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Immobilized human ApoE activated both the classical and the alternative complement pathways. In contrast, ApoE in solution demonstrated an isoform-dependent inhibition of hemolysis and complement deposition at the level of sC5b-9. Using electron microscopy imaging, we confirmed that ApoE interacts differently with C1q depending on its context; surface-bound ApoE predominantly bound C1q globular heads, whereas ApoE in a solution favored the hinge\/stalk region of C1q. As a model for the lipidated state of ApoE in lipoprotein particles, we incorporated ApoE into phosphatidylcholine\/phosphatidylethanolamine liposomes and found that the presence of ApoE on liposomes increased deposition of C1q and C4b from serum when analyzed using flow cytometry. In addition, posttranslational modifications associated with RA, such as citrullination and oxidation, reduced C4b deposition, whereas carbamylation enhanced C4b deposition on immobilized ApoE. Posttranslational modification of ApoE did not alter C1q interaction but affected binding of complement inhibitors factor H and C4b-binding protein. This suggests that changed ability of C4b to deposit on modified ApoE may play an important role. Our data show that posttranslational modifications of ApoE alter its interactions with complement. Moreover, ApoE may play different roles in the body depending on its solubility, and in diseased states such as RA, deposited ApoE may induce local complement activation rather than exert its typical role of inhibition.<\/jats:p>","DOI":"10.4049\/jimmunol.1900372","type":"journal-article","created":{"date-parts":[[2020,4,6]],"date-time":"2020-04-06T18:55:16Z","timestamp":1586199316000},"page":"2779-2790","source":"Crossref","is-referenced-by-count":26,"title":["Apolipoprotein E Triggers Complement Activation in Joint Synovial Fluid of Rheumatoid Arthritis Patients by Binding C1q"],"prefix":"10.1093","volume":"204","author":[{"ORCID":"https:\/\/orcid.org\/0000-0002-2843-9002","authenticated-orcid":false,"given":"Leonie M","family":"Vogt","sequence":"first","affiliation":[{"name":"Division of Medical Protein Chemistry, Department of Translational Medicine, Lund University , 21428 Malm\u00f6 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ewa","family":"Kwasniewicz","sequence":"additional","affiliation":[{"name":"Division of Medical Protein Chemistry, Department of Translational Medicine, Lund University , 21428 Malm\u00f6 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Simone","family":"Talens","sequence":"additional","affiliation":[{"name":"Division of Medical Protein Chemistry, Department of Translational Medicine, Lund University , 21428 Malm\u00f6 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-4304-0681","authenticated-orcid":false,"given":"Carsten","family":"Scavenius","sequence":"additional","affiliation":[{"name":"Department of Molecular Biology and Genetics, Aarhus University , 8000 Aarhus 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40202"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0002-1348-1734","authenticated-orcid":false,"given":"Anna M","family":"Blom","sequence":"additional","affiliation":[{"name":"Division of Medical Protein Chemistry, Department of Translational Medicine, Lund University , 21428 Malm\u00f6 ,","place":["Sweden"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"286","published-online":{"date-parts":[[2020,5,15]]},"reference":[{"key":"2025030417511866300_r1","doi-asserted-by":"crossref","first-page":"2023","DOI":"10.1016\/S0140-6736(16)30173-8","article-title":"Rheumatoid arthritis","volume":"388","author":"Smolen","year":"2016","journal-title":"Lancet"},{"key":"2025030417511866300_r2","doi-asserted-by":"crossref","first-page":"516","DOI":"10.1002\/art.40401","article-title":"Antibody responses to citrullinated and noncitrullinated antigens in the sputum of subjects with rheumatoid arthritis and subjects at risk for development of 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