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Blood, 1 September 2006, Vol. 108, No. 5, pp. 1751-1757. Prepublished online as a Blood First Edition Paper on May 30, 2006; DOI 10.1182/blood-2005-11-011932. This Article Full Text Full Text (PDF) All Versions of this Article: blood-2005-11-011932v1 108/5/1751    most recent Alert me when this article is cited Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Rights and Permissions Citing Articles Citing Articles via HighWire Citing Articles via CrossRef Citing Articles via Google Scholar Google Scholar Articles by Shah, C. Articles by Raynes, J. G. Search for Related Content PubMed PubMed Citation Articles by Shah, C. Articles by Raynes, J. G. Related Collections Immunobiology Phagocytes Social Bookmarking                   What's this?  Previous Article  |  Table of Contents  |  Next Article  PHAGOCYTES Serum amyloid A is an innate immune opsonin for Gram-negative bacteria Chandrabala Shah, Ranjeeta Hari-Dass, and John G. Raynes From the Immunology Unit, Department of Infectious and Tropical Diseases, London School of Hygiene and Tropical Medicine, London, United Kingdom. Serum amyloid A (SAA) is the major acute-phase protein in man and most mammals. Recently we demonstrated that SAA binds to many Gram-negative bacteria including Escherichia coli and Pseudomonas aeruginosa through outer membrane protein A (OmpA) family members. Therefore we investigated whether SAA altered the response of innate phagocytic cells to bacteria. Both the percentage of neutrophils containing E coli and the number of bacteria per neutrophil were greatly increased by SAA opsonization, equivalent to the increase seen for serum opsonization. In contrast, no change was seen for Streptococcus pneumoniae, a bacteria that did not bind SAA. Neutrophil reactive oxygen intermediate production in response to bacteria was also increased by opsonization with SAA. SAA opsonization also increased phagocytosis of E coli by peripheral blood mononuclear cell-derived macrophages. These macrophages showed strong enhancement of TNF- and IL-10 production in response to SAA-opsonized E coli and P aeruginosa. SAA did not enhance responses in the presence of bacteria to which it did not bind. These effects of SAA occur at normal concentrations consistent with SAA binding properties and a role in innate recognition. SAA therefore represents a novel innate recognition protein for Gram-negative bacteria. CiteULike    Connotea    Del.icio.us    Digg    Reddit    Technorati    What's this? This article has been cited by other articles: S. Sandri, D. Rodriguez, E. Gomes, H. P. Monteiro, M. Russo, and A. Campa Is serum amyloid A an endogenous TLR4 agonist? J. Leukoc. Biol., May 1, 2008; 83(5): 1174 - 1180. [Abstract] [Full Text] [PDF] P. Tissieres, I. Dunn-Siegrist, M. Schappi, G. Elson, R. Comte, V. Nobre, and J. Pugin Soluble MD-2 is an acute-phase protein and an opsonin for Gram-negative bacteria Blood, February 15, 2008; 111(4): 2122 - 2131. [Abstract] [Full Text] [PDF] W. Hu, S. Abe-Dohmae, M. Tsujita, N. Iwamoto, O. Ogikubo, T. Otsuka, Y. Kumon, and S. Yokoyama Biogenesis of HDL by SAA is dependent on ABCA1 in the liver in vivo J. Lipid Res., February 1, 2008; 49(2): 386 - 393. [Abstract] [Full Text] [PDF] L. Bjorkman, J. Karlsson, A. Karlsson, M.-J. Rabiet, F. Boulay, H. Fu, J. Bylund, and C. Dahlgren Serum amyloid A mediates human neutrophil production of reactive oxygen species through a receptor independent of formyl peptide receptor like-1 J. Leukoc. Biol., February 1, 2008; 83(2): 245 - 253. [Abstract] [Full Text] [PDF] S. Bozinovski, A. Hutchinson, M. Thompson, L. MacGregor, J. Black, E. Giannakis, A.-S. Karlsson, R. Silvestrini, D. Smallwood, R. Vlahos, et al. Serum Amyloid A Is a Biomarker of Acute Exacerbations of Chronic Obstructive Pulmonary Disease Am. J. Respir. Crit. Care Med., February 1, 2008; 177(3): 269 - 278. [Abstract] [Full Text] [PDF] K. Christenson, L. Bjorkman, C. Tangemo, and J. Bylund Serum amyloid A inhibits apoptosis of human neutrophils via a P2X7-sensitive pathway independent of formyl peptide receptor-like 1 J. Leukoc. Biol., January 1, 2008; 83(1): 139 - 148. [Abstract] [Full Text] [PDF] D. El Kebir, L. Jozsef, T. Khreiss, W. Pan, N. A. Petasis, C. N. Serhan, and J. G. Filep Aspirin-Triggered Lipoxins Override the Apoptosis-Delaying Action of Serum Amyloid A in Human Neutrophils: A Novel Mechanism for Resolution of Inflammation J. Immunol., July 1, 2007; 179(1): 616 - 622. [Abstract] [Full Text] [PDF] Z. Cai, L. Cai, J. Jiang, K.-S. Chang, D. R. van der Westhuyzen, and G. Luo Human Serum Amyloid A Protein Inhibits Hepatitis C Virus Entry into Cells J. Virol., June 1, 2007; 81(11): 6128 - 6133. [Abstract] [Full Text] [PDF]

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