Citrullination of proteins: a common post-translational modification pathway induced by different nanoparticles in vitro and in vivo.

Mohamed, Bashir M.Verma, Navin K.Davies, Anthony M.McGowan, AoifeCrosbie-Staunton, KieranPrina-Mello, AdrieleKelleher, DermotBotting, Catherine H.Causey, Corey P.Thompson, Paul RPruijn, Ger JmKisin, Elena R.Tkach, Alexey V.Shvedova, Anna A.Volkov, Yuri2022-08-232022-08-232012-08-012015-05-22Nanomedicine (Lond). 2012 Aug;7(8):1181-95. doi: 10.2217/nnm.11.177. <a href="http://dx.doi.org/10.2217/nnm.11.177">Link to article on publisher's site</a>1743-5889 (Linking)10.2217/nnm.11.177https://hdl.handle.net/20.500.14038/50024<p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</p>AIM: Rapidly expanding manufacture and use of nanomaterials emphasize the requirements for thorough assessment of health outcomes associated with novel applications. Post-translational protein modifications catalyzed by Ca(2+)-dependent peptidylargininedeiminases have been shown to trigger immune responses including autoantibody generation, a hallmark of immune complexes deposition in rheumatoid arthritis. Therefore, the aim of the study was to assess if nanoparticles are able to promote protein citrullination. MATERIALS and METHODS: Human A549 and THP-1 cells were exposed to silicon dioxide, carbon black or single-walled carbon nanotubes. C57BL/6 mice were exposed to respirable single-walled carbon nanotubes. Protein citrullination, peptidylargininedeiminases activity and target proteins were evaluated. RESULTS: The studied nanoparticles induced protein citrullination both in cultured human cells and mouse lung tissues. Citrullination occurred via the peptidylargininedeiminase-dependent mechanism. Cytokeratines 7, 8, 18 and plectins were identified as intracellular citrullination targets. CONCLUSION: Nanoparticle exposure facilitated post-translational citrullination of proteins.en-USAnimalsCalciumCarbonCell LineCitrullineFemaleHumansHydrolasesLungMiceMice, Inbred C57BLNanostructuresNanotubes, CarbonProtein Processing, Post-TranslationalProteinsSilicon DioxideSootBiochemistryEnzymes and CoenzymesMedicinal-Pharmaceutical ChemistryNanomedicineTherapeuticsCitrullination of proteins: a common post-translational modification pathway induced by different nanoparticles in vitro and in vivo.Journal Articlehttps://escholarship.umassmed.edu/thompson/347135698thompson/34