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Open AccessFeature PaperArticle

Adsorption of Proteins on m-CPPD and Urate Crystals Inhibits Crystal-Induced Cell Responses: Study on Albumin-Crystal Interaction

1
Université Paris 7 Denis Diderot, Inserm UMR 1132 Bioscar, Hôpital Lariboisière, Centre Viggo Petersen, 75010 Paris, France
2
CIRIMAT, Université de Toulouse, CNRS, Université Toulouse 3, Toulouse INP-ENSIACET, 31030 Toulouse, France
3
ITAV-CNRS, Université de Toulouse, CNRS, 31106 Toulouse, France
4
Institut Jacques Monod, UMR7592 CNRS, Université Paris Diderot, 75013 Paris, France
*
Authors to whom correspondence should be addressed.
J. Funct. Biomater. 2019, 10(2), 18; https://doi.org/10.3390/jfb10020018
Received: 31 March 2019 / Revised: 21 April 2019 / Accepted: 23 April 2019 / Published: 25 April 2019
(This article belongs to the Special Issue Functionalized Biomimetic Calcium Phosphates)
The biological effects and cellular activations triggered by monosodium urate (MSU) and calcium pyrophosphate dihydrate (monoclinic: m-CPPD) crystals might be modulated by protein coating on the crystal surface. This study is aimed at: (i) Identifying proteins adsorbed on m-CPPD crystals, and the underlying mechanisms of protein adsorption, and (ii) to understand how protein coating did modulate the inflammatory properties of m-CPPD crystals. The effects of protein coating were assessed in vitro using primary macrophages and THP1 monocytes. Physico-chemical studies on the adsorption of bovine serum albumin (BSA) upon m-CPPD crystals were performed. Adsorption of serum proteins, and BSA on MSU, as well as upon m-CPPD crystals, inhibited their capacity to induce interleukin-1-β secretions, along with a decreased ATP secretion, and a disturbance of mitochondrial membrane depolarization, suggesting an alteration of NLRP3 inflammasome activation. Proteomic analysis identified numerous m-CPPD-associated proteins including hemoglobin, complement, albumin, apolipoproteins and coagulation factors. BSA adsorption on m-CPPD crystals followed a Langmuir-Freundlich isotherm, suggesting that it could modulate m-CPPD crystal-induced cell responses through crystal/cell-membrane interaction. BSA is adsorbed on m-CPPD crystals with weak interactions, confirmed by the preliminary AFM study, but strong interactions of BSA molecules with each other occurred favoring crystal agglomeration, which might contribute to a decrease in the inflammatory properties of m-CPPD crystals. These findings give new insights into the pathogenesis of crystal-related rheumatic diseases and subsequently may open the way for new therapeutic approaches. View Full-Text
Keywords: chondrocalcinosis; gout; Interleukin-1; proteins; m-CPPD crystals; albumin; adsorption chondrocalcinosis; gout; Interleukin-1; proteins; m-CPPD crystals; albumin; adsorption
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Renaudin, F.; Sarda, S.; Campillo-Gimenez, L.; Séverac, C.; Léger, T.; Charvillat, C.; Rey, C.; Lioté, F.; Camadro, J.-M.; Ea, H.-K.; Combes, C. Adsorption of Proteins on m-CPPD and Urate Crystals Inhibits Crystal-Induced Cell Responses: Study on Albumin-Crystal Interaction. J. Funct. Biomater. 2019, 10, 18.

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