The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors

© 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, ma...

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Main Authors: Anggayasti, Wresti Listu, Mancera, Ricardo, Bottomley, Steven, Helmerhorst, Erik
Format: Journal Article
Published: Elsevier 2017
Online Access:http://hdl.handle.net/20.500.11937/51012
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author Anggayasti, Wresti Listu
Mancera, Ricardo
Bottomley, Steven
Helmerhorst, Erik
author_facet Anggayasti, Wresti Listu
Mancera, Ricardo
Bottomley, Steven
Helmerhorst, Erik
author_sort Anggayasti, Wresti Listu
building Curtin Institutional Repository
collection Online Access
description © 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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institution Curtin University Malaysia
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publishDate 2017
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spelling curtin-20.500.11937-510122017-09-13T15:35:12Z The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors Anggayasti, Wresti Listu Mancera, Ricardo Bottomley, Steven Helmerhorst, Erik © 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. 2017 Journal Article http://hdl.handle.net/20.500.11937/51012 10.1002/1873-3468.12545 Elsevier unknown
spellingShingle Anggayasti, Wresti Listu
Mancera, Ricardo
Bottomley, Steven
Helmerhorst, Erik
The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors
title The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors
title_full The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors
title_fullStr The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors
title_full_unstemmed The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors
title_short The self-association of HMGB1 and its possible role in the binding to DNA and cell membrane receptors
title_sort self-association of hmgb1 and its possible role in the binding to dna and cell membrane receptors
url http://hdl.handle.net/20.500.11937/51012