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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

Université Paris 7 Denis Diderot, Inserm UMR 1132 Bioscar, Hôpital Lariboisière, Centre Viggo Petersen, 75010 Paris, France
CIRIMAT, Université de Toulouse, CNRS, Université Toulouse 3, Toulouse INP-ENSIACET, 31030 Toulouse, France
ITAV-CNRS, Université de Toulouse, CNRS, 31106 Toulouse, France
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;
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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