Citrullination of proteins: a common post-translational modification pathway induced by different nanoparticles in vitro and in vivo.
dc.contributor.author | Mohamed, Bashir M. | |
dc.contributor.author | Verma, Navin K. | |
dc.contributor.author | Davies, Anthony M. | |
dc.contributor.author | McGowan, Aoife | |
dc.contributor.author | Crosbie-Staunton, Kieran | |
dc.contributor.author | Prina-Mello, Adriele | |
dc.contributor.author | Kelleher, Dermot | |
dc.contributor.author | Botting, Catherine H. | |
dc.contributor.author | Causey, Corey P. | |
dc.contributor.author | Thompson, Paul R | |
dc.contributor.author | Pruijn, Ger Jm | |
dc.contributor.author | Kisin, Elena R. | |
dc.contributor.author | Tkach, Alexey V. | |
dc.contributor.author | Shvedova, Anna A. | |
dc.contributor.author | Volkov, Yuri | |
dc.date | 2022-08-11T08:11:00.000 | |
dc.date.accessioned | 2022-08-23T17:28:11Z | |
dc.date.available | 2022-08-23T17:28:11Z | |
dc.date.issued | 2012-08-01 | |
dc.date.submitted | 2015-05-22 | |
dc.identifier.citation | Nanomedicine (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> | |
dc.identifier.issn | 1743-5889 (Linking) | |
dc.identifier.doi | 10.2217/nnm.11.177 | |
dc.identifier.uri | http://hdl.handle.net/20.500.14038/50024 | |
dc.description | <p>At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.</p> | |
dc.description.abstract | 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. | |
dc.language.iso | en_US | |
dc.relation | <a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=pubmed&cmd=Retrieve&list_uids=22625207&dopt=Abstract">Link to Article in PubMed</a> | |
dc.relation.url | http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3465773/ | |
dc.subject | Animals | |
dc.subject | Calcium | |
dc.subject | Carbon | |
dc.subject | Cell Line | |
dc.subject | Citrulline | |
dc.subject | Female | |
dc.subject | Humans | |
dc.subject | Hydrolases | |
dc.subject | Lung | |
dc.subject | Mice | |
dc.subject | Mice, Inbred C57BL | |
dc.subject | Nanostructures | |
dc.subject | Nanotubes, Carbon | |
dc.subject | Protein Processing, Post-Translational | |
dc.subject | Proteins | |
dc.subject | Silicon Dioxide | |
dc.subject | Soot | |
dc.subject | Biochemistry | |
dc.subject | Enzymes and Coenzymes | |
dc.subject | Medicinal-Pharmaceutical Chemistry | |
dc.subject | Nanomedicine | |
dc.subject | Therapeutics | |
dc.title | Citrullination of proteins: a common post-translational modification pathway induced by different nanoparticles in vitro and in vivo. | |
dc.type | Journal Article | |
dc.source.journaltitle | Nanomedicine (London, England) | |
dc.source.volume | 7 | |
dc.source.issue | 8 | |
dc.identifier.legacycoverpage | https://escholarship.umassmed.edu/thompson/34 | |
dc.identifier.contextkey | 7135698 | |
html.description.abstract | <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.</p> <p>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.</p> <p>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.</p> <p>CONCLUSION: Nanoparticle exposure facilitated post-translational citrullination of proteins.</p> | |
dc.identifier.submissionpath | thompson/34 | |
dc.contributor.department | Department of Biochemistry and Molecular Pharmacology | |
dc.source.pages | 1181-95 |