title: Adsorption of the inflammatory mediator high-mobility group box 1 by polymers with different charge and porosity.
abstract: High-mobility group box 1 protein (HMGB1) is a conserved protein with a variety of biological functions inside as well as outside the cell. When released by activated immune cells, it acts as a proinflammatory cytokine. Its delayed release has sparked the interest in HMGB1 as a potential therapeutic target. Here, we studied the adsorption of HMGB1 to anionic methacrylate-based polymers as well as to neutral polystyrene-divinylbenzene copolymers. Both groups of adsorbents exhibited efficient binding of recombinant HMGB1 and of HMGB1 derived from lipopolysaccharide-stimulated peripheral blood mononuclear cells. The adsorption characteristics depended on particle size, porosity, accessibility of the pores, and charge of the polymers. In addition to these physicochemical parameters of the adsorbents, modifications of the molecule itself (e.g., acetylation, phosphorylation, and oxidation), interaction with other plasma proteins or anticoagulants (e.g., heparin), or association with extracellular microvesicles may influence the binding of HMGB1 to adsorbents and lead to preferential depletion of HMGB1 subsets with different biological activity.
authors.affiliation: Christian Doppler Laboratory for Innovative Therapy Approaches in Sepsis, Department for Health Sciences and Biomedicine, Danube University Krems, Dr.-Karl-Dorrek-Straße 30, 3500 Krems, Austria.
authors.forename: Carla
authors.identifier: 0000-0002-3680-2668
authors.initials: C
authors.lastname: Tripisciano
authors.affiliation: Christian Doppler Laboratory for Innovative Therapy Approaches in Sepsis, Department for Health Sciences and Biomedicine, Danube University Krems, Dr.-Karl-Dorrek-Straße 30, 3500 Krems, Austria.
authors.forename: Tanja
authors.identifier: 0000-0003-4158-026X
authors.initials: T
authors.lastname: Eichhorn
authors.affiliation: Center for Biomedical Technology, Department for Health Sciences and Biomedicine, Danube University Krems, Dr.-Karl-Dorrek-Straße 30, 3500 Krems, Austria.
authors.forename: Stephan
authors.initials: S
authors.lastname: Harm
authors.affiliation: Christian Doppler Laboratory for Innovative Therapy Approaches in Sepsis, Department for Health Sciences and Biomedicine, Danube University Krems, Dr.-Karl-Dorrek-Straße 30, 3500 Krems, Austria ; Center for Biomedical Technology, Department for Health Sciences and Biomedicine, Danube University Krems, Dr.-Karl-Dorrek-Straße 30, 3500 Krems, Austria.
authors.forename: Viktoria
authors.initials: V
authors.lastname: Weber
mesh_terms: D000327:Adsorption; D000328:Adult; D024243:HMGB1 Protein / Q000378:metabolism*; D006801:Humans; D018836:Inflammation Mediators / Q000378:metabolism*; D007963:Leukocytes, Mononuclear / Q000378:metabolism; D008854:Microscopy, Electron; D009584:Nitrogen; D011108:Polymers / Q000737:chemistry*; D016062:Porosity; D012709:Serum Albumin / Q000378:metabolism; D013696:Temperature
chemical_list: D024243:HMGB1 Protein; D018836:Inflammation Mediators; D011108:Polymers; D012709:Serum Albumin; D009584:Nitrogen