The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors
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© 2016 Federation of European Biochemical SocietiesHigh mobility group box 1 (HMGB1), a chromatin protein, interacts with DNA and controls gene expression. However, when HMGB1 is released from apoptotic or damaged cells, it triggers proinflammatory reactions by interacting with various receptors, mainly receptor for advanced glycation end-products (RAGE) and toll-like receptors (TLRs). The self-association of HMGB1 has been found to be crucial for its DNA-related biological functions. It is influenced by several factors, such as ionic strength, pH, specific divalent metal cations, redox environment and acetylation. This self-association may also play a role in the interaction with RAGE and TLRs and the concomitant inflammatory responses. Future studies should address the potential role of HMGB1 self-association on its interactions with DNA, RAGE and TLRs, as well as the influence of physicochemical factors in different cellular environments on these interactions.
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The effect of physicochemical factors on the self-association of HMGB1: A surface plasmon resonance studyAnggayasti, W.; Mancera, Ricardo; Bottomley, S.; Helmerhorst, Erik (2016)© 2016 Elsevier B.V. HMGB1 triggers proinflammatory reactions by interacting extracellularly with various receptors. HMGB1 also acts in the nucleus by interacting with DNA and controlling DNA transcription, a process which ...
The self-association of High Mobility Group Box 1 (HMGB1): Implications for interaction with Receptor for Advanced Glycation End-products (RAGE) and DNAAnggayasti, Wresti Listu (2015)High Mobility Group Box 1 (HMGB1) plays key roles in inflammatory diseases including cancer and diabetes. Intracellularly, HMGB1 binds DNA and assists transcription. Extracellularly, HMGB1 promotes inflammatory responses ...
Optimization of surface plasmon resonance experiments: Case of high mobility group box 1 (HMGB1) interactionsAnggayasti, W.; Mancera, Ricardo; Bottomley, Steven; Helmerhorst, Erik (2016)© 2016 Elsevier Inc. All rights reserved. Surface plasmon resonance (SPR) is a powerful technique for evaluating protein-protein interactions in real time. However, inappropriately optimized experiments can often lead to ...