The path of murine serum amyloid a through peritoneal macrophages

References

• Jensen L E, Hiney M P, Shields D C, Uhlar C M, Lindsay A J, Whitehead A S. Acute phase proteins in salmonids – Evolutionary analyses and acute phase response. J Immunol 1997; 158: 384–392
   PubMed Web of Science ®Google Scholar
• Santiago P, Roig-Lopez J L, Santiago C, Garcia-Arraras J E. Serum amyloid A protein in an echinoderm: Its primary structure and expression during intestinal regeneration in the sea cucumber Holothuria glaberrima. J Exp Zool 2000; 288: 335–344
   PubMedGoogle Scholar
• Sipe J D. Serum amyloid A: from fibril to function. Current status. Amyloid 2000; 7: 10–12
   PubMed Web of Science ®Google Scholar
• Liepnieks J J, Kluve-Beckerman B, Benson M D. Characterization of amyloid A protein in human secondary amyloidosis: The predominant deposition of serum amyloid A1. Biochim Biophys Acta 1995; 1270: 81–86
   PubMed Web of Science ®Google Scholar
• Hoffman J S, Ericsson L H, Eriksen N, Walsh K A, Benditt E P. Murine tissue amyloid protein AA: NH2-terminal sequence identity with only one of two serum amyloid protein (ApoSAA) gene products. J Exp Med 1984; 159: 641–646
   PubMed Web of Science ®Google Scholar
• Sipe J D, Rokita H, de Beer F C. Cytokine regulation of the mouse SAA gene family. Acute phase proteins: molecular biology, biochemistry, and clinical applications, A Mackiewicz, I Kushner, H Baumann. CRC Press, Boca Raton 1993; 511–526
   Google Scholar
• Morrow J F, Stearman R S, Peltzman C G, Potter D A. Induction of hepatic synthesis of serum amyloid A protein and actin. Proc Natl Acad Sci USA 1981; 78: 4718–4722
   PubMed Web of Science ®Google Scholar
• Benditt E P, Eriksen N. Amyloid protein SAA is associated with high density lipoprotein from human serum. Proc Natl Acad Sci USA 1977; 74: 4025–4028
   PubMed Web of Science ®Google Scholar
• Banka C L, Yuan T, De Beer M C, Kindy M, Curtiss L K, de Beer F C. Serum amyloid A (SAA): Influence on HDL-mediated cellular cholesterol efflux. J Lipid Res 1995; 36: 1058–1065
   PubMed Web of Science ®Google Scholar
• Rocken C, Kisilevsky R. Binding and endocytosis of high density lipoprotein from healthy (HDL) and inflammed (HDLsaa) donors by murine macrophages in-vitro. A light and electronmicroscopic investigation. Amyloid Int J Exp Clin Invest 1997; 4: 259–273
   Web of Science ®Google Scholar
• Tam S P, Flexman A, Hulme J, Kisilevsky R. Promoting export of macrophage cholesterol: the physiological role of a major acute-phase protein, serum amyloid A 2.1. J Lipid Res 2002; 43: 1410–1420
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Tam S P. Macrophage cholesterol efflux and the active domains of serum amyloid A2.1. J Lipid Res 2003; 44: 2257–2269
   PubMed Web of Science ®Google Scholar
• Kluve-Beckerman B, Manaloor J, Leipnieks J J. Binding, trafficking and accumulation of serum amyloid A in peritoneal macrophages. Scand J Immunol 2001; 53: 393–400
   PubMed Web of Science ®Google Scholar
• Ancsin J B, 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: 7172–7181
   PubMed Web of Science ®Google Scholar
• Ancsin J B, Kisilevsky R. Laminin interactions with the apoproteins of acute-phase HDL: preliminary mapping of the laminin binding site on serum amyloid A. Amyloid Int J Exp Clin Invest 1999; 6: 37–47
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Weiler L, Treloar M A. An analysis of alterations in ribosomal conformation using reductive methylation. J Biol Chem 1978; 253: 7101–7108
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Boudreau L. The kinetics of amyloid deposition: I. The effect of amyloid enhancing factor and splenectomy. Lab Invest 1983; 48: 53–59
   PubMed Web of Science ®Google Scholar
• Kisilevsky R, Lemieux L J, Fraser P E, Kong X Q, Hultin P G, Szarek W A. Arresting amyloidosis in vivo using small-molecule anionic sulphonates or sulphates: Implications for Alzheimer's disease. Nat Med 1995; 1: 143–148
   PubMed Web of Science ®Google Scholar
• Ludwin S K. An autoradiographic study of cellular proliferation in remyelination of the central nervous system. Am J Pathol 1979; 95: 683–696
   PubMed Web of Science ®Google Scholar
• Kopriwa B M. A reliable, standardized method for ultrastructural electron microscopic radioautography. Histochemie 1973; 37: 1–17
   PubMedGoogle Scholar
• Jonas A. Reconstitution of high density lipopropteins. Meth Enzymol 1986; 128: 553–582
   PubMed Web of Science ®Google Scholar
• 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 Int J Exp Clin Invest 1994; 1: 174–183
   Web of Science ®Google Scholar
• 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
   PubMed Web of Science ®Google Scholar
• Su S B, Gong W H, Gao J L, Shen W P, Murphy P M, Oppenheim J J, Wang J M. 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
   PubMed Web of Science ®Google Scholar
• Cai L, De Beer M C, de Beer F C, van der Westhuyzen D R. Serum amyloid a is a ligand for scavenger receptor class B type I and inhibits high density lipoprotein binding and selective lipid uptake. J Biol Chem 2005; 280: 2954–2961
   PubMed Web of Science ®Google Scholar
• Elliott-Bryant R, Silbert J E, Sugumaran G. Serum amyloid A, an acute-phase protein, modulates proteoglycan synthesis in cultured murine peritoneal macrophages. Biochem Biophys Res Commun 1999; 261: 298–301
   PubMed Web of Science ®Google Scholar
• Hatanaka E, Pereira-Ribeiro F, Campa A. The acute phase protein serum amyloid A primes neutrophils. FEMS Immunol Med Microbiol 2003; 38: 81–84
   PubMedGoogle Scholar
• Hatanaka E, Carvalho B T, Condino-Neto A, Campa A. Hyperresponsiveness of neutrophils from gp 91phox deficient patients to lipopolysaccharide and serum amyloid A. Immunol Lett 2004; 94: 43–46
   PubMed Web of Science ®Google Scholar
• Saphire A CS, Bark S J, Gerace L. All four homochiral enantiomers of a nuclear localization sequence derived from c-Myc serve as functional import signals. J Biol Chem 1998; 273: 29764–29769
   PubMed Web of Science ®Google Scholar
• Robbins J, Dilworth S M, Laskey R A, Dingwall C. Two interdependent basic domains in nucleoplasm nuclear targeting sequence: indentification of a class of bipartite nuclear targeting sequence. Cell 1991; 64: 615–623
   PubMed Web of Science ®Google Scholar
• Pemberton L F, Paschal B M. Mechanism of receptor-mediated nuclear import and nuclear export. Traffic 2005; 6: 187–198
   PubMed Web of Science ®Google Scholar
• Bryant D M, Stow J L. Nuclear translocation of cell-surface receptors: lessons from fibroblast growth factor. Traffic 2005; 6: 947–954
   PubMed Web of Science ®Google Scholar
• Goldfarb D S, Corbett A H, Mason D A, Harreman M T, Adam S A. Importin α: a multipurpose nuclear-transport receptor. Trends Cell Biol 2004; 14: 505–514
   PubMed Web of Science ®Google Scholar
• Rocken C, Shakespeare A. Pathology, diagnosis and pathogenesis of AA amyloidosis. Virchows Archiv 2002; 440: 111–122
   PubMed Web of Science ®Google Scholar
• Ericsson L H, Eriksen N, Walsh K A, Benditt E P. Primary structure of duck amyloid protein A: The form deposited in tissues may be identical to its serum precursor. FEBS Lett 1987; 218: 11–16
   PubMed Web of Science ®Google Scholar
• Magy N, Liepnieks J J, Benson M D, Kluve-Beckerman B. Amyloid-enhancing factor mediates amyloid formation on fibroblasts via a nidus/template mechanism. Arthritis Rheum 2003; 48: 1430–1437
   PubMed Web of Science ®Google Scholar
• Tape C, Kisilevsky R. Apolipoprotein-A-I and Apolipoprotein SAA Half-Lives During Acute Inflammation and Amyloidogenesis. Biochim Biophys Acta 1990; 1043: 295–300
   PubMed Web of Science ®Google Scholar
• Turnell W, Sarra R, Glover I D, Baum J O, Caspi D, Baltz M L, Pepys M B. Secondary structure prediction of human SAA1 presumptive identification of calcium and lipid binding sites. Mol Biol Med 1986; 3: 387–408
   PubMedGoogle Scholar
• Turnell W G, Sarra R, Glover I OG, Baum J, Caspi D, Baltz M L, Pepys M B. Analysis of x-ray scattering from human AA fibrils using secondary structure predictions of human SAA. Proceedings of the IV International Symposium of Amyloidosis, G G Glenner, E F Osserman, E P Benditt, E Calkins, A S Cohen, D Zucker-Franklin. Plenum Press, New York and London 1986; 49–56
   Google Scholar
• Stevens F J. Hypothetical structure of human serum amyloid A protein. Amyloid J Protein Folding Disord 2004; 11: 71–80
   PubMed Web of Science ®Google Scholar
• Segrest J P, Garber D W, Brouillette C G, Harvey S C, Anantharamaiah G M. The amphipathic alpha helix: A multifunctional structural motif in plasma apolipoproteins. Adv Protein Chem 1994; 45: 303–369
   PubMedGoogle Scholar
• Eriksen N, Benditt E P. Serum amyloid A (ApoSAA) and lipoproteins. Methods Enzymol 1986; 128: 311–320
   PubMed Web of Science ®Google Scholar
• Elimova E, Kisilevsky R, Ancsin J B. Mapping the surface residues on HDL-associated serum amyloid A reveals significant differences between the two major isoforms. Amyloid and Amyloidosis, G Grateau, R Kyle, M Skinner. CRC Press, New York 2005; 197–199
   Google Scholar
• van der Westhuyzen D R, Cai L, De Beer M C, de Beer F C. Serum amyloid a promotes cholesterol efflux mediated by scavenger receptor B-I. J Biol Chem 2005; 280: 35890–35895
   PubMed Web of Science ®Google Scholar
• Hatanaka E, Furlaneto C J, Ribeiro F P, Souza G M, Campa A. Serum amyloid A-induced mRNA expression and release of tumor necrosis factor-alpha (TNF-alpha) in human neutrophils. Immunol Lett 2004; 91: 33–37
   PubMed Web of Science ®Google Scholar