Serum Amyloid A Binding to CLA-1 (CD36 and LIMPII Analogous-1) Mediates Serum Amyloid A Protein-induced Activation of ERK1/2 and p38 Mitogen-activated Protein Kinases

Baranova, Irina N.; Vishnyakova, Tatyana G.; Bocharov, Alexander V.; Kurlander, Roger; Chen, Zhigang; Kimelman, Michael; Remaley, Alan T.; Csákó, György; Fairwell, T; Eggerman, Thomas L.; Patterson, Amy P.

doi:10.1074/jbc.m405009200

Cited by 161 publications

(192 citation statements)

References 73 publications

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“…In addition to FPR2, several other targets have been reported as specific receptors for SAA, including receptor for advanced glycation end products (Yan et al, 2000), the HDL receptor, scavenger receptor class B type I (Cai et al, 2005), CLA-1 (CD36 and LIMPII analogous-1), human orthologue of the Scavenger Receptor Class B Type I (Baranova et al, 2005), P2X7 (Christenson et al, 2008), TLR4 (Sandri et al, 2008), and TLR2 (He et al, 2009). Because we found that SAA stimulated CCL2 production via a PTX-insensitive pathway, we confirmed a role for FPR2 in SAA-induced cellular signaling in HUVECs.…”

Section: Discussionmentioning

confidence: 99%

A pertussis toxin sensitive G-protein-independent pathway is involved in serum amyloid A-induced formyl peptide receptor 2-mediated CCL2 production

et al. 2010

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Section: Discussionmentioning

confidence: 99%

A pertussis toxin sensitive G-protein-independent pathway is involved in serum amyloid A-induced formyl peptide receptor 2-mediated CCL2 production

et al. 2010

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“…Currently four potential candidates for the SAA receptor have been suggested, including Tanis (32) (a membrane selenoprotein), RAGE (33) (the receptor for advanced glycation end product that binds to amyloidogenic forms of SAA), and FPRL1 (5) (a chemotactic 7-transmembrane receptor). Most recently SR-B1 was found to be capable of interacting with SAA both as a free molecule and as a component of HDL (34,35). These do not represent the only potential ways in which SAA might link bacteria with host cells as binding is also reported to laminin and vitronectin (11) and interactions with the integrin receptor ␣IIb␤3 on platelets have Binding was demonstrated using monoclonal anti-SAA followed by fluorescein isothiocyanate-labeled F(abЈ) 2 anti-mouse IgG and recorded 20,000 events.…”

Section: Discussionmentioning

confidence: 99%

Serum Amyloid A Protein Binds to Outer Membrane Protein A of Gram-negative Bacteria

Hari-Dass

Shah²,

Meyer

et al. 2005

Journal of Biological Chemistry

123

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Serum amyloid A (SAA) is the major acute phase protein in man and most mammals. We observed SAA binding to a surprisingly large number of Gram-negative bacteria, including Escherichia coli, Salmonella typhimurium, Shigella flexneri, Klebsiella pneumoniae, Vibrio cholerae, and Pseudomonas aeruginosa. The binding was found to be high affinity and rapid. Importantly, this binding was not inhibited by high density lipoprotein with which SAA is normally complexed in serum. Binding was also observed when bacteria were offered serum containing SAA. Ligand blots following SDS-PAGE or two-dimensional gels revealed two major ligands of 29 and 35 kDa that bound SAA when probing with radiolabeled SAA or SAA and monoclonal anti-SAA. Following fractionation the ligand was found in the outer membrane fraction of E. coli and was identified by matrix-assisted laser desorption ionization time-offlight mass spectrometry to be outer membrane protein A (OmpA). OmpA-deficient E. coli did not bind SAA, and following purification of OmpA the protein retained binding activity. The ligands on other bacteria were likely to be homologues of OmpA because wild type, but not OprF-deficient, P. aeruginosa bound SAA.

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“…During inflammation, SAAs 1 and 2 can also colocalize with HDL (10). However, at higher concentrations, SAA displaces apolipoprotein A-I (ApoA-I) yielding fractions containing SAA, lipid-poor ApoA-I, and lipoprotein-free SAA (11). The lipid-poor form has numerous proinflammatory actions, including chemotactic activity via binding the human N-formyl peptide receptor like-1 expressed on phagocytes (12), and can bind the extracellular matrix and induce matrix metalloproteases and proinflammatory cytokines (13)(14)(15).…”

Section: Serum Amyloid a Induces Monocyte Tissue Factormentioning

confidence: 99%

Serum Amyloid A Induces Monocyte Tissue Factor

Cai

Song

Endoh

et al. 2007

The Journal of Immunology

106

121

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C-reactive protein (CRP) and serum amyloid A (SAA) increase in the blood of patients with inflammatory conditions and CRP-induced monocyte tissue factor (TF) may contribute to inflammation-associated thrombosis. This study demonstrates that SAA is a potent and rapid inducer of human monocyte TF. SAA induced TF mRNA in PBMC within 30 min and optimal procoagulant activity within 4 h, whereas CRP (25 μg/ml)-induced activity was minimal at this time. Unlike CRP, SAA did not synergize with LPS. Procoagulant activity was inhibited by anti-TF and was dependent on factors VII and X, and TF Ag levels were elevated on CD14+ monocytes. Responses were optimal with lymphocytes, although these were not obligatory. Inhibitor studies indicate activation of NF-κB through the ERK1/2 and p38 MAPK pathways; the cyclo-oxygenase pathway was not involved. SAA-induced TF was partially inhibited by high-density lipoprotein, but not by low-density lipoprotein or by apolipoprotein A-I. SAA is a ligand for the receptor for advanced glycation end products (RAGE), and TF generation was suppressed by ∼50% by a RAGE competitor, soluble RAGE, and by ∼85% by anti-RAGE IgG. However, another RAGE ligand, high mobility group box-1 protein, capable of inducing monocyte chemotactic protein-1 mRNA in 2 h, did not induce TF within 24 h. Cross-linking studies confirmed SAA binding to soluble RAGE. Elevated SAA is a marker of disease activity in patients with rheumatoid arthritis, and PBMC from patients with rheumatoid arthritis were more sensitive to SAA than normals, suggesting a new link between inflammation and thrombosis.

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Serum Amyloid A Binding to CLA-1 (CD36 and LIMPII Analogous-1) Mediates Serum Amyloid A Protein-induced Activation of ERK1/2 and p38 Mitogen-activated Protein Kinases

Cited by 161 publications

References 73 publications

A pertussis toxin sensitive G-protein-independent pathway is involved in serum amyloid A-induced formyl peptide receptor 2-mediated CCL2 production

A pertussis toxin sensitive G-protein-independent pathway is involved in serum amyloid A-induced formyl peptide receptor 2-mediated CCL2 production

Serum Amyloid A Protein Binds to Outer Membrane Protein A of Gram-negative Bacteria

Serum Amyloid A Induces Monocyte Tissue Factor

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