Show simple item record

dc.contributor.authorMohamed, Bashir M.
dc.contributor.authorVerma, Navin K.
dc.contributor.authorDavies, Anthony M.
dc.contributor.authorMcGowan, Aoife
dc.contributor.authorCrosbie-Staunton, Kieran
dc.contributor.authorPrina-Mello, Adriele
dc.contributor.authorKelleher, Dermot
dc.contributor.authorBotting, Catherine H.
dc.contributor.authorCausey, Corey P.
dc.contributor.authorThompson, Paul R
dc.contributor.authorPruijn, Ger Jm
dc.contributor.authorKisin, Elena R.
dc.contributor.authorTkach, Alexey V.
dc.contributor.authorShvedova, Anna A.
dc.contributor.authorVolkov, Yuri
dc.date2022-08-11T08:11:00.000
dc.date.accessioned2022-08-23T17:28:11Z
dc.date.available2022-08-23T17:28:11Z
dc.date.issued2012-08-01
dc.date.submitted2015-05-22
dc.identifier.citationNanomedicine (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.issn1743-5889 (Linking)
dc.identifier.doi10.2217/nnm.11.177
dc.identifier.urihttp://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.abstractAIM: 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.isoen_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.urlhttp://www.ncbi.nlm.nih.gov/pmc/articles/PMC3465773/
dc.subjectAnimals
dc.subjectCalcium
dc.subjectCarbon
dc.subjectCell Line
dc.subjectCitrulline
dc.subjectFemale
dc.subjectHumans
dc.subjectHydrolases
dc.subjectLung
dc.subjectMice
dc.subjectMice, Inbred C57BL
dc.subjectNanostructures
dc.subjectNanotubes, Carbon
dc.subjectProtein Processing, Post-Translational
dc.subjectProteins
dc.subjectSilicon Dioxide
dc.subjectSoot
dc.subjectBiochemistry
dc.subjectEnzymes and Coenzymes
dc.subjectMedicinal-Pharmaceutical Chemistry
dc.subjectNanomedicine
dc.subjectTherapeutics
dc.titleCitrullination of proteins: a common post-translational modification pathway induced by different nanoparticles in vitro and in vivo.
dc.typeJournal Article
dc.source.journaltitleNanomedicine (London, England)
dc.source.volume7
dc.source.issue8
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/thompson/34
dc.identifier.contextkey7135698
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.submissionpaththompson/34
dc.contributor.departmentDepartment of Biochemistry and Molecular Pharmacology
dc.source.pages1181-95


This item appears in the following Collection(s)

Show simple item record