Citrullination of proteins: a common post-translational modification pathway induced by different nanoparticles in vitro and in vivo.
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
UMass Chan Affiliations
Department of Biochemistry and Molecular PharmacologyDocument Type
Journal ArticlePublication Date
2012-08-01Keywords
AnimalsCalcium
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
Metadata
Show full item recordAbstract
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 siteDOI
10.2217/nnm.11.177Permanent Link to this Item
http://hdl.handle.net/20.500.14038/50024Notes
At the time of publication, Paul Thompson was not yet affiliated with UMass Medical School.
Related Resources
Link to Article in PubMedae974a485f413a2113503eed53cd6c53
10.2217/nnm.11.177