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dc.date.accessioned2017-03-07T16:08:24Z
dc.date.available2017-03-07T16:08:24Z
dc.date.created2002-12-20T11:53:54Z
dc.date.issued2002
dc.identifier.citationBraathen, Ranveig Sørensen, Vigdis Brandtzæg, Per Sandlie, Inger Johansen, Finn Eirik . The carboxyl-terminal domains of IgA and IgM direct isotype-specific polymerization and interaction with the polymeric immunoglobulin receptor. Journal of Biological Chemistry. 2002, 277(45), 42755-42762
dc.identifier.urihttp://hdl.handle.net/10852/54501
dc.description.abstractMucosal surfaces are protected by polymeric immunoglobulins that are transported across the epithelium by the polymeric immunoglobulin receptor (pIgR). Only polymeric IgA and IgM containing a small polypeptide called the "joining" (J) chain can bind to the pIgR. J chain-positive IgA consists of dimers, and some larger polymers, whereas only IgM pentamers incorporate the J chain. We made domain-swap chimeras between human IgA1 and IgM and found that the COOH-terminal domains of the heavy chains (Ca3 and Cm4, respectively) dictated the size of the polymers formed and also which polymers incorporated the J chain. We also showed that chimeric IgM molecules engineered to contain Ca3 were able to bind the rabbit pIgR. Since the rabbit pIgR normally does not bind IgM, these results suggest that the COOH-terminal domain of the polymeric immunoglobulins is primarily responsible for interaction with the pIgR. Finally, we made a novel chimeric IgA immunoglobulin, containing the terminal domain from IgM. This recombinant molecule formed J chain-containing pentamers that could, like IgA, efficiently form covalent complexes with the human pIgR ectodomain, known as secretory component. This research was originally published in: Journal of Biological Chemistry. © the American Society for Biochemistry and Molecular Biology.en_US
dc.languageEN
dc.titleThe carboxyl-terminal domains of IgA and IgM direct isotype-specific polymerization and interaction with the polymeric immunoglobulin receptoren_US
dc.typeJournal articleen_US
dc.creator.authorBraathen, Ranveig
dc.creator.authorSørensen, Vigdis
dc.creator.authorBrandtzæg, Per
dc.creator.authorSandlie, Inger
dc.creator.authorJohansen, Finn Eirik
cristin.unitcode185,13,14,6
cristin.unitnamePatologiklinikken
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode2
dc.identifier.cristin436390
dc.identifier.bibliographiccitationinfo:ofi/fmt:kev:mtx:ctx&ctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Journal of Biological Chemistry&rft.volume=277&rft.spage=42755&rft.date=2002
dc.identifier.jtitleJournal of Biological Chemistry
dc.identifier.volume277
dc.identifier.issue45
dc.identifier.startpage42755
dc.identifier.endpage42762
dc.identifier.doihttp://dx.doi.org/10.1074/jbc.M205502200
dc.identifier.urnURN:NBN:no-57628
dc.type.documentTidsskriftartikkelen_US
dc.type.peerreviewedPeer reviewed
dc.source.issn0021-9258
dc.identifier.fulltextFulltext https://www.duo.uio.no/bitstream/handle/10852/54501/2/67.%2BJ.%2BBiol.%2BChem.-2002-Braathen-42755-6287330.pdf
dc.type.versionPublishedVersion


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