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J Exp Med. Jul 1, 1994; 180(1): 203–209.
PMCID: PMC2191543

Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes

Abstract

Serum amyloid A (SAA) is an acute phase protein that in the blood is bound to high density lipoproteins; SAA is secreted mainly by hepatocytes, and its concentration increases in the blood up to 1000 times during an inflammatory response. At present, its biological function is unclear. Since some forms of secondary amyloidosis are caused by deposition in tissues of peptides derived from the SAA and leukocytes seem to be involved in this process, we investigated the effect of human SAA on human monocytes and polymorphonuclear cells (PMN). When recombinant human SAA (rSAA) was used at concentrations corresponding to those found during the acute phase (> 0.8 microM), it induced directional migration of monocytes and polymorphonuclear leukocytes. Preincubation of rSAA with high density lipoproteins blocked this chemoattractant activity for both monocytes and PMN. rSAA also regulated the expression of the adhesion proteins CD11b and leukocyte cell adhesion molecule 1 and induced the adhesion of PMN and monocytes to umbilical cord vein endothelial cell monolayers. When subcutaneously injected into mice, rSAA recruited PMN and monocytes at the injection site. On the basis of these data, we suggest that SAA may participate in enhancing the migration of monocytes and PMN to inflamed tissues during an acute phase response.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Skinner M. Protein AA/SAA. J Intern Med. 1992 Dec;232(6):513–514. [PubMed]
  • Kolb-Bachofen V. A review on the biological properties of C-reactive protein. Immunobiology. 1991 Sep;183(1-2):133–145. [PubMed]
  • Glenner GG. Amyloid deposits and amyloidosis. The beta-fibrilloses (first of two parts). N Engl J Med. 1980 Jun 5;302(23):1283–1292. [PubMed]
  • Stone MJ. Amyloidosis: a final common pathway for protein deposition in tissues. Blood. 1990 Feb 1;75(3):531–545. [PubMed]
  • Lavie G, Zucker-Franklin D, Franklin EC. Degradation of serum amyloid A protein by surface-associated enzymes of human blood monocytes. J Exp Med. 1978 Oct 1;148(4):1020–1031. [PMC free article] [PubMed]
  • Silverman SL, Cathcart ES, Skinner M, Cohen AS. The degradation of serum amyloid A protein by activated polymorphonuclear leucocytes: participation of granulocytic elastase. Immunology. 1982 Aug;46(4):737–744. [PMC free article] [PubMed]
  • Glenner GG, Page DL. Amyloid, amyloidosis, and amyloidogenesis. Int Rev Exp Pathol. 1976;15:1–92. [PubMed]
  • Wang JM, Sherry B, Fivash MJ, Kelvin DJ, Oppenheim JJ. Human recombinant macrophage inflammatory protein-1 alpha and -beta and monocyte chemotactic and activating factor utilize common and unique receptors on human monocytes. J Immunol. 1993 Apr 1;150(7):3022–3029. [PubMed]
  • Steinkasserer A, Weiss EH, Schwaeble W, Linke RP. Heterogeneity of human serum amyloid A protein. Five different variants from one individual demonstrated by cDNA sequence analysis. Biochem J. 1990 May 15;268(1):187–193. [PMC free article] [PubMed]
  • Rosseneu M, Soetewey F, Peeters H, Bausserman LL, Herbert PN. Interaction of the apoproteins of very low density and high density lipoproteins with synthetic phospholipids. Eur J Biochem. 1976 Nov 1;70(1):285–289. [PubMed]
  • HAVEL RJ, EDER HA, BRAGDON JH. The distribution and chemical composition of ultracentrifugally separated lipoproteins in human serum. J Clin Invest. 1955 Sep;34(9):1345–1353. [PMC free article] [PubMed]
  • Falk W, Goodwin RH, Jr, Leonard EJ. A 48-well micro chemotaxis assembly for rapid and accurate measurement of leukocyte migration. J Immunol Methods. 1980;33(3):239–247. [PubMed]
  • Hoffman JS, Benditt EP. Secretion of serum amyloid protein and assembly of serum amyloid protein-rich high density lipoprotein in primary mouse hepatocyte culture. J Biol Chem. 1982 Sep 10;257(17):10518–10522. [PubMed]
  • Bausserman LL, Herbert PN, McAdam KP. Heterogeneity of human serum amyloid A proteins. J Exp Med. 1980 Sep 1;152(3):641–656. [PMC free article] [PubMed]
  • Jutila MA, Rott L, Berg EL, Butcher EC. Function and regulation of the neutrophil MEL-14 antigen in vivo: comparison with LFA-1 and MAC-1. J Immunol. 1989 Nov 15;143(10):3318–3324. [PubMed]
  • Lavie G, Zucker-Franklin D, Franklin EC. Elastase-type proteases on the surface of human blood monocytes: possible role in amyloid formation. J Immunol. 1980 Jul;125(1):175–180. [PubMed]
  • Bausserman LL, Herbert PN, Forte T, Klausner RD, McAdam KP, Osborne JC, Jr, Rosseneu M. Interaction of the serum amyloid A proteins with phospholipid. J Biol Chem. 1983 Sep 10;258(17):10681–10688. [PubMed]
  • Garcia-Gonzalez A, Weisman MH. The arthritis of familial Mediterranean fever. Semin Arthritis Rheum. 1992 Dec;22(3):139–150. [PubMed]

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