Serum amyloid A is present in the capillaries and microinfarcts of hypertensive monkey brain: An immunohistochemical study

References

• Eriksen N, Meek R L, Benditt E P. The SAA lipoprotein family. Acute Phase Proteins: Molecular Biology, Biochemistry and Clinical Applications, A Mackiewitz, I H Kushner Baumann. CRC Press, Boca Raton, FL 1993; 93–106
   Google Scholar
• Hoffman J S, Benditt E P. Changes of high density lipoprotein content following endotoxin administration in the mouse: formation of serum amyloid protein-rich subtractions. J Biol Chem 1982; 257: 10510–10517
   PubMed Web of Science ®Google Scholar
• Kushner I. The phenomenon of the acute phase response. Ann NY Acad Sci 1982; 389: 39–48
   PubMed Web of Science ®Google Scholar
• Husbey G, Marhaug G, Dowton B, Sletten K, Sipe J D. Serum amyloid A (SAA): biochemistry, genetics and the pathogenesis of AA amyloidosis. Amyloid Int J Exp Clin Invest 1994; 1: 119–137
   Google Scholar
• Steel D M, Whitehead A S. The major acute phase reactants: C-reactive protein, serum amyloid P component and serum amyloid A protein. Immunol Today 1994; 15: 81–88
   PubMedGoogle Scholar
• Berts J C, Edbrooke M R, Thakker R V, 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
   PubMedGoogle Scholar
• Raynes J G, Eagling S, McAdam K P. Acute-phase protein synthesis in human hepatoma cells. Differential regulation of serum amyloid A (SAA) and haptoglobin by interleukin-1 and interleukin-6. Clin Exp Immunol 1991; 83: 488–491
   PubMed Web of Science ®Google Scholar
• Grehan S, Uhlar C M, Sim R B, Herbert J, Whitehead A S. Expression of a biologically active recombinant mouse IL-1 receptor antagonist and its use in vivo to modulate aspects of the acute phase response. J Immunol 1997; 159: 369–78
   PubMed Web of Science ®Google Scholar
• Jiang S L, Lozanski G, Samols D, Kushner I. Induction of human serum amyloid A in Hep 3B cells by IL-6 and JL-1 beta involves both transcriptional and post-transcrip-tional mechanisms. J Immunol 1995; 154: 825–31
   PubMedGoogle Scholar
• Lozanski G, Jiang S L, Samols D, Kushner I. C-reactive protein and serum amyloid A mRNA stability following induction by cytokines. Cytokine 1996; 8: 534–40
   PubMedGoogle Scholar
• Rokita H, Loose L D, Bartle L M, Sipe J D. Synergism of interleukin-1 and interleukin- 6 induces serum amyloid A production while depressing fibrinogen: a quantative analysis. J Rheumatology 1994; 21: 400–405
   PubMed Web of Science ®Google Scholar
• Rygg M. Cytokine-induced differential expression of serum amyloid A genes in fetal and neonatal rabbits. Clinical & Experimental Immunology 1996; 103: 335–42
   PubMedGoogle Scholar
• Meek R L, Benditt E P. Rat tissues express serum amyloid A protein-related mRNAs. Proc Natl Acad Sci USA 1989; 86: 1890–1894
   PubMed Web of Science ®Google Scholar
• Meek R L, Urieli-Shoval S, Benditt E P. Expression of apolipo-protein serum amyloid A mRNA in human atherosclerotic lesions and cultured vascular cells: implications for serum amyloid A function. Proc Natl Acad Sci USA 1994; 91: 3186–3190
   PubMed Web of Science ®Google Scholar
• Ramadori R G, Sipe J D, Colten H R. Expression and regulation of the murine serum amyloid A (SAA) gene in extrahepatic sites. J Immunol 1985; 135: 3645–3647
   PubMed Web of Science ®Google Scholar
• Webb C F, Tucker P W, Dowton S B. Expression and sequence analysis of serum amyloid A in the Syrian hamster. Biochemistry 1989; 28: 4785–4790
   PubMedGoogle Scholar
• Aldo-Benson M A, Benson M D. SAA suppression of immune response in vitro: evidence for an effect on T cell-macrophage interaction. J Immunol 1982; 128: 2390–2392
   PubMed Web of Science ®Google Scholar
• Brinckerhoff C E, Mitchell T I, Karmilowicz M J, Kluve-Beckerman B, Benson M D. Autocrine induction of collagenase by serum amyloid A-like and B2-microplugin-like proteins. Science 1989; 243: 655–657
   PubMed Web of Science ®Google Scholar
• Zimlichman S, Danon A, Nathan I, Mozes G, Shainkin-Kestenbaum R. Serum amyloid A, an acute phase protein, inhibits platelet activation. J Lab Med 1990; 116: 180–186
   PubMed Web of Science ®Google Scholar
• Baumberger C, Ulevitch R J, Dayer J M. Modulation of endotoxic activity of lipopolysaccharide by high density lipoprotein. Pathobiology 1991; 59: 378–383
   PubMed Web of Science ®Google Scholar
• Linke R P, 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
   PubMed 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
• Preciado-Patt L, 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
   PubMedGoogle Scholar
• Badolato R, Wang J M, Murphy W J, Lloyd A R, Michiel D F, Bausserman L L, Kevin D J, Oppenheim J J. 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
   PubMed Web of Science ®Google Scholar
• Hardardottir I, Sipe J D, Moser A H, Fielding C J, Feingold K R, Grunfeld C. LPS and cytokines regulate extra hepatic mRNA levels of apolipoproteins during the acute phase response in Syrian hamster. Biochim Biophys Acta 1977; 1344: 210–220
   Google Scholar
• Liang J S, Sloane J A, Wells J M, Abraham C R, Fine R E, Sipe J D. Evidence for local production of acute phase response apolipoprotein serum amyloid A in Alzheimer's disease brain. Neuroscience Lett 1997; 225: 73–76
   PubMed Web of Science ®Google Scholar
• Elias M F, Wolf P A, D'Agostino R B, Cobb G, White L R. Untreated blood pressure level is inveresely related to cognitive functioning: the Framingham study. Am J Epidemiol 1993; 138: 353–364
   PubMed Web of Science ®Google Scholar
• Waldstein S R. Hypertension and neuropsychological function: a lifespan perspective. Exp Aging Res 1995; 21: 321–352
   PubMed Web of Science ®Google Scholar
• Kemper T L, Moss M B, Hollander W, Prusty S. Microinfraction as a result of hypertension in a primate model of cerebrovascular disease. Acta Neuropath 1999; 98: 295–303
   PubMedGoogle Scholar
• Moss M B, Rosene D L, Kemper T L, Prusty S, Hollander W. Hypertension-induced memory impairment and microinfraction in monkeys. Soc Neurosci Abstr 1993; 19: 196
   Google Scholar
• Moss M B. Innovative Animal Models of CNS Diseases: From molecule to therapy, D F Emerich, E L Dean. Humana Press. 1999, A primate model of hypertensive cerebrovascular disease. In: (Eds), Totowa N.J., (in press)
   Google Scholar
• Hollander W, Madoff I, Paddock J, Kirkpatrick B. Aggravation of atherosclerosis by hypertension in a subhuman primate model with coarctation of the aorta. Circ Res 1976; 38 (Suppl II): 63–72
   Google Scholar
• Hollander W, Prusty S, Kirkpatrick B, Paddock J, Nagrai S. Role of hypertension in ischemic heart disease and cerebral vascular disease in the cynomolgus monkey with coarctation of the aorta. Circ Res 1977; 40 (Suppl I), I-70-I-83
   Google Scholar
• Godenir N L, Jeenah M S, Coetzee G A, van der Westhuyzen D R, Strachan A F, de Beer F C. Standardization of the quantitation of serum amyloid A protein (SAA) in human serum. J Immunol Methods 1985; 83: 217–225
   PubMed Web of Science ®Google Scholar
• Urieli-Shoval S, Meek R L, Hanson R H, Eriksen N, Benditt E P. Human serum amyloid A genes are expressed in monocyte/macrophage cell lines. Am J Pathol 1994; 145: 650–660
   PubMed Web of Science ®Google Scholar
• Chu C J, Lee F Y, Chang F Y, Wang S S, Lin H C, Wu S L, Tai C C, Lee S D. Hyperdynamic circulation in prehe-patic portal hypertension: role of tumor necrosis factor-alpha. Chung Hua i Hsueh Tsa Chih- Chinese Medical J 1997; 59: 145–50
   Google Scholar
• Kawai Y, Matsumoto Y, Watanabe K, Yamamoto H, Satoh K, Murata M, Handa M, Ikeda Y. Hemodynamic forces modulate the effects of cytokines on fibrinolytic activity of endothelial cells. Blood 1996; 87: 2314–21
   PubMed Web of Science ®Google Scholar
• Kuehn B E, Hoff W J, Wallock M E. Cardiopulmonary bypass with adequate flow and perfusion pressures prevents endotoxaemia and pathologic cytokine production. Perfusion 1995; 10: 27–31
   PubMedGoogle Scholar
• Nerem R M, Alexander R W, Chapell D C, Medford R M, Varner S E, Taylor W R. The study of the influence of flow on vascular endothelial biology. Am J Med Sciences 1998; 316: 169–75
   PubMed Web of Science ®Google Scholar
• Bouloumine A, Bauersachs J, Linz W. Endothelial dysfunction coincides with an enhanced nitric oxide synthase expression and superoxide anion production. Hypertension 1997; 30: 1628–1633
   PubMedGoogle Scholar
• Chou T ZC, Yen M-H, Li C-Y. Alterations to nitric oxide synthase expression with aging and hypertension. Hypertension 1998; 31: 643–648
   PubMed Web of Science ®Google Scholar
• Kontos H A, Wei E P, Navari R M. Responses of cerebral arteries and arterioles to acute hypotension and hypertension. Am J Physio. 1978; 234: H371–383
   Google Scholar
• Kontos H A. Oxygen radicals in cerebral vascular injury. Circ Res 1985; 57: 508–516
   PubMed Web of Science ®Google Scholar
• Singh A, Sventek P, Lariviere R, Thibault G, Schiffrin E L. Inductible nitric oxide synthase in vascular smooth muscle cells from prehypertensive spontaneously hypertensive rats. Am J Hypertension 1996; 9: 867–77
   PubMed Web of Science ®Google Scholar
• Keffer J, Probert L, Cazlaris H, Georgopoulos S, Kioussis D, Kollias G. Transgenic mice expressing human tumor necrosis factor, a predictive genetic model of arthritis. EMBO J 1991; 10: 4025–4031
   PubMed Web of Science ®Google Scholar
• Schwab J H, Anderle S K, Brown R R, Dalldorf F G, Thompson R C. Pro-and anti-inflammatory roles of interleukin-1 in recurrence of bacterial cell wall-induced arthritis in rats. Infect Immun 1991; 59: 4436–4442
   PubMed Web of Science ®Google Scholar
• Sipe J D. Amyloidosis. Annu Rev Biochem 1992; 61: 947–975
   PubMed Web of Science ®Google Scholar
• Liang J S, Schreiber B M, Salmona M, Phillip G, Gonnerman W A, de Beer F C, Sipe J D. Amino terminal region of acute phase, but not constitutive, serum amyloid A (apoSAA) specifically binds and transports cholesterol into aortic smooth muscle and Hep G2 cells. J Lipid Res 1996; 37: 2109–2116
   PubMed Web of Science ®Google Scholar
• Schreiber B M, Veverbrants M, Fine R E, Blusztajn J K, Salmona M, Patel A, Sipe J D. Apolipoprotein serum amyloid A (SAA) down regulates smooth muscle cell lipid biosynthesis. J Biochem 1999; 344: 7–13
   Google Scholar