Glenner GG: Isolation of a low molecular weight serum component antigenically related to an amyloid fibril protein of unknown origin. Proc Natl Acad Sci U S A 1975, 72:1473-1476.
    • (1975) Proc Natl Acad Sci U S A , vol.72 , pp. 1473-1476
    • Linke, R.P.1    Sipe, J.D.2    Pollock, P.S.3    Ignaczak, T.F.4    Glenner, G.G.5
  • 6
    • 0025887189 scopus 로고
    • The human acute-phase serum amyloid A gene family: Structure, evolution and expression in hepatoma cells
    • 6 Betts JC, Edbrooke MR, Thakker R, Woo P: The human acute-phase serum amyloid A gene family: structure, evolution and expression in hepatoma cells. Scand J Immunol 1991, 34:471-482.
    • (1991) Scand J Immunol , vol.34 , pp. 471-482
    • Betts, J.C.1    Edbrooke, M.R.2    Thakker, R.3    Woo, P.4
  • 7
    • 0027977021 scopus 로고
    • Evolution of the serum amyloid A (SAA) protein superfamily
    • 7 Uhlar CM, Burgess CJ, Sharp PM, Whitehead AS: Evolution of the serum amyloid A (SAA) protein superfamily. Genomics 1994, 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
  • 8
    • 0028012820 scopus 로고
    • The human serum amyloid A protein (SAA) superfamily gene cluster: Mapping to chromosome 11p15.1 by physical and genetic linkage analysis
    • 8 Sellar GC, Jordan SA, Bickmore WA, Fantes JA, van Heyningen V, Whitehead AS: The human serum amyloid A protein (SAA) superfamily gene cluster: mapping to chromosome 11p15.1 by physical and genetic linkage analysis. Genomics 1994, 19:221-227.
    • (1994) Genomics , vol.19 , pp. 221-227
    • Sellar, G.C.1    Jordan, S.A.2    Bickmore, W.A.3    Fantes, J.A.4    Van Heyningen, V.5    Whitehead, A.S.6
  • 9
    • 0028135412 scopus 로고
    • Use of somatic cell hybrids and fluorescence in situ hybridization to localize the functional serum amyloid A (SAA) genes to chromosome 11p15.4-p15.1 and the entire SAA superfamily to chromosome 11p15
    • 9 Watson G, See CG, Woo P: Use of somatic cell hybrids and fluorescence in situ hybridization to localize the functional serum amyloid A (SAA) genes to chromosome 11p15.4-p15.1 and the entire SAA superfamily to chromosome 11p15. Genomics 1994, 23:694-696.
    • (1994) Genomics , vol.23 , pp. 694-696
    • Watson, G.1    See, C.G.2    Woo, P.3
  • 10
    • 0026045547 scopus 로고
    • Nonexpression of the human serum amyloid A three (SAA3) gene
    • 10 Kluve-Beckerman B, Drumm ML, Benson MD: Nonexpression of the human serum amyloid A three (SAA3) gene. DNA Cell Biol 1991, 10:651-661.
    • (1991) DNA Cell Biol , vol.10 , pp. 651-661
    • Kluve-Beckerman, B.1    Drumm, M.L.2    Benson, M.D.3
  • 11
    • 0026761363 scopus 로고
    • Identification of novel members of the serum amyloid A protein superfamily as constitutive apolipoproteins of high density lipoprotein
    • 11 Whitehead AS, deBeer MC, Steel DM, Rits M, Lelias JM, Lane WS, deBeer FC: Identification of novel members of the serum amyloid A protein superfamily as constitutive apolipoproteins of high density lipoprotein. J Biol Chem 1992, 267:3862-3867.
    • (1992) J Biol Chem , vol.267 , pp. 3862-3867
    • Whitehead, A.S.1    DeBeer, M.C.2    Steel, D.M.3    Rits, M.4    Lelias, J.M.5    Lane, W.S.6    DeBeer, F.C.7
  • 13
    • 0028202075 scopus 로고
    • Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: Implications for serum amyloid A function
    • 13 Meek RL, Urieli-Shoval S, Benditt EP: Expression of apolipoprotein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: implications for serum amyloid A function. Proc Natl Acad Sci U S A 1994, 91:3186-3190.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 3186-3190
    • Meek, R.L.1    Urieli-Shoval, S.2    Benditt, E.P.3
  • 14
    • 0031788669 scopus 로고    scopus 로고
    • Widespread expression of serum amyloid A in histologically normal human tissues: Predominant localization to the epithelium
    • 14 Urieli-Shoval S, Cohen P, Eisenberg S, Matzner Y: Widespread expression of serum amyloid A in histologically normal human tissues: predominant localization to the epithelium. J Histochem Cytochem 1998, 46:1377-1384. By in situ hybridization, immunohistochemistry, and reverse transcriptase polymerase chain reaction analyses, the authors demonstrated SAA mRNA and protein expression in many histologically normal human tissues. The authors suggested that one or more SAA proteins produced in human tissues might be constitutively expressed to serve as a first line of defense or in proper maintenance and function of human tissues (housekeeping role). Furthermore, the various proposed functions of SAA might be exerted by SAA locally produced in human tissues rather than by liver-derived SAA.
    • (1998) J Histochem Cytochem , vol.46 , pp. 1377-1384
    • Urieli-Shoval, S.1    Cohen, P.2    Eisenberg, S.3    Matzner, Y.4
  • 15
    • 0029662219 scopus 로고    scopus 로고
    • Mapping of the mouse serum amyloid A gene cluster by long-range polymerase chain reaction
    • 15 Butler A, Whitehead AS: Mapping of the mouse serum amyloid A gene cluster by long-range polymerase chain reaction. Immunogenetics 1996, 44:468-474.
    • (1996) Immunogenetics , vol.44 , pp. 468-474
    • Butler, A.1    Whitehead, A.S.2
  • 16
    • 0023002352 scopus 로고
    • Amyloid A gene family expression in different mouse tissues
    • 16 Meek RL, Benditt EP: Amyloid A gene family expression in different mouse tissues. J Exp Med 1986, 164:2006-2017.
    • (1986) J Exp Med , vol.164 , pp. 2006-2017
    • Meek, R.L.1    Benditt, E.P.2
  • 17
    • 0033045614 scopus 로고    scopus 로고
    • Revised nomenclature for serum amyloid A (SAA)
    • 17 Sipe J: Revised nomenclature for serum amyloid A (SAA). Amyloid:Int J Exp Clin Invest 1999, 6:67-70. This is a revised nomenclature for the multiple SAA genes in humans and mice and their various allelic variants. The attendees of the recent SAA Gordon Research Conference and the VIII International Symposium on Amyloidosis recommended it. The attention of AA and SAA researchers is called to the changes in the SAA nomenclature.
    • (1999) Amyloid:Int J Exp Clin Invest , vol.6 , pp. 67-70
    • Sipe, J.1
  • 18
    • 0033545342 scopus 로고    scopus 로고
    • Acute-phase proteins and other systemic responses to inflammation
    • 18 Gabay C, Kushner I: Acute-phase proteins and other systemic responses to inflammation. N Engl J Med 1999, 340:448-454.
    • (1999) N Engl J Med , vol.340 , pp. 448-454
    • Gabay, C.1    Kushner, I.2
  • 19
    • 0024420907 scopus 로고
    • Serum amyloid A in the mouse: Sites of uptake and mRNA expression
    • 19 Meek RL, Eriksen N, Benditt EP: Serum amyloid A in the mouse: sites of uptake and mRNA expression. Am J Pathol 1989, 135:411-419.
    • (1989) Am J Pathol , vol.135 , pp. 411-419
    • Meek, R.L.1    Eriksen, N.2    Benditt, E.P.3
  • 20
    • 0022179342 scopus 로고
    • Expression and regulation of the murine serum amyloid A (SAA) gene in extrahepatic sites
    • 20 Ramadori G, Sipe JD, Colten HR: Expression and regulation of the murine serum amyloid A (SAA) gene in extrahepatic sites. J Immunol 1985, 135:3645-3647.
    • (1985) J Immunol , vol.135 , pp. 3645-3647
    • Ramadori, G.1    Sipe, J.D.2    Colten, H.R.3
  • 21
    • 0031576813 scopus 로고    scopus 로고
    • LPS and cytokines regulate extrahepatic mRNA levels of apolipoproteins during the acute phase response in Syrian hamsters
    • 21 Hardardottir I, Sipe J, Moser AH, Fielding CJ, Feingold KR, Grunfeld C: LPS and cytokines regulate extrahepatic mRNA levels of apolipoproteins during the acute phase response in Syrian hamsters. Biochim Biophys Acta 1997, 1344:210-220.
    • (1997) Biochim Biophys Acta , vol.1344 , pp. 210-220
    • Hardardottir, I.1    Sipe, J.2    Moser, A.H.3    Fielding, C.J.4    Feingold, K.R.5    Grunfeld, C.6
  • 22
    • 0029834741 scopus 로고    scopus 로고
    • Both acute phase and constitutive serum amyloid A are present in atherosclerotic lesions
    • 22 Yamada T, Kakihara T, Kamishima T, Fukuda T, Kawai T: Both acute phase and constitutive serum amyloid A are present in atherosclerotic lesions. Pathol Int 1996 46:797-800.
    • (1996) Pathol Int , vol.46 , pp. 797-800
    • Yamada, T.1    Kakihara, T.2    Kamishima, T.3    Fukuda, T.4    Kawai, T.5
  • 23
    • 0030847776 scopus 로고    scopus 로고
    • Regulation of extrahepatic apolipoprotein serum amyloid A (apoSAA) gene expression by interleukin-1 alpha alone: Synthesis and secretion of apoSAA by cultured aortic smooth muscle cells
    • 23 Kumon Y, Sipe JD, Brinckerhoff CE, Schreiber BM: Regulation of extrahepatic apolipoprotein serum amyloid A (apoSAA) gene expression by interleukin-1 alpha alone: synthesis and secretion of apoSAA by cultured aortic smooth muscle cells. Scand J Immunol 1997, 46:284-291.
    • (1997) Scand J Immunol , vol.46 , pp. 284-291
    • Kumon, Y.1    Sipe, J.D.2    Brinckerhoff, C.E.3    Schreiber, B.M.4
  • 24
    • 0029840517 scopus 로고    scopus 로고
    • Expression and regulation of constitutive and acute phase serum amyloid A mRNAs in hepatic and non-hepatic cell lines
    • 24 Steel DM, Donoghue FC, O'Neill RM, Uhlar CM, Whitehead AS: Expression and regulation of constitutive and acute phase serum amyloid A mRNAs in hepatic and non-hepatic cell lines. Scand J Immunol 1996, 44:493-500.
    • (1996) Scand J Immunol , vol.44 , pp. 493-500
    • Steel, D.M.1    Donoghue, F.C.2    O'Neill, R.M.3    Uhlar, C.M.4    Whitehead, A.S.5
  • 25
    • 0031552382 scopus 로고    scopus 로고
    • Evidence for local production of acute phase response apolipoprotein serum amyloid A in Alzheimer's disease brain
    • 25 Liang JS, Sloane JA, Wells JM, Abraham CR, Fine RE, Sipe JD: Evidence for local production of acute phase response apolipoprotein serum amyloid A in Alzheimer's disease brain. Neurosci Lett 1997, 225:73-76.
    • (1997) Neurosci Lett , vol.225 , pp. 73-76
    • Liang, J.S.1    Sloane, J.A.2    Wells, J.M.3    Abraham, C.R.4    Fine, R.E.5    Sipe, J.D.6
  • 26
    • 0032916193 scopus 로고    scopus 로고
    • Local expression of acute phase serum amyloid A mRNA in rheumatoid arthritis synovial tissue and cells
    • 26 Kumon Y, Suehiro T, Hashimoto K, Nakatani K, Sipe JD: Local expression of acute phase serum amyloid A mRNA in rheumatoid arthritis synovial tissue and cells. J Rheumatol 1999, 26:785-790.
    • (1999) J Rheumatol , vol.26 , pp. 785-790
    • Kumon, Y.1    Suehiro, T.2    Hashimoto, K.3    Nakatani, K.4    Sipe, J.D.5
  • 27
    • 0032530560 scopus 로고    scopus 로고
    • Regulation of serum amyloid A protein expression during the acute-phase response
    • 27 Jensen LE, Whitehead AS: Regulation of serum amyloid A protein expression during the acute-phase response. Biochem J 1998, 334:489-503. This is an extensive review of the various molecular mechanisms regulating SAA expression. It includes proposed models for the cytokine network, transcription activators, and repressors mediating expression of SAA during the acute-phase response.
    • (1998) Biochem J , vol.334 , pp. 489-503
    • Jensen, L.E.1    Whitehead, A.S.2
  • 28
    • 0032908017 scopus 로고    scopus 로고
    • Mechanism of minimally modified LDL-mediated induction of serum amyloid A gene in monocyte/macrophage cells
    • 28 Ray BK, Chatterjee S, Ray A: Mechanism of minimally modified LDL-mediated induction of serum amyloid A gene in monocyte/macrophage cells. DNA Cell Biol 1999, 18:65-73.
    • (1999) DNA Cell Biol , vol.18 , pp. 65-73
    • Ray, B.K.1    Chatterjee, S.2    Ray, A.3
  • 29
    • 0033548185 scopus 로고    scopus 로고
    • Activation of sp1 and its functional co-operation with serum amyloid A-activating sequence binding factor in synoviocyte cells trigger synergistic action of interleukin-1 and interleukin-6 in serum amyloid A gene expression
    • 29 Ray A, Schatten H, Ray BK: Activation of Sp1 and its functional co-operation with serum amyloid A-activating sequence binding factor in synoviocyte cells trigger synergistic action of interleukin-1 and interleukin-6 in serum amyloid A gene expression. J Biol Chem 1999, 274:4300-4308.
    • (1999) J Biol Chem , vol.274 , pp. 4300-4308
    • Ray, A.1    Schatten, H.2    Ray, B.K.3
  • 30
    • 0028967721 scopus 로고
    • Kinetic modeling and mathematical analysis indicate that acute phase gene expression in Hep3B cells is regulated by both transcriptional and posttranscriptional mechanisms
    • 30 Jiang SL, Samols D, Rzewnicki D, Macintyre SS, Greber I, Sipe J, Kushner I: Kinetic modeling and mathematical analysis indicate that acute phase gene expression in Hep3B cells is regulated by both transcriptional and posttranscriptional mechanisms. J Clin Invest 1995, 95:1253-1261.
    • (1995) J Clin Invest , vol.95 , pp. 1253-1261
    • Jiang, S.L.1    Samols, D.2    Rzewnicki, D.3    Macintyre, S.S.4    Greber, I.5    Sipe, J.6    Kushner, I.7
  • 31
    • 0028797236 scopus 로고
    • Induction of human serum amyloid A in Hep3B cells by IL-6 and IL-1 beta involves both transcriptional and post-transcriptional mechanisms
    • 31 Jiang SL, Lozanski G, Samols D, Kushner I: Induction of human serum amyloid A in Hep3B cells by IL-6 and IL-1 beta involves both transcriptional and post-transcriptional mechanisms. J Immunol 1995, 154:825-831.
    • (1995) J Immunol , vol.154 , pp. 825-831
    • Jiang, S.L.1    Lozanski, G.2    Samols, D.3    Kushner, I.4
  • 32
    • 0030722633 scopus 로고    scopus 로고
    • The sphingomyelin-ceramide pathway participates in cytokine regulation of C-reactive protein and serum amyloid A, but not alpha-fibrinogen
    • 32 Lozanski G, Berthier F, Kushner I: The sphingomyelin-ceramide pathway participates in cytokine regulation of C-reactive protein and serum amyloid A, but not alpha-fibrinogen. Biochem J 1997, 328:271-275.
    • (1997) Biochem J , vol.328 , pp. 271-275
    • Lozanski, G.1    Berthier, F.2    Kushner, I.3
  • 33
    • 0029126986 scopus 로고
    • Serum amyloid A induces calcium mobilization and chemotaxis of human monocytes by activating a pertussis toxin-sensitive signaling pathway
    • 33 Badolato R, Johnston JA, Wang JM, McVicar D, Xu LL, Oppenheim JJ, Kelvin DJ: Serum amyloid A induces calcium mobilization and chemotaxis of human monocytes by activating a pertussis toxin-sensitive signaling pathway. J Immunol 1995, 155:4004-4010.
    • (1995) J Immunol , vol.155 , pp. 4004-4010
    • Badolato, R.1    Johnston, J.A.2    Wang, J.M.3    McVicar, D.4    Xu, L.L.5    Oppenheim, J.J.6    Kelvin, D.J.7
  • 34
    • 0033534791 scopus 로고    scopus 로고
    • Serum amyloid A induces chemotaxis of human mast cells by activating a pertussis toxin-sensitive signal transduction pathway
    • 34 Olsson N, Siegbahn A, Nilsson G: Serum amyloid A induces chemotaxis of human mast cells by activating a pertussis toxin-sensitive signal transduction pathway. Biochem Biophys Res Commun 1999, 254:143-146.
    • (1999) Biochem Biophys Res Commun , vol.254 , pp. 143-146
    • Olsson, N.1    Siegbahn, A.2    Nilsson, G.3
  • 35
    • 0000485181 scopus 로고    scopus 로고
    • A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells
    • 35 Su SB, Gong W, Gao JL, Shen W, Murphy PM, Oppenheim JJ, Wang JM: A seven-transmembrane, G protein-coupled receptor, FPRL1, mediates the chemotactic activity of serum amyloid A for human phagocytic cells. J Exp Med 1999, 189:395-402.
    • (1999) J Exp Med , vol.189 , pp. 395-402
    • Su, S.B.1    Gong, W.2    Gao, J.L.3    Shen, W.4    Murphy, P.M.5    Oppenheim, J.J.6    Wang, J.M.7
  • 36
    • 23444460848 scopus 로고
    • Serum amyloid A is a chemoattractant: Induction of migration, adhesion and tissue infiltration of monocytes and polymorphonuclear leukocytes
    • 36 Badolato R, Wang JM, Murphy WJ, Lloyd AR, Michiel DF, Bausserman LL, et al.: Serum amyloid A is a chemoattractant: induction of migration, adhesion and tissue infiltration of monocytes and polymorphonuclear leukocytes. J Exp Med 1994, 180:203-209.
    • (1994) J Exp Med , vol.180 , pp. 203-209
    • Badolato, R.1    Wang, J.M.2    Murphy, W.J.3    Lloyd, A.R.4    Michiel, D.F.5    Bausserman, L.L.6
  • 38
    • 0026647903 scopus 로고
    • Serum amyloid A changes high density lipoprotein's cellular affinity: A clue to serum amyloid's principal function
    • 38 Kisilevsky R, Subrahmanyan L: Serum amyloid A changes high density lipoprotein's cellular affinity: a clue to serum amyloid's principal function. Lab Invest 1992, 66:778-785.
    • (1992) Lab Invest , vol.66 , pp. 778-785
    • Kisilevsky, R.1    Subrahmanyan, L.2
  • 39
    • 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
    • 39 Liang JS, Schreiber BM, Salmona M, Phillip G, Gonnerman WA, de Beer FC, Sipe JD: 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, 37:2109-2116.
    • (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    Sipe, J.D.7
  • 40
    • 0025730743 scopus 로고
    • Modulation of endotoxic activity of lipopolysaccharide by high-density lipoprotein
    • 40 Baumberger C, Ulevitch R, Dayer J: Modulation of endotoxic activity of lipopolysaccharide by high-density lipoprotein. Pathobiology 1991, 59:378-383.
    • (1991) Pathobiology , vol.59 , pp. 378-383
    • Baumberger, C.1    Ulevitch, R.2    Dayer, J.3
  • 41
    • 0020045084 scopus 로고
    • SAA suppression of immune response in vitro: Evidence for an effect on T cell-macrophage interaction
    • 41 Aldo-Benson MA, Benson MD: SAA suppression of immune response in vitro: evidence for an effect on T cell-macrophage interaction. J Immunol 1982, 128:2390-2392.
    • (1982) J Immunol , vol.128 , pp. 2390-2392
    • Aldo-Benson, M.A.1    Benson, M.D.2
  • 43
    • 0030310907 scopus 로고    scopus 로고
    • Effect of serum amyloid A, HDL-apolipoprotein on endothelial cell proliferation: Implication of an enigmatic protein to atherosclerosis
    • 43 Shainkin-Kestenbaum R, Zimlichman S, Lis M, Lidor C, Pomerantz M, Knyszynski A, et al.: Effect of serum amyloid A, HDL-apolipoprotein on endothelial cell proliferation: implication of an enigmatic protein to atherosclerosis. Biomed Pept Proteins Nucleic Acids 1997, 2:79-84.
    • (1997) Biomed Pept Proteins Nucleic Acids , vol.2 , pp. 79-84
    • Shainkin-Kestenbaum, R.1    Zimlichman, S.2    Lis, M.3    Lidor, C.4    Pomerantz, M.5    Knyszynski, A.6
  • 45
    • 0025785598 scopus 로고
    • Inhibition of the oxidative burst response of N formyl peptide-stimulated neutrophils by serum amyloid A protein
    • 45 Linke RP, Bock V, Valet G, Rothe G: Inhibition of the oxidative burst response of N formyl peptide-stimulated neutrophils by serum amyloid A protein. Biochem Biophys Res Commun 1991, 176:1100-1105.
    • (1991) Biochem Biophys Res Commun , vol.176 , pp. 1100-1105
    • Linke, R.P.1    Bock, V.2    Valet, G.3    Rothe, G.4
  • 47
    • 0028227317 scopus 로고
    • Inhibition of cell adhesion to glycoproteins of the extracellular matrix by peptides corresponding to serum amyloid A: Toward understanding the physiological role of an enigmatic protein
    • 47 Preciado PL, Levartowsky D, Pras M, Hershkoviz R, Lider O, Fridkin M: Inhibition of cell adhesion to glycoproteins of the extracellular matrix by peptides corresponding to serum amyloid A: toward understanding the physiological role of an enigmatic protein. Eur J Biochem 1994, 223:35-42.
    • (1994) Eur J Biochem , vol.223 , pp. 35-42
    • Preciado, P.L.1    Levartowsky, D.2    Pras, M.3    Hershkoviz, R.4    Lider, O.5    Fridkin, M.6
  • 48
    • 0029100030 scopus 로고
    • A novel biologic function of serum amyloid A: Induction of T lymphocyte migration and adhesion
    • 48 Xu L, Badolato R, Murphy WJ, Longo DL, Anver M, Hale S, et al.: A novel biologic function of serum amyloid A: induction of T lymphocyte migration and adhesion. J Immunol 1995, 155:1184-1190.
    • (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
  • 49
    • 0030043750 scopus 로고    scopus 로고
    • Serum amyloid A binds specific extracellular matrix glycoproteins and induces the adhesion of resting CD4+ T cells
    • 49 Preciado-Patt L, Hershkoviz R, Fridkin M, Lider O: Serum amyloid A binds specific extracellular matrix glycoproteins and induces the adhesion of resting CD4+ T cells. J Immunol 1996, 156:1189-1895.
    • (1996) J Immunol , vol.156 , pp. 1189-1895
    • Preciado-Patt, L.1    Hershkoviz, R.2    Fridkin, M.3    Lider, O.4
  • 52
    • 0031805385 scopus 로고    scopus 로고
    • Serum amyloid A protein induces production of matrix metalloproteinases by human synovial fibroblasts
    • 52 Migita K, Kawabe Y, Tominaga M, Origuchi T, Aoyagi T, Eguchi K: Serum amyloid A protein induces production of matrix metalloproteinases by human synovial fibroblasts. Lab Invest 1998, 78:535-539.
    • (1998) Lab Invest , vol.78 , pp. 535-539
    • Migita, K.1    Kawabe, Y.2    Tominaga, M.3    Origuchi, T.4    Aoyagi, T.5    Eguchi, K.6
  • 53
    • 0027417158 scopus 로고
    • The acute phase reactant serum amyloid A (SAA3) is a novel substrate for degradation by the metalloproteinases collagenase and stromelysin
    • 53 Mitchell TI, Jeffrey JJ, Palmiter 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, 1156:245-254.
    • (1993) Biochim Biophys Acta , vol.1156 , pp. 245-254
    • Mitchell, T.I.1    Jeffrey, J.J.2    Palmiter, R.D.3    Brinckerhoff, C.E.4
  • 55
    • 0022911274 scopus 로고
    • Secondary structure prediction of human SAA1: Presumptive identification of calcium and lipid binding sites
    • 55 Turnell W, Sarra R, Glover ID, Baum JO, Caspi D, Baltz ML, Pepys MB: 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    Pepys, M.B.7
  • 56
    • 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
    • 56 Patel H, Bramall J, Waters H, De Beer MC, 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.C.4    Woo, P.5
  • 57
    • 0031023166 scopus 로고    scopus 로고
    • Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A
    • 57 Ancsin JB, Kisilevsky R: Characterization of high affinity binding between laminin and the acute-phase protein, serum amyloid A. J Biol Chem 1997, 272:406-413.
    • (1997) J Biol Chem , vol.272 , pp. 406-413
    • Ancsin, J.B.1    Kisilevsky, R.2
  • 58
    • 0032967093 scopus 로고    scopus 로고
    • Laminin interactions with the apoproteins of acute-phase HDL: Preliminary mapping of the laminin binding site on serum amyloid A
    • 58 Ancsin JB, Kisilevsky R: Laminin interactions with the apoproteins of acute-phase HDL: preliminary mapping of the laminin binding site on serum amyloid A. Amyloid:lnt J Exp Clin Invest 1999, 6:37-47.
    • (1999) Amyloid:Int J Exp Clin Invest , vol.6 , pp. 37-47
    • Ancsin, J.B.1    Kisilevsky, R.2
  • 59
    • 0033548474 scopus 로고    scopus 로고
    • The heparin/heparan sulfate-binding site on aposerum amyloid A: Implications for the therapeutic intervention of amyloidosis
    • 59 Ancsin JB, Kisilevsky R: The heparin/heparan sulfate-binding site on aposerum amyloid A: implications for the therapeutic intervention of amyloidosis. J Biol Chem 1999, 274:7172-7181. A heparin/heparan sulfate binding site was found on SAA and was implicated in the pathogenesis of AA amyloidosis. This site mediates binding of many proteins to heparan-sulfate-proteoglycans found in the extracellular matrices of human tissues and is implicated in many physiologic and pathologic processes involving cell attachment, migration, proliferation, and differentiation. The significance of this site in SAA, beyond its possible role in AA amyloidosis, requires further investigation.
    • (1999) J Biol Chem , vol.274 , pp. 7172-7181
    • Ancsin, J.B.1    Kisilevsky, R.2
  • 60
    • 0033021099 scopus 로고    scopus 로고
    • A cell culture system for the study of amyloid pathogenesis: Amyloid formation by peritoneal macrophages cultured with recombinant serum amyloid A
    • 60 Kluve-Beckerman B, Liepnieks JJ, Wang L, Benson MD: A cell culture system for the study of amyloid pathogenesis: amyloid formation by peritoneal macrophages cultured with recombinant serum amyloid A. Am J Pathol 1999, 155:123-133.
    • (1999) Am J Pathol , vol.155 , pp. 123-133
    • Kluve-Beckerman, B.1    Liepnieks, J.J.2    Wang, L.3    Benson, M.D.4
  • 62
    • 0033522983 scopus 로고    scopus 로고
    • Induction of β-sheet structure in amyloidogenic peptides by neutralization of aspartate: A model for amyloid nucleation
    • 62 Orpiszewski J, Benson MD: Induction of β-sheet structure in amyloidogenic peptides by neutralization of aspartate: a model for amyloid nucleation. J Mol Biol 1999, 289:413-428.
    • (1999) J Mol Biol , vol.289 , pp. 413-428
    • Orpiszewski, J.1    Benson, M.D.2
  • 64
    • 0031026962 scopus 로고    scopus 로고
    • Rheumatoid arthritis exhibits reduced acute phase and enhanced constitutive serum amyloid A protein in synovial fluid relative to serum: A comparison with C-reactive protein
    • 64 Kumon Y, Loose LD, Birbara CA, Sipe JD: Rheumatoid arthritis exhibits reduced acute phase and enhanced constitutive serum amyloid A protein in synovial fluid relative to serum: a comparison with C-reactive protein. J Rheumatol 1997, 24:14-19.
    • (1997) J Rheumatol , vol.24 , pp. 14-19
    • Kumon, Y.1    Loose, L.D.2    Birbara, C.A.3    Sipe, J.D.4
  • 65
    • 0028965566 scopus 로고
    • Synovial fluid from rheumatoid arthritis patients contains sufficient levels of IL-1 beta and IL-6 to promote production of serum amyloid A by Hep3B cells
    • 65 McNiff PA, Stewart C, Sullivan J, Showell HJ, Gabel CA: Synovial fluid from rheumatoid arthritis patients contains sufficient levels of IL-1 beta and IL-6 to promote production of serum amyloid A by Hep3B cells. Cytokine 1995, 7:209-219.
    • (1995) Cytokine , vol.7 , pp. 209-219
    • McNiff, P.A.1    Stewart, C.2    Sullivan, J.3    Showell, H.J.4    Gabel, C.A.5
  • 66
    • 0018718840 scopus 로고
    • Serum amyloid A to monitor cancer dissemination
    • 66 Rosenthal CJ, Sullivan LE: Serum amyloid A to monitor cancer dissemination. Ann Intern Med 1979, 91:383-390.
    • (1979) Ann Intern Med , vol.91 , pp. 383-390
    • Rosenthal, C.J.1    Sullivan, L.E.2
  • 67
    • 0022480472 scopus 로고
    • Serum amyloid A (SAA) variations in patients with cancer: Correlation with disease activity, stage, primary site, and prognosis
    • 67 Biran H, Friedman N, Neumann L, Pras M, Shainkin-Kestenbaum R: Serum amyloid A (SAA) variations in patients with cancer: correlation with disease activity, stage, primary site, and prognosis. J Clin Pathol 1986, 39:794-797.
    • (1986) J Clin Pathol , vol.39 , pp. 794-797
    • Biran, H.1    Friedman, N.2    Neumann, L.3    Pras, M.4    Shainkin-Kestenbaum, R.5
  • 68
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • 68 Ruoslahti E, Pierschbacher MD: New perspectives in cell adhesion: RGD and integrins. Science 1987, 238:491-496.
    • (1987) Science , vol.238 , pp. 491-496
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 69
    • 0025911046 scopus 로고
    • Inhibition of angiogenesis in vitro by Arg-Gly-Asp-containing synthetic peptide
    • 69 Nicosia RF, Bonanno E: Inhibition of angiogenesis in vitro by Arg-Gly-Asp-containing synthetic peptide. Am J Pathol 1991, 138:829-833.
    • (1991) Am J Pathol , vol.138 , pp. 829-833
    • Nicosia, R.F.1    Bonanno, E.2
  • 70
    • 0030069443 scopus 로고    scopus 로고
    • Inhibition of angiogenesis, tumor growth and experimental metastasis of human fibrosarcoma cells HT1080 by a multimeric form of the laminin sequence Tyr-lle-Gly-Ser-Arg (YIGSR)
    • 70 Iwamoto Y, Nomizu M, Yamada Y, Ito Y, Tanaka K, Sugioka Y: Inhibition of angiogenesis, tumor growth and experimental metastasis of human fibrosarcoma cells HT1080 by a multimeric form of the laminin sequence Tyr-lle-Gly-Ser-Arg (YIGSR). Br J Cancer 1996, 73:589-595.
    • (1996) Br J Cancer , vol.73 , pp. 589-595
    • Iwamoto, Y.1    Nomizu, M.2    Yamada, Y.3    Ito, Y.4    Tanaka, K.5    Sugioka, Y.6
  • 71
    • 0032918632 scopus 로고    scopus 로고
    • Serum amyloid A (SAA): A concise review of biology, assay methods and clinical usefulness
    • 71 Yamada T: Serum amyloid A (SAA): a concise review of biology, assay methods and clinical usefulness. Clin Chem Lab Med 1999, 37:381-388.
    • (1999) Clin Chem Lab Med , vol.37 , pp. 381-388
    • Yamada, T.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.