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Factor H binds to washed human platelets
Lunds universitet.ORCID iD: 0000-0002-9953-2829
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2005 (English)In: Journal of Thrombosis and Haemostasis, ISSN 1538-7933, E-ISSN 1538-7836, Vol. 3, no 1, p. 154-162Article in journal (Refereed) Published
Abstract [en]

Background: Factor H regulates the alternative pathway of complement. The protein has three heparin-binding sites, is synthesized primarily in the liver and copurifies from platelets with thrombospondin-1. Factor H mutations at the C-terminus are associated with atypical hemolytic uremic syndrome, a condition in which platelets are consumed. Objectives The aim of this study was to investigate if factor H interacts with platelets.

Methods: Binding of factor H, recombinant G or N-terminus constructs and a C-terminus mutant to washed (plasma and complement-free) platelets was analyzed by flow cytometry. Binding of factor H and constructs to thrombospondin-1 was measured by surface plasmon resonance.

Results: Factor H bound to platelets in a dose-dependent manner. The major binding site was localized to the C-terminus. The interaction was partially blocked by heparin. Inhibition with anti-GPIIb/IIIa, or with fibrinogen, suggested that the platelet GPIIb/IIIa receptor is involved in factor H binding. Factor H binds to thrombospondin-1. Addition of thrombospondin-1 increased factor H binding to platelets. Factor H mutated at the C-terminus also bound to platelets, albeit to a significantly lesser degree.

Conclusions: This study reports a novel property of factor H, i.e. binding to platelets, either directly via the GPIIb/IIIa receptor or indirectly via thrombospondin-1, in the absence of complement. Binding to platelets was mostly mediated by the C-terminal region of factor H and factor H mutated at the C-terminus exhibited reduced binding.

Place, publisher, year, edition, pages
2005. Vol. 3, no 1, p. 154-162
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Cell and Molecular Biology
Identifiers
URN: urn:nbn:se:hkr:diva-12662DOI: 10.1111/j.1538-7836.2004.01010.xISI: 000226380500024PubMedID: 15634279OAI: oai:DiVA.org:hkr-12662DiVA, id: diva2:739741
Available from: 2014-08-21 Created: 2014-08-21 Last updated: 2018-01-11Bibliographically approved

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Vaziri-Sani, Fariba

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