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- W4313356439 abstract "Abstract Cholesterol crystals (CC) play an essential role in the formation of atherosclerotic plaques by inducing inflammation and by functioning as an endogenous danger signal. CC activate the classical and the alternative complement pathways, but the role of the lectin pathway is unknown. In this study we hypothesized that pattern recognition molecules (PRM) from the lectin pathway bind CC and functions as an upstream innate inflammatory signal in the pathophysiology of atherosclerosis. We investigated the binding of the PRMs mannose-binding lectin (MBL), ficolin-1, ficolin-2, and ficolin-3, the associated serine proteases, and complement activation products to CC using recombinant proteins, specific inhibitors as well as deficient and normal sera. Binding was assessed by flow cytometry and microscopy. The results showed that the lectin pathway was activated on CC by binding of ficolin-2 and MBL, resulting in activation and deposition of complement activation products. MBL bound to CC in a calcium dependent manner while ficolin-2 binding was calcium independent. No binding was observed for ficolin-1 or ficolin-3. Moreover, we demonstrated that IgM, but not IgG bound to CC and that C1q binding was facilitated by IgM. In conclusion our study demonstrates that PRMs from the lectin pathway recognize CC and provides evidence for an important role for this pathway in the inflammatory response induced by CC in the pathophysiology of atherosclerosis." @default.
- W4313356439 created "2023-01-06" @default.
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- W4313356439 date "2016-05-01" @default.
- W4313356439 modified "2023-10-13" @default.
- W4313356439 title "Cholesterol crystals activate the lectin complement pathway via ficolin-2 and MBL - implications for the progression of atherosclerosis" @default.
- W4313356439 doi "https://doi.org/10.4049/jimmunol.196.supp.202.26" @default.
- W4313356439 hasPublicationYear "2016" @default.
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