Peptidylarginine deiminase and deiminated proteins are detected throughout early halibut ontogeny - Complement components C3 and C4 are post-translationally deiminated in halibut (Hippoglossus hippoglossus L.)

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dc.contributorHáskóli Íslandsen_US
dc.contributorUniversity of Icelanden_US
dc.contributor.authorMagnadottir, Bergljot
dc.contributor.authorBragason, Birkir
dc.contributor.authorBricknell, Ian
dc.contributor.authorBowden, Timothy
dc.contributor.authorNicholas, Anthony P.
dc.contributor.authorHristova, Mariya
dc.contributor.authorGuðmundsdóttir, Sigríður
dc.contributor.authorDodds, Alister W.
dc.contributor.authorLange, Sigrun
dc.contributor.departmentTilraunastöð í meinafræði að Keldum (HÍ)en_US
dc.contributor.departmentInstitute for Experimental Pathology, Keldur (UI)en_US
dc.date.accessioned2020-05-15T11:48:20Z
dc.date.available2020-05-15T11:48:20Z
dc.date.issued2019-03
dc.descriptionPublisher's version (útgefin grein)en_US
dc.description.abstractPost-translational protein deimination is mediated by peptidylarginine deiminases (PADs), which are calcium dependent enzymes conserved throughout phylogeny with physiological and pathophysiological roles. Protein deimination occurs via the conversion of protein arginine into citrulline, leading to structural and functional changes in target proteins. In a continuous series of early halibut development from 37 to 1050° d, PAD, total deiminated proteins and deiminated histone H3 showed variation in temporal and spatial detection in various organs including yolksac, muscle, skin, liver, brain, eye, spinal cord, chondrocytes, heart, intestines, kidney and pancreas throughout early ontogeny. For the first time in any species, deimination of complement components C3 and C4 is shown in halibut serum, indicating a novel mechanism of complement regulation in immune responses and homeostasis. Proteomic analysis of deiminated target proteins in halibut serum further identified complement components C5, C7, C8 C9 and C1 inhibitor, as well as various other immunogenic, metabolic, cytoskeletal and nuclear proteins. Post-translational deimination may facilitate protein moonlighting, an evolutionary conserved phenomenon, allowing one polypeptide chain to carry out various functions to meet functional requirements for diverse roles in immune defences and tissue remodelling.en_US
dc.description.sponsorshipThe authors wish to thank Birgir Kristjánsson and the staff at Fiskeldi Eyjafjardar, þorlákshöfn, Iceland, and the staff at Fiskey hf, Hjalteyri, Iceland for providing the fish and sampling facilities. Thanks are due to Sigurður Helgason, Gísli Jónsson and Margrét Jónsdóttir, Keldur, Institute for Experimental Pathology University of Iceland, and to Paul Cook, FRS Marine Laboratory, Aberdeen, Scotland, for preparation of larval samples. Thanks also to Antony Willis, MRC Immunochemistry Unit, Department of Biochemistry, Oxford, for N-terminal amino acid sequence analysis and Michael Deery at the Cambridge Centre for Proteomics. This work was supported in parts by the EC grant Fishaid QLK2-CT-2000-01076 , The Icelandic Ministry of Fisheries , The Icelandic Research Council (RANNIS) , the European Molecular Biology Organisation (EMBO) and a University of Westminster start-up grant to SL. The authors declare no competing interest.en_US
dc.description.versionPeer Revieweden_US
dc.format.extent1-19en_US
dc.identifier.citationMagnadóttir, B. et al., 2019. Peptidylarginine deiminase and deiminated proteins are detected throughout early halibut ontogeny - Complement components C3 and C4 are post-translationally deiminated in halibut (Hippoglossus hippoglossus L.). Developmental and Comparative Immunology, 92, pp.1–19.en_US
dc.identifier.doi10.1016/j.dci.2018.10.016
dc.identifier.issn0145-305X
dc.identifier.journalDevelopmental & Comparative Immunologyen_US
dc.identifier.urihttps://hdl.handle.net/20.500.11815/1802
dc.language.isoenen_US
dc.publisherElsevier BVen_US
dc.relation.ispartofseriesDevelopmental & Comparative Immunology;92
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectComplementen_US
dc.subjectHalibuten_US
dc.subjectHippoglossus hippoglossus Len_US
dc.subjectOntogenyen_US
dc.subjectPentraxinen_US
dc.subjectPeptidylarginine deiminaseen_US
dc.subjectProtein deiminationen_US
dc.subjectLúðaen_US
dc.subjectLífeðlisfræðien_US
dc.subjectMeinafræðien_US
dc.subjectPrótínen_US
dc.titlePeptidylarginine deiminase and deiminated proteins are detected throughout early halibut ontogeny - Complement components C3 and C4 are post-translationally deiminated in halibut (Hippoglossus hippoglossus L.)en_US
dc.typeinfo:eu-repo/semantics/articleen_US
dcterms.licenseThis is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/BY-NC-ND/4.0/)en_US

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