Expression, detection and assay of a neoantigen (Neo-CRP) associated with a free, human C-reactive protein subunit

Potempa, Lawrence A.; Siegel, Joan N.; Fedel, Barry A.; Potempa, Rita T.; Gewürz, Henry

doi:10.1016/0161-5890(87)90028-9

Cited by 138 publications

(138 citation statements)

References 43 publications

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“…mCRP was thoroughly dialysed in phosphate buffer (10 mM Na 2 HPO 4 , 10 mM NaH 2 PO 4 , 15 mM NaCl, pH 7.4). 10 Factor H deletion constructs SCRs 1-7 (FHL1), 39 The HepG Factor H mutant has five amino acid residues exchanged (that is, R1203E, R1206E, R1210S, K1230S and R1231A) and was expressed on an SCRs 15-20 backbone. 40 mCRP and pCRP binding to immobilized Factor H. Binding of mCRP and pCRP to immobilized Factor H was analyzed by ELISA using a TC buffer (Tris-calcium-buffer 140 mM NaCl, 10 mM Tris, 2 mM CaCl 2 , 1 mM MgCl 2 , pH 7.4) 18 or phosphate-buffered saline.…”

Section: Factor H Interacts With Monomeric Crp M Mihlan Et Almentioning

confidence: 99%

“…7,8 This 125-kDa pentameric form (pCRP) is modified on calcium depletion, heat or urea treatment, surface attachment, by inflammatory conditions, oxidative stress, low pH or by proteases, and dissociates into monomeric units of 23 kDa, termed monomeric CRP (mCRP). [9][10][11] The exact biological functions of pCRP and mCRP are currently unclear. Both mCRP and pCRP bind to damaged cells.…”

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confidence: 99%

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Monomeric CRP contributes to complement control in fluid phase and on cellular surfaces and increases phagocytosis by recruiting factor H

et al. 2009

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Section: Factor H Interacts With Monomeric Crp M Mihlan Et Almentioning

confidence: 99%

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confidence: 99%

Monomeric CRP contributes to complement control in fluid phase and on cellular surfaces and increases phagocytosis by recruiting factor H

et al. 2009

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“…Conformationally altered forms of CRP express several epitopes that are not present on native CRP 16 and display properties distinct from those of native CRP. [17][18][19] …”

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confidence: 99%

Conformational Rearrangement in C-Reactive Protein Is Required for Proinflammatory Actions on Human Endothelial Cells

et al. 2004

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Background-C-reactive protein (CRP) has been suggested to actively amplify the inflammatory response underlying coronary heart diseases by directly activating endothelial cells. In this study, we investigated whether loss of the cyclic pentameric structure of CRP, resulting in formation of modified or monomeric CRP (mCRP), is a prerequisite for endothelial cell activation. Methods and Results-We examined the impact of native CRP and mCRP on the production of monocyte chemoattractant protein-1 (MCP-1) and interleukin-8 (IL-8), key regulators of leukocyte recruitment, and on the expression of intercellular adhesion molecule-1 (ICAM-1), E-selectin, and vascular adhesion molecule-1 (VCAM-1) in human cultured coronary artery endothelial cells (HCAECs). Incubation with mCRP for 4 hours increased MCP-1 and IL-8 secretion and mRNA levels and expression of ICAM-1, E-selectin, and VCAM-1 protein and mRNA. Significant induction occurred at 1 to 5 g/mL, reached a maximum at 30 g/mL, and did not require the presence of serum. Native CRP was without detectable effects at 4 hours, whereas it enhanced cytokine release after a 24-hour incubation. An anti-Fc␥RIII (CD16) but not an anti-Fc␥RII (CD32) antibody produced a 14% to 32% reduction of the mCRP effects (PϽ0.05). mCRP but not CRP evoked phosphorylation of p38 mitogen-activated protein kinase, and inhibition of this kinase with SB 203580 reversed the effects of mCRP. Furthermore, culture of HCAECs in the presence of SB203580 markedly decreased mCRP-stimulated E-selectin and ICAM-1-dependent adhesion of neutrophils to HCAECs (PϽ0.001). Conclusions-Loss of pentameric symmetry in CRP, resulting in formation of mCRP, promotes a proinflammatory HCAEC phenotype through a p38 MAPK-dependent mechanism.

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“…Subsequent studies confirmed the enhanced interactions of mCRP with modified lipoproteins [61] and complement [62][63][64][65][66][67] and further revealed the important contributions of mCRP in promoting non-inflammatory clearance of apoptotic or necrotic cells by controlling complement activation on the cell surface through balanced recruitment of C1q, Factor H and C4bp [64][65][66]. Because inappropriate handling of CRP, including lyophilization [68], storage in the absence of calcium [69] and immobilization onto microtiter wells [60,70], leads to the disruption of the pentameric structure, the reported properties of CRP suffering these technical pitfalls should be re-evaluated with Factor H interaction as a prominent example [60,64,71].…”

Section: The Bioactivities Of Crp Are Dependent On Conformational Statesmentioning

confidence: 76%

Regulated conformation changes in C-reactive protein orchestrate its role in atherogenesis

2012

Chin. Sci. Bull.

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C-reactive protein (CRP) is a prototypic human acute phase reactant composed of five identical subunits. Emerging evidence indicates that CRP is not merely a predictor of cardiovascular disease, but may also be a direct mediator. However, the diverse and sometimes contradictory activities of CRP have considerably hampered the attempts to define the exact role of CRP in atherogenesis. Here, we review the multiple layers of regulation of CRP's structure and function, highlighting how local inflammation conditions, such as the abundance of damaged cell membranes and redox homeostasis, can tip the balance of the pro-and antiinflammatory activities of CRP. We propose that the highly controlled interplay between different structural conformations of CRP underlies its intrinsic property as a fine modulator of inflammation and atherogenesis. C-reactive protein, inflammation, atherosclerosis, redox Citation:Ma X, Ji S R, Wu Y. Regulated conformation changes in C-reactive protein orchestrate its role in atherogenesis.

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Expression, detection and assay of a neoantigen (Neo-CRP) associated with a free, human C-reactive protein subunit

Cited by 138 publications

References 43 publications

Monomeric CRP contributes to complement control in fluid phase and on cellular surfaces and increases phagocytosis by recruiting factor H

Monomeric CRP contributes to complement control in fluid phase and on cellular surfaces and increases phagocytosis by recruiting factor H

Conformational Rearrangement in C-Reactive Protein Is Required for Proinflammatory Actions on Human Endothelial Cells

Regulated conformation changes in C-reactive protein orchestrate its role in atherogenesis

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