Sökning: onr:"swepub:oai:DiVA.org:lnu-68145" > Eculizumab-C5 compl...
Fältnamn | Indikatorer | Metadata |
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000 | 03906naa a2200481 4500 | |
001 | oai:DiVA.org:lnu-68145 | |
003 | SwePub | |
008 | 171002s2017 | |||||||||||000 ||eng| | |
024 | 7 | a https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-681452 URI |
024 | 7 | a https://doi.org/10.1016/j.molimm.2017.05.0212 DOI |
040 | a (SwePub)lnu | |
041 | a engb eng | |
042 | 9 SwePub | |
072 | 7 | a ref2 swepub-contenttype |
072 | 7 | a art2 swepub-publicationtype |
100 | 1 | a Nilsson, Per H.,d 1980-u Linnéuniversitetet,Institutionen för kemi och biomedicin (KOB),Oslo Univ Hosp, Norway;Univ Oslo, Norway,Linnaeus Ctr Biomat Chem, BMC;HoRB4 aut0 (Swepub:lnu)enipe |
245 | 1 0 | a Eculizumab-C5 complexes express a C5a neoepitope in vivo :b Consequences for interpretation of patient complement analyses |
264 | 1 | b Elsevier,c 2017 |
338 | a electronic2 rdacarrier | |
520 | a The complement system has obtained renewed clinical focus due to increasing number of patients treated with eculizumab, a monoclonal antibody inhibiting cleavage of C5 into C5a and C5b. The FDA approved indications are paroxysmal nocturnal haemoglobinuria and atypical haemolytic uremic syndrome, but many other diseases are candidates for complement inhibition. It has been postulated that eculizumab does not inhibit C5a formation in vivo, in contrast to what would be expected since it blocks C5 cleavage. We recently revealed that this finding was due to a false positive reaction in a C5a assay. In the present study, we identified expression of a neoepitope which was exposed on C5 after binding to eculizumab in vivo. By size exclusion chromatography of patient serum obtained before and after infusion of eculizumab, we document that the neoepitope was exposed in the fractions containing the eculizumab-C5 complexes, being positive in this actual C5a assay and negative in others. Furthermore, we confirmed that it was the eculizumab-C5 complexes that were detected in the C5a assay by adding an anti-IgG4 antibody as detection antibody. Competitive inhibition by anti-C5 antibodies localized the epitope to the C5a moiety of C5. Finally, acidification of C5, known to alter C5 conformation, induced a neoepitope reacting identical to the one we explored, in the C5a assays. These data are important for interpretation of complement analyses in patients treated with eculizumab. | |
650 | 7 | a NATURVETENSKAPx Biologix Immunologi0 (SwePub)106052 hsv//swe |
650 | 7 | a NATURAL SCIENCESx Biological Sciencesx Immunology0 (SwePub)106052 hsv//eng |
653 | a Complement | |
653 | a Eculizumab | |
653 | a C5 | |
653 | a C5a | |
653 | a Neoepitope | |
653 | a Immunologi | |
653 | a Immunology | |
700 | 1 | a Thomas, Anub Mathewu Oslo Univ Hosp, Norway4 aut |
700 | 1 | a Bergseth, Gretheu Nordland Hosp, Norway4 aut |
700 | 1 | a Gustavsen, Aliceu Oslo Univ Hosp, Norway4 aut |
700 | 1 | a Volokhina, Elena B.u Radboud Univ Nijmegen, Netherlands;Radboud Univ Nijmegen, Netherlands4 aut |
700 | 1 | a van den Heuvel, Lambertus P.u Radboud Univ Nijmegen, Netherlands;Univ Hosp Leuven, Belgium4 aut |
700 | 1 | a Barratt-Due, Andreasu Oslo Univ Hosp, Norway4 aut |
700 | 1 | a Mollnes, Tom E.u Oslo Univ Hosp, Norway;Univ Oslo, Norway;Nordland Hosp, Norway;Univ Tromso, Norway;Norwegian Univ Sci & Technol, Norway4 aut |
710 | 2 | a Linnéuniversitetetb Institutionen för kemi och biomedicin (KOB)4 org |
773 | 0 | t Molecular Immunologyd : Elsevierg 89, s. 111-114q 89<111-114x 0161-5890x 1872-9142 |
856 | 4 | u https://doi.org/10.1016/j.molimm.2017.05.021y Fulltext |
856 | 4 | u https://lnu.diva-portal.org/smash/get/diva2:1146254/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print |
856 | 4 | u https://doi.org/10.1016/j.molimm.2017.05.021 |
856 | 4 8 | u https://urn.kb.se/resolve?urn=urn:nbn:se:lnu:diva-68145 |
856 | 4 8 | u https://doi.org/10.1016/j.molimm.2017.05.021 |
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