Therapeutic potential of phosphoethanolamine-bound C-reactive protein in atherosclerosis

Agrawal, Alok

doi:10.2217/17460875.3.6.599

Cited by 1 publication

(2 citation statements)

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“…The PCh-binding site of CRP participates in the binding of CRP to E-LDL because PCh has been shown to inhibit binding of CRP to E-LDL. We have shown recently that PEt, which, like PCh, presumably also blocks the PCh-binding site of CRP, does not inhibit binding of CRP to E-LDL; instead, PEt enhances the binding of CRP to E-LDL [34, 35]. The capacity of CRP to bind to E-LDL is a beneficial function of CRP because, by doing so, CRP can prevent formation of macrophage foam cells [34,35].…”

Section: Introductionmentioning

confidence: 99%

“…We have shown recently that PEt, which, like PCh, presumably also blocks the PCh-binding site of CRP, does not inhibit binding of CRP to E-LDL; instead, PEt enhances the binding of CRP to E-LDL [34, 35]. The capacity of CRP to bind to E-LDL is a beneficial function of CRP because, by doing so, CRP can prevent formation of macrophage foam cells [34,35]. mCRP exhibits bioactivities different from the bioactivities of CRP [15,36–39].…”

Section: Introductionmentioning

confidence: 99%

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Binding of the monomeric form of C-reactive protein to enzymatically-modified low-density lipoprotein: Effects of phosphoethanolamine

Singh

Suresh

Hammond

et al. 2009

Clinica Chimica Acta

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Background-The 5 subunits of native pentameric C-reactive protein (CRP) are dissociated to generate monomeric form of CRP (mCRP) in some in vitro conditions, both physiological and nonphysiological, and also in vivo. Many bioactivities of mCRP generated by urea-treatment of CRP and of mCRP generated by mutating the primary structure of CRP have been reported. The bioactivities of mCRP generated by spontaneous dissociation of CRP are largely unexplored.Methods-We purified mCRP generated by spontaneous dissociation of CRP and investigated the binding of mCRP to enzymatically-modified low-density lipoprotein (E-LDL).Results-mCRP was approximately 60 times more potent than CRP in binding to E-LDL. In the presence of the small-molecule compound phosphoethanolamine (PEt), at 37°C, the binding of mCRP to E-LDL was enhanced <2-fold, while the binding of CRP to E-LDL was enhanced >10-fold. In contrast, PEt inhibited the binding of both CRP and mCRP to pneumococcal Cpolysaccharide, another phosphocholine-containing ligand to which CRP and mCRP were found to bind. We have not investigated yet whether PEt alters the structure of CRP at 37°C.Conclusions-Combined data suggest that the targeting of CRP with the aim to monomerize CRP in vivo may be an effective approach to capture modified forms of LDL.

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