Pattern Recognition by Pentraxins

  • Alok Agrawal
  • Prem Prakash Singh
  • Barbara Bottazzi
  • Cecilia Garlanda
  • Alberto Mantovani
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 653)


Pentraxins are a family of evolutionarily conserved pattern-recognition proteins that are made up of five identical subunits. Based on the primary structure of the subunit, the pentraxins are divided into two groups: short pentraxins and long pentraxins. C-reactive protein (CRP) and serum amyloid P-component (SAP) are the two short pentraxins. The prototype protein of the long pentraxin group is pentraxin 3 (PTX3). CRP and SAP are produced primarily in the liver while PTX3 is produced in a variety of tissues during inflammation. The main functions of short pentraxins are to recognize a variety of pathogenic agents and then to either eliminate them or neutralize their harmful effects by utilizing the complement pathways and macrophages in the host. CRP binds to modified low-density lipoproteins, bacterial polysaccharides, apoptotic cells, and nuclear materials. By virtue of these recognition functions, CRP participates in the resolution of cardiovascular, infectious, and autoimmune diseases. SAP recognizes carbohydrates, nuclear substances, and amyloid fibrils and thus participates in the resolution of infectious diseases, autoimmunity, and amyloidosis. PTX3 interacts with several ligands, including growth factors, extracellular matrix component and selected pathogens, playing a role in complement activation and facilitating pathogen recognition by phagocytes. In addition, data in gene-targeted mice show that PTX3 is essential in female fertility, participating in the assembly of the cumulus oophorus extracellular matrix. PTX3 is therefore a nonredundant component of the humoral arm of innate immunity as well as a tuner of inflammation. Thus, in conjunction with the other components of innate immunity, the pentraxins use their pattern-recognition property for the benefit of the host.


Hyaluronic Acid Serum Amyloid Classical Complement Pathway PTX3 Plasma Level Human Serum Amyloid 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


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  1. 1.
    Garlanda C, Bottazzi B, Bastone A et al. Pentraxins at the crossroads between innate immunity, inflammation, matrix deposition, and female fertility. Annu Rev Immunol 2005; 23:337–366.PubMedCrossRefGoogle Scholar
  2. 2.
    Agrawal A. CRP after 2004. Mol Immunol 2005; 42:927–930.PubMedCrossRefGoogle Scholar
  3. 3.
    Volanakis JE. Human C-reactive protein: Expression, structure, and function. Mol Immunol 2001; 38:189–197.PubMedCrossRefGoogle Scholar
  4. 4.
    Black S, Kushner I, Samols D. C-reactive protein. J Biol Chem 2004; 279:48487–48490.PubMedCrossRefGoogle Scholar
  5. 5.
    Skinner M, Cohen AS. Amyloid P component. Methods Enzymol 1988; 163:523–536.PubMedCrossRefGoogle Scholar
  6. 6.
    Osmand AP, Friedenson B, Gewurz H et al. Characterization of C-reactive protein and the complement subcomponent C1t as homologous proteins displaying cyclic pentameric symmetry (pentraxins). Proc Natl Acad Sci USA 1977; 74:739–743.PubMedCrossRefGoogle Scholar
  7. 7.
    Tillett WS, Francis Jr T. Serological reactions in pneumonia with a nonprotein somatic fraction of pneumococcus. J Exp Med 1930; 52:561–571.PubMedCrossRefGoogle Scholar
  8. 8.
    Hirschfield GM, Pepys MB. C-reactive protein and cardiovascular disease: New insights from an old molecule. QJM 2003; 96:793–807.PubMedCrossRefGoogle Scholar
  9. 9.
    Cathcart ES, Comerford FR, Cohen AS. Immunological studies on a protein extracted from human secondary amyloid. New Engl J Med 1965; 273:143–146.PubMedCrossRefGoogle Scholar
  10. 10.
    Pepys MB, Rademacher TW, Amatayakul-Chantler S et al. Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure. Proc Natl Acad Sci USA 1994; 91:5602–5606.PubMedCrossRefGoogle Scholar
  11. 11.
    Whitehead AS, Zahedi K, Rits M et al. Mouse C-reactive protein: Generation of cDNA clones, structural analysis, and induction of mRNA during inflammation. Biochem J 1990; 266:283–290.PubMedGoogle Scholar
  12. 12.
    Pepys MB, Dash AC, Fletcher TC et al. Analogues in other mammals and in fish of human plasma proteins, C-reactive protein and amyloid P component. Nature 1978; 273:168–170.PubMedCrossRefGoogle Scholar
  13. 13.
    Ying SC, Marchalonis JJ, Gewurz AT et al. Reactivity of anti-human C-reactive protein and serum amyloid P component monoclonal antibodies with limulin and pentraxins of other species. Immunology 1992; 76:324–330.PubMedGoogle Scholar
  14. 14.
    Nguyen NY, Suzuki A, Boykins RA et al. The amino acid sequence of Limulus C-reactive protein: Evidence of polymorphism. J Biol Chem 1986; 261:10456–10465.PubMedGoogle Scholar
  15. 15.
    Agrawal A, Mitra S, Ghosh N et al. C-reactive protein in hemolymph of a mollusc, Achatina fulica Bowdich. Indian J Exp Biol 1990; 28:788–789.PubMedGoogle Scholar
  16. 16.
    De Beer FC, Baltz ML, Munn EA et al. Isolation and characterization of C-reactive protein and serum amyloid P component in the rat. Immunology 1982; 45:55–70.PubMedGoogle Scholar
  17. 17.
    Hurlimann J, Thorbecke GJ, Hochwald GM. The liver as the site of C-reactive protein formation. J Exp Med 1966; 123:365–378.PubMedCrossRefGoogle Scholar
  18. 18.
    Ganapathi MK, Rzewnicki D, Samols D et al. Effect of combinations of cytokines and hormones on synthesis of serum amyloid A and C-reactive protein in Hep3B cells. J Immunol 1991; 147:1261–1265.PubMedGoogle Scholar
  19. 19.
    Agrawal A, Samols D, Kushner I. Transcription factor c-Rel enhances C-reactive protein expression by facilitating the binding of C/EBPβ to the promoter. Mol Immunol 2003; 40:373–380.PubMedCrossRefGoogle Scholar
  20. 20.
    Voleti B, Agrawal A. Regulation of basal and induced expression of C-reactive protein through an overlapping element for OCT-1 and NF-κB on the proximal promoter. J Immunol 2005; 175:3386–3390.PubMedGoogle Scholar
  21. 21.
    Voleti B, Agrawal A. Statins and nitric oxide reduce C-reactive protein production while inflammatory conditions persist. Mol Immunol 2006; 43:891–896.PubMedCrossRefGoogle Scholar
  22. 22.
    Gould JM, Weiser JN. Expression of C-reactive protein in the human respiratory tract. Infect Immun 2001; 69:1747–1754.PubMedCrossRefGoogle Scholar
  23. 23.
    Jabs WJ, Busse M, Kruger S et al. Expression of C-reactive protein by renal cell carcinomas and unaffected surrounding renal tissue. Kidney Int 2005; 68:2103–2110.PubMedCrossRefGoogle Scholar
  24. 24.
    Szalai AJ, Van Ginkel FW, Dalrymple SA et al. Testosterone and IL-6 requirements for human C-reactive protein gene expression in transgenic mice. J Immunol 1998; 160:5294–5299.PubMedGoogle Scholar
  25. 25.
    Coe JE, Ross MJ. Amyloidosis and female protein in the Syrian hamster: Concurrent regulation by sex hormones. J Exp Med 1990; 171:1257–1267.PubMedCrossRefGoogle Scholar
  26. 26.
    Vigushin DM, Pepys MB, Hawkins PN. Metabolic and scintigraphic studies of radioiodinated human C-reactive protein in health and disease. J Clin Invest 1993; 91:1351–1357.PubMedCrossRefGoogle Scholar
  27. 27.
    Hawkins PN, Wootten R, Pepys MB. Metabolic studies of radioiodinated serum amyloid P component in normal subjects and patients with systemic amyloidosis. J Clin Invest 1990; 86:1862–1869.PubMedCrossRefGoogle Scholar
  28. 28.
    Gotschlich EC, Edelman GM. C-reactive protein: A molecule composed of subunits. Proc Natl Acad Sci USA 1965; 54:558–566.PubMedCrossRefGoogle Scholar
  29. 29.
    Oliveria EB, Gotschlich EC, Liu TY. Primary structure of human C-reactive protein. J Biol Chem 1979; 254:489–502.Google Scholar
  30. 30.
    Shrive AK, Cheetham GM, Holden D et al. Three-dimensional structure of human C-reactive protein. Nature Struct Biol 1996; 3:346–354.PubMedCrossRefGoogle Scholar
  31. 31.
    Hamazaki H. Structure and significance of N-linked sugar unit of human serum amyloid P component. Biochim Biophys Acta 1990; 1037:435–438.PubMedGoogle Scholar
  32. 32.
    Emsley J, White HE, O’Hara BP et al. Structure of pentameric human serum amyloid P component. Nature 1994; 367:338–345.PubMedCrossRefGoogle Scholar
  33. 33.
    Sørensen IJ, Andersen O, Nielsen EH et al. Native human serum amyloid P component is a single pentamer. Scand J Immunol 1995; 41:263–267.PubMedCrossRefGoogle Scholar
  34. 34.
    Abernethy TJ, Avery OT. The occurrence during acute infections of a protein not normally present in the blood. I. Distribution of the reactive protein in patients’ sera and the effect of calcium on the flocculation reaction with C-polysaccharide of pneumococcus. J Exp Med 1941; 73:173–182.PubMedCrossRefGoogle Scholar
  35. 35.
    Kinoshita CM, Ying SC, Hugli TE et al. Elucidation of a protease-sensitive site involved in the binding of calcium to C-reactive protein. Biochemistry 1989; 28:9840–9848.PubMedCrossRefGoogle Scholar
  36. 36.
    Volanakis JE, Kaplan MH. Specificity of C-reactive protein for choline phosphate residues of pneumococcal C-polysaccharide. Proc Soc Exp Biol Med 1971; 136:612–614.PubMedGoogle Scholar
  37. 37.
    Nauta AJ, Daha MR, Van Kooten C et al. Recognition and clearance of apoptotic cells: A role for complement and pentraxins. Trends Immunol 2003; 24:148–154.PubMedCrossRefGoogle Scholar
  38. 38.
    Thompson D, Pepys MB, Wood SP. The physiological structure of human C-reactive protein and its complex with phosphocholine. Structure 1999; 7:169–177.PubMedCrossRefGoogle Scholar
  39. 39.
    Agrawal A, Xu Y, Ansardi D et al. Probing the phosphocholine-binding site of human C-reactive protein by site-directed mutagenesis. J Biol Chem 1992; 267:25352–25358.Google Scholar
  40. 40.
    Agrawal A, Lee S, Carson M et al. Site-directed mutagenesis of the phosphocholine-binding site of human C-reactive protein: Role of Thr76 and Trp67. J Immunol 1997; 158:345–350.PubMedGoogle Scholar
  41. 41.
    Agrawal A, Simpson MJ, Black S et al. A C-reactive protein mutant that does not bind to phosphocholine and pneumococcal C-polysaccharide. J Immunol 2002; 169:3217–3222.PubMedGoogle Scholar
  42. 42.
    Kinoshita CM, Gewurz AT, Siegel JN et al. A protease-sensitive site in the proposed Ca2+-binding region of human serum amyloid P component and other pentraxins. Protein Sci 1992; 1:700–709.PubMedCrossRefGoogle Scholar
  43. 43.
    Bijl M, Horst G, Bijzet J et al. Serum amyloid P component binds to late apoptotic cells and mediates their uptake by monocyte-derived macrophages. Arthrit Rheumat 2003; 48:248–254.CrossRefGoogle Scholar
  44. 44.
    Christner RB, Mortensen RF. Specificity of the binding interaction between human serum amyloid P-component and immobilized human C-reactive protein. J Biol Chem 1994; 269:9760–9766.PubMedGoogle Scholar
  45. 45.
    Aquilina JA, Robinson CV. Investigating interactions of the pentraxins serum amyloid P component and C-reactive protein by mass spectrometry. Biochem J 2003; 375:323–328.PubMedCrossRefGoogle Scholar
  46. 46.
    Mold C, Rodgers CP, Kaplan RL et al. Binding of human C-reactive protein to bacteria. Infect Immun 1982; 38:392–395.PubMedGoogle Scholar
  47. 47.
    De Beaufort AJ, Langermans JAM, Matze-Van Der Lans AM et al. Difference in binding of killed and live Streptococcus pneumoniae serotypes by C-reactive protein. Scand J Immunol 1997; 46:597–600.PubMedCrossRefGoogle Scholar
  48. 48.
    Weiser JN, Pan M, McGowan KL et al. Phosphorylcholine on the lipopolysaccharide of Haemophilus influenzae contributes to persistence in the respiratory tract and sensitivity to serum killing mediated by C-reactive protein. J Exp Med 1998; 187:631–640.PubMedCrossRefGoogle Scholar
  49. 49.
    Serino L, Virji M. Genetic and functional analysis of the phosphorylcholine moiety of commensal Neisseria lipopolysaccharide. Mol Microbiol 2002; 43:437–448.PubMedCrossRefGoogle Scholar
  50. 50.
    Kindmark CO. Stimulating effect of C-reactive protein on phagocytosis of various species of pathogenic bacteria. Clin Exp Immunol 1971; 8:941–948.PubMedGoogle Scholar
  51. 51.
    Yother J, Volanakis JE, Briles DE. Human C-reactive protein is protective against fatal Streptococcus pneumoniae infection in mice. J Immunol 1982; 128:2374–2376.PubMedGoogle Scholar
  52. 52.
    Mold C, Nakayama S, Holzer TJ et al. C-reactive protein is protective against Streptococcus pneumoniae infection in mice. J Exp Med 1981; 154:1703–1708.PubMedCrossRefGoogle Scholar
  53. 53.
    Szalai AJ, Briles DE, Volanakis JE. Human C-reactive protein is protective against fatal Streptococcus pneumoniae infection in transgenic mice. J Immunol 1995; 155:2557–2563.PubMedGoogle Scholar
  54. 54.
    Szalai AJ. The antimicrobial activity of C-reactive protein. Microbes Infect 2002; 4:201–205.PubMedCrossRefGoogle Scholar
  55. 55.
    Szalai AJ, VanCott JL, McGhee JR et al. Human C-reactive protein is protective against fatal Salmonella enterica serovar typhimurium infection in transgenic mice. Infect Immun 2000; 68:5652–5656.PubMedCrossRefGoogle Scholar
  56. 56.
    De Haas CJC, van Leeuwen EMM, Van Bommel T et al. Serum amyloid P component bound to Gram-negative bacteria prevents lipopolysaccharide-mediated classical pathway complement activation. Infect Immun 2000; 68:1753–1759.PubMedCrossRefGoogle Scholar
  57. 57.
    De Haas CJC, Van Der Tol ME, Van Kessel KPM et al. A synthetic lipopolysaccharide-binding peptide based on amino acids 27–39 of serum amyloid P component inhibits lipopolysaccharide-induced responses in human blood. J Immunol 1998; 161:3607–3615.PubMedGoogle Scholar
  58. 58.
    De Haas CJC, Van Der Zee R, Benaissa-Trouw B et al. Lipopolysaccharide (LPS)-binding synthetic peptides derived from serum amyloid P component neutralize LPS. Infect Immun 1999; 67:2790–2796.PubMedGoogle Scholar
  59. 59.
    Noursadeghi M, Bickerstaff MC, Gallimore JR et al. Role of serum amyloid P component in bacterial infection: Protection of the host or protection of the pathogen. Proc Natl Acad Sci USA 2000; 97:14584–14589.PubMedCrossRefGoogle Scholar
  60. 60.
    Van Molle W, Hochepied T, Brouckaert P et al. The major acute-phase protein, serum amyloid P component, in mice is not involved in endogenous resistance against tumor necrosis factor alpha-induced lethal hepatitis, shock, and skin necrosis. Infect Immun 2000; 68:5026–5029.PubMedCrossRefGoogle Scholar
  61. 61.
    Singh PP, Gervais F, Skamene E et al. Serum amyloid P-component-induced enhancement of macrophage listericidal activity. Infect Immun 1986; 52:688–694.PubMedGoogle Scholar
  62. 62.
    De Beer FC, Soutar AK, Baltz ML et al. Low density lipoprotein and very low density lipoprotein are selectively bound by aggregated C-reactive protein. J Exp Med 1982; 156:230–242.PubMedCrossRefGoogle Scholar
  63. 63.
    Bhakdi S, Torzewski M, Klouche M et al. Complement and atherogenesis: Binding of CRP to degraded, nonoxidized LDL enhances complement activation. Arterioscler Thromb Vasc Biol 1999; 19:2348–2354.PubMedGoogle Scholar
  64. 64.
    Chang MK, Binder CJ, Torzewski M et al. C-reactive protein binds to both oxidized LDL and apoptotic cells through recognition of a common ligand: Phosphorylcholine of oxidized phospholipids. Proc Natl Acad Sci USA 2002; 99:13043–13048.PubMedCrossRefGoogle Scholar
  65. 65.
    Taskinen S, Kovanen PT, Jarva H et al. Binding of C-reactive protein to modified low-density-lipoprotein particles: Identification of cholesterol as a novel ligand for C-reactive protein. Biochem J 2002; 367:403–412.PubMedCrossRefGoogle Scholar
  66. 66.
    Reynolds GD, Vance RP. C-reactive protein immunohistochemical localization in normal and atherosclerotic human aortas. Arch Pathol Lab Med 1987; 111:265–269.PubMedGoogle Scholar
  67. 67.
    Sun H, Koike T, Ichikawa T et al. C-reactive protein in atherosclerotic lesions: Its origin and pathophysiological significance. Am J Pathol 2005; 167:1139–1148.PubMedGoogle Scholar
  68. 68.
    Bhakdi S, Torzewski M, Paprotka K et al. Possible protective role for C-reactive protein in atherogenesis: Complement activation by modified lipoproteins halts before detrimental terminal sequence. Circulation 2004; 109:1870–1876.PubMedCrossRefGoogle Scholar
  69. 69.
    Hirschfield GM, Gallimore JR, Kahan MC et al. Transgenic human C-reactive protein is not proatherogenic in apolipoprotein E-deficient mice. Proc Natl Acad Sci USA 2005; 102:8309–8314.PubMedCrossRefGoogle Scholar
  70. 70.
    Reifenberg K, Lehr HA, Baskal D et al. Role of C-reactive protein in atherogenesis: Can the apolipoprotein E knockout mouse provide the answer? Arterioscler Thromb Vasc Biol 2005; 25:1641–1646.PubMedCrossRefGoogle Scholar
  71. 71.
    Trion A, De Maat MP, Jukema JW et al. No effect of C-reactive protein on early atherosclerosis development in apolipoprotein E*3-leiden/human C-reactive protein transgenic mice. Arterioscler Thromb Vasc Biol 2005; 25:1635–1640.PubMedCrossRefGoogle Scholar
  72. 72.
    Schwedler SB, Amann K, Wernicke K et al. Native C-reactive protein increases whereas modified C-reactive protein reduces atherosclerosis in apolipoprotein E-knockout mice. Circulation 2005; 112:1016–1023.PubMedCrossRefGoogle Scholar
  73. 73.
    Libby P, Ridker PM. Inflammation and atherosclerosis: Role of C-reactive protein in risk assessment. Am J Med 2004; 116:9S–16S.PubMedCrossRefGoogle Scholar
  74. 74.
    Gitlin JD, Gitlin JI, Gitlin D. Localization of C-reactive protein in synovium of patients with rheumatoid arthritis. Arthrit Rheum 1977; 20:1491–1499.CrossRefGoogle Scholar
  75. 75.
    Robey FA, Jones KD, Tanaka T et al. Binding of C-reactive protein to chromatin and nucleosome core particles: A possible physiological role of C-reactive protein. J Biol Chem 1984; 259:7311–7316.PubMedGoogle Scholar
  76. 76.
    Du Clos TW. The interaction of C-reactive protein and serum amyloid P component with nuclear antigens. Mol Biol Rep 1996; 23:253–260.PubMedCrossRefGoogle Scholar
  77. 77.
    Shephard EG, Smith PJ, Coetzee S et al. Pentraxin binding to isolated rat liver nuclei. Biochem J 1991; 279:257–262.PubMedGoogle Scholar
  78. 78.
    Butler PJG, Tennent GA, Pepys MB. Pentraxin-chromatin interactions: Serum amyloid P component specifically displaces H1-type histones and solubilizes native long chromatin. J Exp Med 1999; 172:13–18.CrossRefGoogle Scholar
  79. 79.
    Pepys MB, Butler PJG. Serum amyloid P component is the major calcium-dependent specific DNA binding protein of the serum. Biochem Biophys Res Comm 1987; 148:308–313.PubMedCrossRefGoogle Scholar
  80. 80.
    Breathnach SM, Kofler H, Sepp N et al. Serum amyloid P component binds to cell nuclei in vitro and to in vivo deposits of extracellular chromatin in systemic lupus erythematosus. J Exp Med 1989; 170:1433–1438.PubMedCrossRefGoogle Scholar
  81. 81.
    DuClos TW, Mold C, Stump RF. Identification of a polypeptide sequence that mediates nuclear localization of the acute phase protein C-reactive protein. J Immunol 1990; 145:3869–3875.Google Scholar
  82. 82.
    DuClos TW, Zlock LT, Hicks PS et al. Decreased autoantibody levels and enhanced survival of (NZB x NZW) F1 mice treated with C-reactive protein. Clin Immunol Immunopathol 1994; 70:22–27.CrossRefGoogle Scholar
  83. 83.
    Rodriguez W, Mold C, Kataranovski M et al. Reversal of ongoing proteinuria in autoimmune mice by treatment with C-reactive protein. Arthritis Rheum 2005; 52:642–650.PubMedCrossRefGoogle Scholar
  84. 84.
    Szalai AJ, Weaver CT, McCrory MA et al. Delayed lupus onset in (NZB x NZW) F1 mice expressing a human C-reactive protein transgene. Arthritis Rheum 2003; 48:1602–1611.PubMedCrossRefGoogle Scholar
  85. 85.
    Kottgen E, Hell B, Kage A et al. Lectin specificity and binding characteristics of human C-reactive protein. J Immunol 1992; 149:445–453.PubMedGoogle Scholar
  86. 86.
    Brown MR, Anderson BE. Receptor-ligand interactions between serum amyloid P component and model soluble immune complexes. J Immunol 1993; 151:2087–2095.PubMedGoogle Scholar
  87. 87.
    Bickerstaff MCM, Botto M, Hutchinson WL et al. Serum amyloid P component controls chromatin degradation and prevents antinuclear autoimmunity. Nature Med 1999; 5:694–697.PubMedCrossRefGoogle Scholar
  88. 88.
    Soma M, Tamaoki T, Kawano H et al. Mice lacking serum amyloid P component do not necessarily develop severe autoimmune disease. Biochem Biophys Res Comm 2001; 286:200–205.PubMedCrossRefGoogle Scholar
  89. 89.
    Potempa LA, Siegel JN, Gewurz H. Binding reactivity of C-reactive protein for polycations. II. Modulatory effects of calcium and phosphocholine. J Immunol 1981; 127:1509–1514.PubMedGoogle Scholar
  90. 90.
    Salonen EM, Vartio T, Hedman K et al. Binding of fibronectin by the acute phase reactant C-reactive protein. J Biol Chem 1984; 259:1496–1501.PubMedGoogle Scholar
  91. 91.
    Tseng J, Mortensen RF. Binding of human C-reactive protein to plasma fibronectin occurs via the phosphorylcholine-binding site. Mol Immunol 1988; 25:679–686.PubMedCrossRefGoogle Scholar
  92. 92.
    Suresh MV, Singh SK, Agrawal A. Interaction of calcium-bound C-reactive protein with fibronectin is controlled by pH: In vivo implications. J Biol Chem 2004; 279:52552–52557.PubMedCrossRefGoogle Scholar
  93. 93.
    Tseng J, Mortensen RF. Binding specificity of mouse serum amyloid P-component for fibronectin. Immunol Invest 1986; 15:749–761.PubMedCrossRefGoogle Scholar
  94. 94.
    Barna BP, Eppstein DA, Thomassen MJ et al. Therapeutic effects of a synthetic peptide of C-reactive protein in preclinical tumor models. Cancer Immunol Immunother 1993; 36:171–176.PubMedCrossRefGoogle Scholar
  95. 95.
    Higgenbotham JD, Heidelberger M, Gotschlich EC. Degradation of a pneumococcal type-specific polysaccharide with exposure of group-specificity. Proc Natl Acad Sci USA 1970; 67:138–142.CrossRefGoogle Scholar
  96. 96.
    Kempka G, Toos PH, Kolb-Bachofen V. A membrane-associated form of C-reactive protein is the galactose-specific particle receptor on rat liver macrophages. J Immunol 1990; 144:1004–1009.PubMedGoogle Scholar
  97. 97.
    Baldo BA, Fletcher TC, Pepys J. Isolation of a peptide-polysaccharide from the dermatophyte Epidermophyton floccosum and a study of its reaction with human C-reactive protein and mouse anti-phosphorylcholine myeloma serum. Immunology 1977; 32:831–842.PubMedGoogle Scholar
  98. 98.
    Jensen TDB, Schønheyder H, Andersen P et al. Binding of C-reactive protein to Aspergillus fumigatus fractions. J Med Microbiol 1986; 21:173–177.PubMedCrossRefGoogle Scholar
  99. 99.
    Pied S, Nussler A, Pontet M et al. C-reactive protein protects against preerythrocytic stages of malaria. Infect Immun 1989; 57:278–282.PubMedGoogle Scholar
  100. 100.
    Taylor K, Hoole D. Interactions between rat C-reactive protein and adult Hymenolepis diminuta. Parasitology 1997; 115:297–302.PubMedCrossRefGoogle Scholar
  101. 101.
    Pritchard DG, Volanakis JE, Slutski GM et al. C-reactive protein binds Leishmanial excreted factors. Proc Soc Exp Biol Med 1985; 178:500–503.PubMedGoogle Scholar
  102. 102.
    Culley FJ, Harris RA, Kaye PM et al. C-reactive protein binds to a novel ligand on Leishmania donovani and increases uptake into human macrophages. J Immunol 1996; 156:4691–4696.PubMedGoogle Scholar
  103. 103.
    Bee A, Culley FJ, Alkhalife IS et al. Transformation of Leishmania mexicana metacyclic promastigotes to amastigote-like forms mediated by binding of human C-reactive protein. Parasitology 2001; 122:521–529.PubMedCrossRefGoogle Scholar
  104. 104.
    Hind CRK, Collins PM, Baltz ML et al. Human serum amyloid P component, a circulating lectin with specificity for the cyclic 4,6-pyruvate acetal of galactose. Biochem J 1985; 225:107–111.PubMedGoogle Scholar
  105. 105.
    Loveless RW, Floyd-O’Sullivan G, Raynes JG et al. Human serum amyloid P is a multispecific adhesive protein whose ligands include 6-phosphorylated mannose and the 3-sulphated saccharides galactose, M-acetylgalactosamine and glucuronic acid. EMBO J 1992; 11:813–819.PubMedGoogle Scholar
  106. 106.
    Brown MR, Anderson BE. Receptor-ligand interactions between serum amyloid P component and model soluble immune complexes. J Immunol 1993; 151:2087–2095.PubMedGoogle Scholar
  107. 107.
    Li XA, Hatanaka K, Guo L et al. Binding of serum amyloid P component to heparin in human serum. Biochim Biophys Acta 1994; 1201:142–148.Google Scholar
  108. 108.
    Zahedi K. Characterization of the binding of serum amyloid P to type IV collagen. J Biol Chem 1996; 271:14897–14902.PubMedGoogle Scholar
  109. 109.
    Danielsen B, Sørensen IJ, Nybo M et al. Calcium-dependent and-independent binding of the pentraxin serum amyloid P component to glycosaminoglycans and amyloid proteins: Enhanced binding at slightly acid pH. Biochim Biophys Acta 1997; 1339:73–78.PubMedGoogle Scholar
  110. 110.
    Williams EC, Huppert BJ, Asakura S. Neutralization of the anticoagulant effects of glycosaminoglycans by serum amyloid P component: Comparison with other plasma and platelet proteins. J Lab Clin Med 1992; 120:159–167.PubMedGoogle Scholar
  111. 111.
    Meyers K, Smith R, Williams EC. Inhibition of fibrin polymerization by serum amyloid P component and heparin. Thromb Haemost 1987; 57:345–348.Google Scholar
  112. 112.
    Coker AR, Purvis A, Baker D et al. Molecular chaperone properties of serum amyloid P component. FEBS Lett 2000; 473:199–202.PubMedCrossRefGoogle Scholar
  113. 113.
    Filep J, Földes-Filep E. Effects of C-reactive protein on human neutrophil granulocytes challenged with n-formyl-methionyl-leucyl-phenylalanine and platelet-activating factor. Life Sci 1989; 44:517–524.PubMedCrossRefGoogle Scholar
  114. 114.
    Xia D, Samols D. Transgenic mice expressing rabbit C-reactive protein are resistant to endotoxemia. Proc Natl Acad Sci USA 1997; 94:2575–2580.PubMedCrossRefGoogle Scholar
  115. 115.
    Kilpatrick JM, Virella G. Inhibition of platelet-activating factor by rabbit C-reactive protein. Clin Immunol Immunopathol 1985; 37:276–281.PubMedCrossRefGoogle Scholar
  116. 116.
    Vigo C. Effect of C-reactive protein on platelet-activating factor-induced platelet aggregation and membrane stabilization. J Biol Chem 1985; 260:3418–3422.PubMedGoogle Scholar
  117. 117.
    Filep JG, Hermán F, Kelemen E et al. C-reactive protein inhibits binding of platelet-activating factor to human platelets. Thromb Res 1991; 61:411–421.PubMedCrossRefGoogle Scholar
  118. 118.
    Khreiss T, Jozsef L, Potempa LA et al. Opposing effects of CRP isoforms on shear-induced neutrophil-platelet adhesion and neutrophil aggregation in whole blood. Circulation 2004; 110:2713–2720.PubMedCrossRefGoogle Scholar
  119. 119.
    Black S, Wilson A, Samols D. An intact phosphocholine-binding site is necessary for transgenic rabbit C-reactive protein to protect mice against challenge with platelet-activating factor. J Immunol 2005; 175:1192–1196.PubMedGoogle Scholar
  120. 120.
    Bout D, Joseph M, Pontet M et al. Rat resistance to schistosomiasis: Platelet-mediated cytotoxicity induced by C-reactive protein. Science 1986; 231:153–156.PubMedCrossRefGoogle Scholar
  121. 121.
    Kaplan MH, Volanakis JE. Interaction of C-reactive protein complexes with the complement system. I. Consumption of human complement associated with the reaction of C-reactive protein with pneumococcal C-polysaccharide and with the choline phosphatides, lecithin, and sphingomyelin. J Immunol 1974; 112:2135–2147.PubMedGoogle Scholar
  122. 122.
    Siegel J, Rent R, Gewurz H. Interactions of C-reactive protein complexes with the complement system. I. Protamine-induced consumption of complement in acute phase sera. J Exp Med 1974; 140:631–647.PubMedCrossRefGoogle Scholar
  123. 123.
    Berman S, Gewurz H, Mold C. Binding of C-reactive protein to nucleated cells leads to complement activation without cytolysis. J Immunol 1986; 136:1354–1359.PubMedGoogle Scholar
  124. 124.
    Agrawal A, Volanakis JE. Probing the C1q-binding site on human C-reactive protein by site-directed mutagenesis. J Immunol 1994; 152:5404–5410.PubMedGoogle Scholar
  125. 125.
    Agrawal A, Shrive AK, Greenhough TJ et al. Topology and structure of the C1q-binding site on C-reactive protein. J Immunol 2001; 166:3998–4004.PubMedGoogle Scholar
  126. 126.
    Gaboriaud C, Juanhuix J, Gruez A et al. The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J Biol Chem 2003; 278:46974–46982.PubMedCrossRefGoogle Scholar
  127. 127.
    Kishore U, Ghai R, Greenhough TJ et al. Structural and functional anatomy of the globular domain of complement protein C1q. Immunol Lett 2004; 95:113–128.PubMedCrossRefGoogle Scholar
  128. 128.
    Roumenina LT, Ruseva MM, Zlatarova A et al. Interaction of C1q with IgG1, C-reactive protein and pentraxin 3: Mutational studies using recombinant globular head regions of human C1q A, B and C chains. Biochemistry 2006; 45:4093–4104.PubMedCrossRefGoogle Scholar
  129. 129.
    Evans Jr TC, Nelsestuen GL. Dissociation of serum amyloid P from C4b-binding protein and other sites by lactic acid: Potential role of lactic acid in the regulation of pentraxin function. Biochemistry 1995; 34:10440–10447.PubMedCrossRefGoogle Scholar
  130. 130.
    Hicks PS, Saunero-Nava L, Du Clos TW et al. Serum amyloid P component binds to histones and activates the classical complement pathway. J Immunol 1992; 149:3689–3694.PubMedGoogle Scholar
  131. 131.
    Ying SC, Gewurz AT, Jiang H et al. Human serum amyloid P component oligomers bind and activate the classical complement pathway via residues 14–26 and 76–92 of the A chain collagen-like region of C1q. J Immunol 1993; 150:169–176.PubMedGoogle Scholar
  132. 132.
    Gershov D, Kim S, Brot N et al. C-reactive protein binds to apoptotic cells, protects the cells from assembly of the terminal complement components, and sustains an antiinflammatory innate immune response: Implications for systemic autoimmunity. J Exp Med 2000; 192:1353–1363.PubMedCrossRefGoogle Scholar
  133. 133.
    Jarva H, Jokiranta TS, Hellwage J et al. Regulation of complement activation by C-reactive protein: Targeting the complement inhibitory activity of factor H by an interaction with short consensus repeat domains 7 and 8–11. J Immunol 1999; 163:3957–3962.PubMedGoogle Scholar
  134. 134.
    Mold C, Gewurz H, Du Clos TW. Regulation of complement activation by C-reactive protein. Immunopharmacology 1999; 42:23–30.PubMedCrossRefGoogle Scholar
  135. 135.
    Giannakis E, Male DA, Ormsby RJ et al. Multiple ligand binding sites on domain seven of human complement factor H. Int Immunopharmacol 2001; 1:433–443.PubMedCrossRefGoogle Scholar
  136. 136.
    Suresh MV, Singh SK, Ferguson Jr DA et al. Role of the property of C-reactive protein to activate the classical pathway of complement in protecting mice from Streptococcus pneumoniae infection. J Immunol 2006; 176:4369–4374.PubMedGoogle Scholar
  137. 137.
    Müller H, Fehr J. Binding of C-reactive protein to human polymorphonuclear leukocytes: Evidence for association of binding sites with Fc receptors. J Immunol 1986; 136:2202–2207.PubMedGoogle Scholar
  138. 138.
    Marnell LL, Mold C, Volzer MA et al. C-reactive protein binds to FcγRI in transfected COS cells. J Immunol 1995; 155:2185–2193.PubMedGoogle Scholar
  139. 139.
    Bharadwaj D, Stein MP, Volzer M et al. The major receptor for C-reactive protein on leukocytes is Fcγ receptor II. J Exp Med 1999; 190:585–590.PubMedCrossRefGoogle Scholar
  140. 140.
    Chi M, Tridandapani S, Zhong W et al. C-reactive protein induces signaling through FcγRIIa on HL-60 granulocytes. J Immunol 2002; 168:1413–1418.PubMedGoogle Scholar
  141. 141.
    Bodman-Smith KB, Melendex AJ, Campbell I et al. C-reactive protein-mediated phagocytosis and phospholipase D signalling through the high-affinity receptor for immunoglobulin G (FcγRI). Immunology 2002; 107:252–260.PubMedCrossRefGoogle Scholar
  142. 142.
    Manolov DE, Rocker C, Hombach V et al. Ultrasensitive confocal fluorescence microscopy of C-reactive protein interacting with FcγRIIa. Arterioscler Thromb Vasc Biol 2004; 24:2372–2377.PubMedCrossRefGoogle Scholar
  143. 143.
    Heuertz RM, Schneider GP, Potempa LA et al. Native and modified C-reactive protein bind different receptors on human neutrophils. Int J Biochem Cell Biol 2005; 37:320–335.PubMedCrossRefGoogle Scholar
  144. 144.
    Bang R, Marnell L, Mold C et al. Analysis of binding sites in human C-reactive protein for FcγRI, FcγRIIa, and C1q by site-directed mutagenesis. J Biol Chem 2005; 280:25095–25102.PubMedCrossRefGoogle Scholar
  145. 145.
    Zeller JM, Landay AL, Lint TF et al. Enhancement of human peripheral blood monocyte respiratory burst activity by aggregated C-reactive protein. J Leukoc Biol 1986; 40:769–783.PubMedGoogle Scholar
  146. 146.
    Tebo JM, Mortensen RF. Internalization and degradation of receptor bound C-reactive protein by U-937 cells: Induction of H2O2 production and tumoricidal activity. Biochim Biophys Acta 1991; 1095:210–216.PubMedCrossRefGoogle Scholar
  147. 147.
    Mold C, Rodic-Polic B, DuClos TW. Protection from Streptococcus pneumoniae infection by C-reactive protein and natural antibody requires complement but not Fcγ receptors. J Immunol 2002; 168:6375–6381.PubMedGoogle Scholar
  148. 148.
    Mold C, Rodriguez W, Rodic-Polic B et al. C-reactive protein mediates protection from lipopolysaccharide through interactions with FcγR. J Immunol 2002; 169:7019–7025.PubMedGoogle Scholar
  149. 149.
    Barna BP, Thomassen MJ, Wiedemann HP et al. Modulation of human alveolar macrophage tumoricidal activity by C-reactive protein. J Biol Response Mod 1988; 7:483–487.PubMedGoogle Scholar
  150. 150.
    Mortensen RF, Duszkiewicz JA. Mediation of CRP-dependent phagocytosis through mouse macrophage Fc-receptors. J Immunol 1977; 119:1611–1616.PubMedGoogle Scholar
  151. 151.
    Zahedi K, Tebo JM, Siripont J et al. Binding of human C-reactive protein to mouse macrophages is mediated by distinct receptors. J Immunol 1989; 142:2384–2392.PubMedGoogle Scholar
  152. 152.
    Stein MP, Mold C, DuClos TW. C-reactive protein binding to murine leukocytes requires Fcγ receptors. J Immunol 2000; 164:1514–1520.PubMedGoogle Scholar
  153. 153.
    Bharadwaj D, Mold C, Markham E et al. Serum amyloid P component binds to Fc gamma receptors and opsonizes particles for phagocytosis. J Immunol 2001; 166:6735–6741.PubMedGoogle Scholar
  154. 154.
    Mold C, Gresham HD, DuClos TW. Serum amyloid P component and C-reactive protein mediate phagocytosis through murine FcγRs. J Immunol 2001; 166:1200–1205.PubMedGoogle Scholar
  155. 155.
    Hamazaki H. Ca2+-dependent binding of human serum amyloid P component to Alzheimer’s β-amyloid peptide. J Biol Chem 1995; 270:10392–10394.PubMedGoogle Scholar
  156. 156.
    Janciauskiene S, García De Frutos P, Carlemalm E et al. Inhibition of Alzheimer β-peptide fibril formation by serum amyloid P component. J Biol Chem 1995; 270:26041–26044.PubMedCrossRefGoogle Scholar
  157. 157.
    Urbányi Z, Lakics V, Erdö SL. Serum amyloid P component-induced cell death in primary cultures of rat cerebral cortex. Eur J Pharmacol 1994; 270:375–378.PubMedGoogle Scholar
  158. 158.
    Togashi S, Lim SK, Kawano H et al. Serum amyloid P component enhances induction of murine amyloidosis. Lab Invest 1997; 77:525–531.PubMedGoogle Scholar
  159. 159.
    Botto M, Hawkins PM, Bickerstaff MCM et ai. Amyloid deposition is delayed in mice with targeted deletion of the serum amyloid P component gene. Nature Med 1997; 3:855:859.PubMedGoogle Scholar
  160. 160.
    Tennent GA, Lovat LB, Pepys MB. Serum amyloid P component prevents proteolysis of the amyloid fibrils of Alzheimer disease and systemic amyloidosis. Proc Natl Acad Sci USA 1995; 92:4299–4303.PubMedCrossRefGoogle Scholar
  161. 161.
    Breviario F, d’Aniello EM, Golay J et al. Interleukin-1-inducible genes in endothelial cells: Cloning of a new gene related to C-reactive protein and serum amyloid P component. J Biol Chem 1992; 267:22190–22197.PubMedGoogle Scholar
  162. 162.
    Lee GW, Lee TH, Vilcek J. TSG-14, a tumor necrosis factorand IL-1-inducible protein, is a novel member of the pentaxin family of acute phase proteins. J Immunol 1993; 150:1804–1812.PubMedGoogle Scholar
  163. 163.
    Bottazzi B, Garlanda C, Salvatori G et ai. Pentraxins as a key component of innate immunity. Curr Opin Immunol 2006; 18:10–15.PubMedCrossRefGoogle Scholar
  164. 164.
    Bottazzi B, Vouret-Craviari V, Bastone A et al. Multimer formation and ligand recognition by the long pentraxin PTX3: Similarities and differences with the short pentraxins C-reactive protein and serum amyloid P component. J Biol Chem 1997; 272:32817–32823.PubMedCrossRefGoogle Scholar
  165. 165.
    Nauta AJ, Bottazzi B, Mantovani A et al. Biochemical and functional characterization of the interaction between pentraxin 3 and C1q. Eur J Immunol 2003; 33:465–473.PubMedCrossRefGoogle Scholar
  166. 166.
    Rusnati M, Camozzi M, Moroni E et al. Selective recognition of fibroblast growth factor-2 by the long pentraxin PTX3 inhibits angiogenesis. Blood 2004; 104:92–99.PubMedCrossRefGoogle Scholar
  167. 167.
    Salustri A, Garlanda C, Hirsch E et al. PTX3 plays a key role in the organization of the cumulus oophorus extracellular matrix and in in vivo fertilization. Development 2004; 131:1577–1586.PubMedCrossRefGoogle Scholar
  168. 168.
    Garlanda C, Hirsch E, Bozza S et al. Nonredundant role of the long pentraxin PTX3 in anti-fungal innate immune response. Nature 2002; 420:182–186.PubMedCrossRefGoogle Scholar
  169. 169.
    Jeannin P, Bottazzi B, Sironi M et al. Complexity and complementarity of outer membrane protein A recognition by cellular and humoral innate immunity receptors. Immunity 2005; 22:551–560.PubMedCrossRefGoogle Scholar
  170. 170.
    Diniz SN, Nomizo R, Cisalpino PS et al. PTX3 function as an opsonin for the dectin-1-dependent internalization of zymosan by macrophages. J Leukoc Biol 2004; 75:649–656.PubMedCrossRefGoogle Scholar
  171. 171.
    Dias AA, Goodman AR, Dos Santos JL et al. TSG-14 transgenic mice have improved survival to endotoxemia and to CLP-induced sepsis. J Leukoc Biol 2001; 69:928–936.PubMedGoogle Scholar
  172. 172.
    Souza DG, Soares AC, Pinho V et al. Increased mortality and inflammation in tumor necrosis factor-stimulated gene-14 transgenic mice after ischemia and reperfusion injury. Am J Pathol 2002; 160:1755–1765.PubMedGoogle Scholar
  173. 173.
    Varani S, Elvin JA, Yan C et al. Knockout of pentraxin 3, a downstream target of growth differentiation factor-9, causes female subfertility. Mol Endocrinol 2002; 16:1154–1167.PubMedCrossRefGoogle Scholar
  174. 174.
    Introna M, Alles W, Castellano M et al. Cloning of mouse ptx3, a new member of the pentraxin gene family expressed at extrahepatic sites. Blood 1996; 87:1862–1872.PubMedGoogle Scholar
  175. 175.
    Vidal Alles V, Bottazzi B, Peri G et al. Inducible expression of PTX3, a new member of the pentraxin family, in human mononuclear phagocytes. Blood 1994; 84:3483–3493.PubMedGoogle Scholar
  176. 176.
    Polentarutti N, Bottazzi B, Di Santo E et al. Inducible expression of the long pentraxin PTX3 in the central nervous system. J Neuroimmunol 2000; 106:87–94.PubMedCrossRefGoogle Scholar
  177. 177.
    Goodman AR, Levy DE, Reis LF et al. Differential regulation of TSG-14 expression in murine fibroblasts and peritoneal macrophages. J Leukoc Biol 2000; 67:387–395.PubMedGoogle Scholar
  178. 178.
    Klouche M, Peri G, Knabbe C et al. Modified atherogenic lipoproteins induce expression of pentraxin-3 by human vascular smooth muscle cells. Atherosclerosis 2004; 175:221–228.PubMedCrossRefGoogle Scholar
  179. 179.
    Abderrahim-Ferkoune A, Bezy O, Chiellini C et al. Characterization of the long pentraxin PTX3 as a TNFa-induced secreted protein of adipose cells. J Lipid Res 2003; 44:994–1000.PubMedCrossRefGoogle Scholar
  180. 180.
    Luchetti MM, Piccinini G, Mantovani A et al. Expression and production of the long pentraxin PTX3 in rheumatoid arthritis. Clin Exp Immunol 2000; 119:196–202.PubMedCrossRefGoogle Scholar
  181. 181.
    Nauta AJ, de Haij S, Bottazzi B et al. Human renal epithelial cells produce the long pentraxin PTX3. Kidney Int 2005; 67:543–553.PubMedCrossRefGoogle Scholar
  182. 182.
    Dos Santos CC, Han B, Andrade CF et al. DNA microarray analysis of gene expression in alveolar epithelial cells in response to TNFa, LPS, and cyclic stretch. Physiol Genomics 2004; 19:331–342.PubMedCrossRefGoogle Scholar
  183. 183.
    Doni A, Peri G, Chieppa M et al. Production of the soluble pattern recognition receptor PTX3 by myeloid, but not plasmacytoid, dendritic cells. Eur J Immunol 2003; 33:2886–2893.PubMedCrossRefGoogle Scholar
  184. 184.
    Baruah P, Propato A, Dumitriu IE et al. The pattern recognition receptor PTX3 is recruited at the synapse between dying and dendritic cells and edits the cross-presentation of self, viral and tumor antigens. Blood 2006; 107:151–158.PubMedCrossRefGoogle Scholar
  185. 185.
    Polentarutti N, Picardi G, Basile A et al. Interferon-γ inhibits expression of the long pentraxin PTX3 in human monocytes. Eur J Immunol 1998; 28:496–501.PubMedCrossRefGoogle Scholar
  186. 186.
    Doni A, Mosca M, Bottazzi B et al. Regulation of PTX3, a key component of the humoral innate immunity, in human dendritic cells: Stimulation by IL-10 and inhibition by IFNγ. J Leukoc Biol 2006; 79:797–802.PubMedCrossRefGoogle Scholar
  187. 187.
    Zhang X, Jafari N, Barnes RB et al. Studies of gene expression in human cumulus cells indicate pentraxin 3 as a possible marker for oocyte quality. Fertil Steril 2005; 83:1169–1179.PubMedCrossRefGoogle Scholar
  188. 188.
    Paffoni A, Ragni G, Doni A et al. Follicular fluid levels of the long pentraxin PTX3. J Soc Gynecol Invest 2006; 13:226–231.CrossRefGoogle Scholar
  189. 189.
    Cetini I, Cozzi V, Pasqualini F et al. Elevated maternal levels of the long pentraxin 3 (PTX3) in preeclampsia and intrauterine growth restriction. Am J Obstet Gynecol 2006; 194:1347–1353.CrossRefGoogle Scholar
  190. 190.
    Gaziano R, Bozza S, Bellocchio S et al. Anti-Aspergillus fumigatus efficacy of pentraxin 3 alone and in combination with antifungals. Antimicrob Agents Chemother 2004; 48:4414–4421.PubMedCrossRefGoogle Scholar
  191. 191.
    Ravizza T, Moneta D, Bottazzi B et al. Dynamic induction of the long pentraxin PTX3 in the CNS after limbic seizures: Evidence for a protective role in seizure-induced neurodegeneration. Neuroscience 2001; 105:43–53.PubMedCrossRefGoogle Scholar
  192. 192.
    Familian A, Zwart B, Huisman HG et al. Chromatin-independent binding of serum amyloid P component to apoptotic cells. J Immunol 2001; 167:647–654.PubMedGoogle Scholar
  193. 193.
    Rovere P, Peri G, Fazzini F et al. The long pentraxin PTX3 binds to apoptotic cells and regulates their clearance by antigen-presenting dendritic cells. Blood 2000; 96:4300–4306.PubMedGoogle Scholar
  194. 194.
    Rolph MS, Zimmer S, Bottazzi B et al. Production of the long pentraxin PTX3 in advanced atherosclerotic plaques. Arterioscler Thromb Vasc Biol 2002; 22:e10–e14.PubMedCrossRefGoogle Scholar
  195. 195.
    Napoleone E, Di Santo A, Bastone A et al. Long pentraxin PTX3 up-regulates tissue factor expression in human endothelial cells: A novel link between vascular inflammation and clotting activation. Arterioscler Thromb Vasc Biol 2002; 22:782–787.PubMedCrossRefGoogle Scholar
  196. 196.
    Napoleone E, Di Santo A, Peri G et al. The long pentraxin PTX3 up-regulates tissue factor in activated monocytes: Another link between inflammation and clotting activation. J Leukoc Biol 2004; 76:203–209.PubMedCrossRefGoogle Scholar
  197. 197.
    Peri G, Introna M, Corradi D et al. PTX3, A prototypical long pentraxin, is an early indicator of acute myocardial infarction in humans. Circulation 2000; 102:636–641.PubMedGoogle Scholar
  198. 198.
    Latini R, Maggioni AP, Peri G et al. Prognostic significance of the long pentraxin PTX3 in acute myocardial infarction. Circulation 2004; 110:2349–2354.PubMedCrossRefGoogle Scholar
  199. 199.
    Muller B, Peri G, Doni A et al. Circulating levels of the long pentraxin PTX3 correlate with severity of infection in critically ill patients. Crit Care Med 2001; 29:1404–1407.PubMedCrossRefGoogle Scholar
  200. 200.
    Mairuhu AT, Peri G, Setiati TE et al. Elevated plasma levels of the long pentraxin, pentraxin 3, in severe dengue virus infections. J Med Virol 2005; 76:547–552.PubMedCrossRefGoogle Scholar
  201. 201.
    Azzurri A, Sow OY, Amedei A et al. IFN-γ-inducible protein 10 and pentraxin 3 plasma levels are tools for monitoring inflammation and disease activity in Mycobacterium tuberculosis infection. Microbes Infect 2005; 7:1–8.PubMedCrossRefGoogle Scholar
  202. 202.
    Fazzini F, Peri G, Doni A et al. PTX3 in small-vessel vasculitides: An independent indicator of disease activity produced at sites of inflammation. Arthritis Rheum 2001; 44:2841–2850.PubMedCrossRefGoogle Scholar
  203. 203.
    Pascual V, Allantaz F, Arce E et al. Role of interleukin-1 (IL-1) in the pathogenesis of systemic onset juvenile idiopathic arthritis and clinical response to IL-1 blockade. J Exp Med 2005; 201:1479–1486.PubMedCrossRefGoogle Scholar

Copyright information

© Landes Bioscience and Springer Science+Business Media 2009

Authors and Affiliations

  • Alok Agrawal
    • 1
  • Prem Prakash Singh
    • 1
  • Barbara Bottazzi
    • 2
  • Cecilia Garlanda
    • 2
  • Alberto Mantovani
    • 2
    • 3
  1. 1.Department of Pharmacology, James H. Quillen College of MedicineEast Tennessee State UniversityJohnson CityUSA
  2. 2.Istituto Clinico HumanitasRozzano, MilanItaly
  3. 3.Centro IDET Institute of General PathologyUniversity of MilanMilanItaly

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