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Adsorption of proteins on m-CPPD and urate crystals inhibits crystal-induced cell responses: study on albumin-crystal interaction

Renaudin, Felix and Sarda, Stéphanie and Campillo-Gimenez, Laure and Séverac, Childerick and Léger, Thibaut and Charvillat, Cédric and Rey, Christian and Lioté, Frédéric and Camadro, Jean-Michel and Ea, Hang-Korng and Combes, Christèle Adsorption of proteins on m-CPPD and urate crystals inhibits crystal-induced cell responses: study on albumin-crystal interaction. (2019) Journal of Functional Biomaterials, 10 (2). 1-19. ISSN 2079-4983

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Official URL: https://dx.doi.org/10.3390/jfb10020018


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 e_ects 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.

Item Type:Article
HAL Id:hal-02178796
Audience (journal):International peer-reviewed journal
Uncontrolled Keywords:
Institution:French research institutions > Centre National de la Recherche Scientifique - CNRS (FRANCE)
Université de Toulouse > Institut National Polytechnique de Toulouse - Toulouse INP (FRANCE)
French research institutions > Institut National de la Santé et de la Recherche Médicale - INSERM (FRANCE)
Other partners > Université de Paris Diderot - Paris 7 (FRANCE)
Université de Toulouse > Université Toulouse III - Paul Sabatier - UT3 (FRANCE)
Laboratory name:
Agence Nationale de la Recherche - Société Française de Rhumatologie
Deposited On:10 Jul 2019 08:54

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