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

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    Authors
    Mohamed, Bashir M.
    Verma, Navin K.
    Davies, Anthony M.
    McGowan, Aoife
    Crosbie-Staunton, Kieran
    Prina-Mello, Adriele
    Kelleher, Dermot
    Botting, Catherine H.
    Causey, Corey P.
    Thompson, Paul R
    Pruijn, Ger Jm
    Kisin, Elena R.
    Tkach, Alexey V.
    Shvedova, Anna A.
    Volkov, Yuri
    Show allShow less
    UMass Chan Affiliations
    Department of Biochemistry and Molecular Pharmacology
    Document Type
    Journal Article
    Publication Date
    2012-08-01
    Keywords
    Animals
    Calcium
    Carbon
    Cell Line
    Citrulline
    Female
    Humans
    Hydrolases
    Lung
    Mice
    Mice, Inbred C57BL
    Nanostructures
    Nanotubes, Carbon
    Protein Processing, Post-Translational
    Proteins
    Silicon Dioxide
    Soot
    Biochemistry
    Enzymes and Coenzymes
    Medicinal-Pharmaceutical Chemistry
    Nanomedicine
    Therapeutics
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    Link to Full Text
    http://www.ncbi.nlm.nih.gov/pmc/articles/PMC3465773/
    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.
    Source
    Nanomedicine (Lond). 2012 Aug;7(8):1181-95. doi: 10.2217/nnm.11.177. Link to article on publisher's site
    DOI
    10.2217/nnm.11.177
    Permanent Link to this Item
    http://hdl.handle.net/20.500.14038/50024
    Notes

    At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.

    Related Resources
    Link to Article in PubMed
    ae974a485f413a2113503eed53cd6c53
    10.2217/nnm.11.177
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