Adsorption of Proteins on m-CPPD and Urate Crystals Inhibits Crystal-induced Cell Responses: Study on Albumin-crystal Interaction.
Interleukin-1
adsorption
albumin
chondrocalcinosis
gout
m-CPPD crystals
proteins
Journal
Journal of functional biomaterials
ISSN: 2079-4983
Titre abrégé: J Funct Biomater
Pays: Switzerland
ID NLM: 101570734
Informations de publication
Date de publication:
25 Apr 2019
25 Apr 2019
Historique:
received:
31
03
2019
revised:
21
04
2019
accepted:
23
04
2019
entrez:
28
4
2019
pubmed:
28
4
2019
medline:
28
4
2019
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 31027151
pii: jfb10020018
doi: 10.3390/jfb10020018
pmc: PMC6616386
pii:
doi:
Types de publication
Journal Article
Langues
eng
Subventions
Organisme : Agence Nationale de la Recherche
ID : ANR-12-BS08-0022-01
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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