The self‐association of HMGB 1 and its possible role in the binding to DNA and cell membrane receptors
High mobility group box 1 ( HMGB 1), a chromatin protein, interacts with DNA and controls gene expression. However, when HMGB 1 is released from apoptotic or damaged cells, it triggers proinflammatory reactions by interacting with various receptors, mainly receptor for advanced glycation end‐product...
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creator | Anggayasti, Wresti L. Mancera, Ricardo L. Bottomley, Steve Helmerhorst, Erik |
description | High mobility group box 1 (
HMGB
1), a chromatin protein, interacts with
DNA
and controls gene expression. However, when
HMGB
1 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 (
TLR
s). The self‐association of
HMGB
1 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
TLR
s and the concomitant inflammatory responses. Future studies should address the potential role of
HMGB
1 self‐association on its interactions with
DNA
,
RAGE
and
TLR
s, as well as the influence of physicochemical factors in different cellular environments on these interactions. |
doi_str_mv | 10.1002/1873-3468.12545 |
format | Article |
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HMGB
1), a chromatin protein, interacts with
DNA
and controls gene expression. However, when
HMGB
1 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 (
TLR
s). The self‐association of
HMGB
1 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
TLR
s and the concomitant inflammatory responses. Future studies should address the potential role of
HMGB
1 self‐association on its interactions with
DNA
,
RAGE
and
TLR
s, as well as the influence of physicochemical factors in different cellular environments on these interactions.</description><identifier>ISSN: 0014-5793</identifier><identifier>EISSN: 1873-3468</identifier><identifier>DOI: 10.1002/1873-3468.12545</identifier><language>eng</language><ispartof>FEBS letters, 2017-01, Vol.591 (2), p.282-294</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c865-9a57cc883e0405760cb523017ae71220f3c8f3bd01de922d6afe4e470b8546083</citedby><cites>FETCH-LOGICAL-c865-9a57cc883e0405760cb523017ae71220f3c8f3bd01de922d6afe4e470b8546083</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,777,781,27905,27906</link.rule.ids></links><search><creatorcontrib>Anggayasti, Wresti L.</creatorcontrib><creatorcontrib>Mancera, Ricardo L.</creatorcontrib><creatorcontrib>Bottomley, Steve</creatorcontrib><creatorcontrib>Helmerhorst, Erik</creatorcontrib><title>The self‐association of HMGB 1 and its possible role in the binding to DNA and cell membrane receptors</title><title>FEBS letters</title><description>High mobility group box 1 (
HMGB
1), a chromatin protein, interacts with
DNA
and controls gene expression. However, when
HMGB
1 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 (
TLR
s). The self‐association of
HMGB
1 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
TLR
s and the concomitant inflammatory responses. Future studies should address the potential role of
HMGB
1 self‐association on its interactions with
DNA
,
RAGE
and
TLR
s, as well as the influence of physicochemical factors in different cellular environments on these interactions.</description><issn>0014-5793</issn><issn>1873-3468</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><recordid>eNo9kE1OwzAQhS0EEqWwZusLpB3_xc6yFGiRCmy6jxxnTI3SuLKzYccROCMnIS2IzRu9pzej0UfILYMZA-BzZrQohCzNjHEl1RmZ_CfnZALAZKF0JS7JVc7vMHrDqgnZbXdIM3b--_PL5hxdsEOIPY2erp9Xd5RR27c0DJkeYs6h6ZCmOEro6TBuNqFvQ_9Gh0jvXxanrsOuo3vcN8n2YxkdHoaY8jW58LbLePM3p2T7-LBdrovN6-ppudgUzpSqqKzSzhkjECQoXYJrFBfAtEXNOAcvnPGiaYG1WHHeltajRKmhMUqWYMSUzH_PujT-m9DXhxT2Nn3UDOojp_pIpT5SqU-cxA-C2Vpz</recordid><startdate>201701</startdate><enddate>201701</enddate><creator>Anggayasti, Wresti L.</creator><creator>Mancera, Ricardo L.</creator><creator>Bottomley, Steve</creator><creator>Helmerhorst, Erik</creator><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>201701</creationdate><title>The self‐association of HMGB 1 and its possible role in the binding to DNA and cell membrane receptors</title><author>Anggayasti, Wresti L. ; Mancera, Ricardo L. ; Bottomley, Steve ; Helmerhorst, Erik</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c865-9a57cc883e0405760cb523017ae71220f3c8f3bd01de922d6afe4e470b8546083</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Anggayasti, Wresti L.</creatorcontrib><creatorcontrib>Mancera, Ricardo L.</creatorcontrib><creatorcontrib>Bottomley, Steve</creatorcontrib><creatorcontrib>Helmerhorst, Erik</creatorcontrib><collection>CrossRef</collection><jtitle>FEBS letters</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Anggayasti, Wresti L.</au><au>Mancera, Ricardo L.</au><au>Bottomley, Steve</au><au>Helmerhorst, Erik</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The self‐association of HMGB 1 and its possible role in the binding to DNA and cell membrane receptors</atitle><jtitle>FEBS letters</jtitle><date>2017-01</date><risdate>2017</risdate><volume>591</volume><issue>2</issue><spage>282</spage><epage>294</epage><pages>282-294</pages><issn>0014-5793</issn><eissn>1873-3468</eissn><abstract>High mobility group box 1 (
HMGB
1), a chromatin protein, interacts with
DNA
and controls gene expression. However, when
HMGB
1 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 (
TLR
s). The self‐association of
HMGB
1 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
TLR
s and the concomitant inflammatory responses. Future studies should address the potential role of
HMGB
1 self‐association on its interactions with
DNA
,
RAGE
and
TLR
s, as well as the influence of physicochemical factors in different cellular environments on these interactions.</abstract><doi>10.1002/1873-3468.12545</doi><tpages>13</tpages></addata></record> |
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source | Wiley Online Library Journals Frontfile Complete; Wiley Free Content; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
title | The self‐association of HMGB 1 and its possible role in the binding to DNA and cell membrane receptors |
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