Egyszerű nézet

dc.contributor.author Kopp A
dc.contributor.author Strobel S
dc.contributor.author Tortajada A
dc.contributor.author Rodriguez de Cordoba S
dc.contributor.author Sanchez-Corral P
dc.contributor.author Prohászka, Zoltán
dc.contributor.author Lopez-Trascasa M
dc.contributor.author Józsi, Mihály
dc.date.accessioned 2018-10-10T13:22:35Z
dc.date.available 2018-10-10T13:22:35Z
dc.date.issued 2012
dc.identifier 84864823657
dc.identifier.citation pagination=1858-1867; journalVolume=189; journalIssueNumber=4; journalTitle=JOURNAL OF IMMUNOLOGY;
dc.identifier.uri http://repo.lib.semmelweis.hu//handle/123456789/6352
dc.identifier.uri doi:10.4049/jimmunol.1200357
dc.description.abstract Atypical hemolytic uremic syndrome (aHUS) is a renal disease associated with complement alternative pathway dysregulation and is characterized by endothelial injury. Pentraxin 3 (PTX3) is a soluble pattern recognition molecule expressed by endothelial cells and upregulated under inflammatory conditions. PTX3 activates complement, but it also binds the complement inhibitor factor H. In this study, we show that native factor H, factor H-like protein 1, and factor H-related protein 1 (CFHR1) bind to PTX3 and that PTX3-bound factor H and factor H-like protein 1 maintain their complement regulatory activities. PTX3, when bound to extracellular matrix, recruited functionally active factor H. Residues within short consensus repeat 20 of factor H that are relevant for PTX3 binding were identified using a peptide array. aHUS-associated factor H mutations within this binding site caused a reduced factor H binding to PTX3. Similarly, seven of nine analyzed anti-factor H autoantibodies isolated from aHUS patients inhibited the interaction between factor H and PTX3, and five autoantibodies also inhibited PTX3 binding to CFHR1. Moreover, the aHUS-associated CFHR1*B variant showed reduced binding to PTX3 in comparison with CFHR1*A. Thus, the interactions of PTX3 with complement regulators are impaired by certain mutations and autoantibodies affecting factor H and CFHR1, which could result in an enhanced local complement-mediated inflammation, endothelial cell activation, and damage in aHUS.
dc.relation.ispartof urn:issn:0022-1767
dc.title Atypical hemolytic uremic syndrome-associated variants and autoantibodies impair binding of factor H and factor H-related protein 1 to pentraxin 3
dc.type Journal Article
dc.date.updated 2018-09-02T08:56:39Z
dc.language.rfc3066 en
dc.identifier.mtmt 2035763
dc.identifier.wos 000307216000038
dc.identifier.pubmed 22786770
dc.contributor.department SE/AOK/K/III. Sz. Belgyógyászati Klinika
dc.contributor.institution Semmelweis Egyetem


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