The extracellular release of Schistosoma mansoni HMGB1 nuclear protein is mediated by acetylation
Schistosoma mansoni HMGB1 (SmHMGB1) was revealed to be a substrate for the parasite histone acetyltransferases SmGCN5 and SmCBP1. We found that full-length SmHMGB1, as well as its HMG-box B (but not HMG-box A) were acetylated in vitro by SmGCN5 and SmCBP1. However, SmCBP1 was able to acetylate both...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2009-12, Vol.390 (4), p.1245-1249 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1249 |
|---|---|
| container_issue | 4 |
| container_start_page | 1245 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 390 |
| creator | Carneiro, Vitor Coutinho de Moraes Maciel, Renata de Abreu da Silva, Isabel Caetano da Costa, Rodrigo Furtado Madeira Paiva, Claudia Neto Bozza, Marcelo Torres Fantappié, Marcelo Rosado |
| description | Schistosoma mansoni HMGB1 (SmHMGB1) was revealed to be a substrate for the parasite histone acetyltransferases SmGCN5 and SmCBP1. We found that full-length SmHMGB1, as well as its HMG-box B (but not HMG-box A) were acetylated
in vitro by SmGCN5 and SmCBP1. However, SmCBP1 was able to acetylate both substrates more efficiently than SmGCN5. Interestingly, the removal of the C-terminal acidic tail of SmHMGB1 (SmHMGB1ΔC) resulted in increased acetylation of the protein. We showed by mammalian cell transfection assays that SmHMGB1 and SmHMGB1ΔC were transported from the nucleus to the cytoplasm after sodium butyrate (NaB) treatment. Importantly, after NaB treatment, SmHMGB1 was also present outside the cell. Together, our data suggest that acetylation of SmHMGB1 plays a role in cellular trafficking, culminating with its secretion to the extracellular milieu. The possible role of SmHMGB1 acetylation in the pathogenesis of schistosomiasis is discussed. |
| doi_str_mv | 10.1016/j.bbrc.2009.10.129 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_22199937</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X09021202</els_id><sourcerecordid>877570183</sourcerecordid><originalsourceid>FETCH-LOGICAL-c525t-1222cdb6eea12e2200afecccc4e215744c5658f44226a7d8f1f4f28b68427f583</originalsourceid><addsrcrecordid>eNqFkUGLFDEQhYMo7rj6BzxIwIOnHpOadNIBL-6iu8KKB1fwFtLpCpOhu7MmaXH-vWlnwJvmUlB89ch7j5CXnG054_LtYdv3yW2BMb1dd6AfkQ1nmjXAmXhMNowx2YDm3y_Is5wPjHEupH5KLrjulAYhNsTe75Hir5Ksw3FcRptowhFtRho9_er2IZeY42TpZOcc50BvP99ccTovrlKJPqRYMMw0ZDrhEGzBgfZHWtXKcbQlxPk5eeLtmPHFeV6Sbx8_3F_fNndfbj5dv79rXAttaTgAuKGXiJYDQjVlPbr6BAJvlRCulW3nhQCQVg2d51546HrZCVC-7XaX5PVJN-YSTHahoNu7OM_oigHgWuudqtSbE1U__mPBXMwU8mrdzhiXbDqlWsV4t_svqXaCSybblYQT6VLMOaE3DylMNh0NZ2ZtyhzM2pRZm_qzA12PXp3ll74m9_fkXE0F3p0ArKH9DJhWTzi7mnJaLQ0x_Ev_NwVupBg</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>734160653</pqid></control><display><type>article</type><title>The extracellular release of Schistosoma mansoni HMGB1 nuclear protein is mediated by acetylation</title><source>MEDLINE</source><source>ScienceDirect Journals (5 years ago - present)</source><creator>Carneiro, Vitor Coutinho ; de Moraes Maciel, Renata ; de Abreu da Silva, Isabel Caetano ; da Costa, Rodrigo Furtado Madeira ; Paiva, Claudia Neto ; Bozza, Marcelo Torres ; Fantappié, Marcelo Rosado</creator><creatorcontrib>Carneiro, Vitor Coutinho ; de Moraes Maciel, Renata ; de Abreu da Silva, Isabel Caetano ; da Costa, Rodrigo Furtado Madeira ; Paiva, Claudia Neto ; Bozza, Marcelo Torres ; Fantappié, Marcelo Rosado</creatorcontrib><description>Schistosoma mansoni HMGB1 (SmHMGB1) was revealed to be a substrate for the parasite histone acetyltransferases SmGCN5 and SmCBP1. We found that full-length SmHMGB1, as well as its HMG-box B (but not HMG-box A) were acetylated
in vitro by SmGCN5 and SmCBP1. However, SmCBP1 was able to acetylate both substrates more efficiently than SmGCN5. Interestingly, the removal of the C-terminal acidic tail of SmHMGB1 (SmHMGB1ΔC) resulted in increased acetylation of the protein. We showed by mammalian cell transfection assays that SmHMGB1 and SmHMGB1ΔC were transported from the nucleus to the cytoplasm after sodium butyrate (NaB) treatment. Importantly, after NaB treatment, SmHMGB1 was also present outside the cell. Together, our data suggest that acetylation of SmHMGB1 plays a role in cellular trafficking, culminating with its secretion to the extracellular milieu. The possible role of SmHMGB1 acetylation in the pathogenesis of schistosomiasis is discussed.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2009.10.129</identifier><identifier>PMID: 19879244</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; ACETYLATION ; Active Transport, Cell Nucleus ; Animals ; Cell Nucleus - metabolism ; Cells, Cultured ; CYTOPLASM ; Histone Acetyltransferases - metabolism ; HMGB1 ; HMGB1 Protein - metabolism ; IN VITRO ; INFLAMMATION ; PATHOGENESIS ; PROTEINS ; SCHISTOSOMA ; Schistosoma mansoni ; Schistosoma mansoni - metabolism ; SCHISTOSOMIASIS ; Schistosomiasis mansoni - parasitology ; SECRETION ; SODIUM ; SUBSTRATES</subject><ispartof>Biochemical and biophysical research communications, 2009-12, Vol.390 (4), p.1245-1249</ispartof><rights>2009 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c525t-1222cdb6eea12e2200afecccc4e215744c5658f44226a7d8f1f4f28b68427f583</citedby><cites>FETCH-LOGICAL-c525t-1222cdb6eea12e2200afecccc4e215744c5658f44226a7d8f1f4f28b68427f583</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.bbrc.2009.10.129$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,780,784,885,3548,27922,27923,45993</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19879244$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/22199937$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Carneiro, Vitor Coutinho</creatorcontrib><creatorcontrib>de Moraes Maciel, Renata</creatorcontrib><creatorcontrib>de Abreu da Silva, Isabel Caetano</creatorcontrib><creatorcontrib>da Costa, Rodrigo Furtado Madeira</creatorcontrib><creatorcontrib>Paiva, Claudia Neto</creatorcontrib><creatorcontrib>Bozza, Marcelo Torres</creatorcontrib><creatorcontrib>Fantappié, Marcelo Rosado</creatorcontrib><title>The extracellular release of Schistosoma mansoni HMGB1 nuclear protein is mediated by acetylation</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Schistosoma mansoni HMGB1 (SmHMGB1) was revealed to be a substrate for the parasite histone acetyltransferases SmGCN5 and SmCBP1. We found that full-length SmHMGB1, as well as its HMG-box B (but not HMG-box A) were acetylated
in vitro by SmGCN5 and SmCBP1. However, SmCBP1 was able to acetylate both substrates more efficiently than SmGCN5. Interestingly, the removal of the C-terminal acidic tail of SmHMGB1 (SmHMGB1ΔC) resulted in increased acetylation of the protein. We showed by mammalian cell transfection assays that SmHMGB1 and SmHMGB1ΔC were transported from the nucleus to the cytoplasm after sodium butyrate (NaB) treatment. Importantly, after NaB treatment, SmHMGB1 was also present outside the cell. Together, our data suggest that acetylation of SmHMGB1 plays a role in cellular trafficking, culminating with its secretion to the extracellular milieu. The possible role of SmHMGB1 acetylation in the pathogenesis of schistosomiasis is discussed.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>ACETYLATION</subject><subject>Active Transport, Cell Nucleus</subject><subject>Animals</subject><subject>Cell Nucleus - metabolism</subject><subject>Cells, Cultured</subject><subject>CYTOPLASM</subject><subject>Histone Acetyltransferases - metabolism</subject><subject>HMGB1</subject><subject>HMGB1 Protein - metabolism</subject><subject>IN VITRO</subject><subject>INFLAMMATION</subject><subject>PATHOGENESIS</subject><subject>PROTEINS</subject><subject>SCHISTOSOMA</subject><subject>Schistosoma mansoni</subject><subject>Schistosoma mansoni - metabolism</subject><subject>SCHISTOSOMIASIS</subject><subject>Schistosomiasis mansoni - parasitology</subject><subject>SECRETION</subject><subject>SODIUM</subject><subject>SUBSTRATES</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkUGLFDEQhYMo7rj6BzxIwIOnHpOadNIBL-6iu8KKB1fwFtLpCpOhu7MmaXH-vWlnwJvmUlB89ch7j5CXnG054_LtYdv3yW2BMb1dd6AfkQ1nmjXAmXhMNowx2YDm3y_Is5wPjHEupH5KLrjulAYhNsTe75Hir5Ksw3FcRptowhFtRho9_er2IZeY42TpZOcc50BvP99ccTovrlKJPqRYMMw0ZDrhEGzBgfZHWtXKcbQlxPk5eeLtmPHFeV6Sbx8_3F_fNndfbj5dv79rXAttaTgAuKGXiJYDQjVlPbr6BAJvlRCulW3nhQCQVg2d51546HrZCVC-7XaX5PVJN-YSTHahoNu7OM_oigHgWuudqtSbE1U__mPBXMwU8mrdzhiXbDqlWsV4t_svqXaCSybblYQT6VLMOaE3DylMNh0NZ2ZtyhzM2pRZm_qzA12PXp3ll74m9_fkXE0F3p0ArKH9DJhWTzi7mnJaLQ0x_Ev_NwVupBg</recordid><startdate>20091225</startdate><enddate>20091225</enddate><creator>Carneiro, Vitor Coutinho</creator><creator>de Moraes Maciel, Renata</creator><creator>de Abreu da Silva, Isabel Caetano</creator><creator>da Costa, Rodrigo Furtado Madeira</creator><creator>Paiva, Claudia Neto</creator><creator>Bozza, Marcelo Torres</creator><creator>Fantappié, Marcelo Rosado</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>C1K</scope><scope>F1W</scope><scope>H95</scope><scope>H97</scope><scope>L.G</scope><scope>OTOTI</scope></search><sort><creationdate>20091225</creationdate><title>The extracellular release of Schistosoma mansoni HMGB1 nuclear protein is mediated by acetylation</title><author>Carneiro, Vitor Coutinho ; de Moraes Maciel, Renata ; de Abreu da Silva, Isabel Caetano ; da Costa, Rodrigo Furtado Madeira ; Paiva, Claudia Neto ; Bozza, Marcelo Torres ; Fantappié, Marcelo Rosado</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c525t-1222cdb6eea12e2200afecccc4e215744c5658f44226a7d8f1f4f28b68427f583</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>ACETYLATION</topic><topic>Active Transport, Cell Nucleus</topic><topic>Animals</topic><topic>Cell Nucleus - metabolism</topic><topic>Cells, Cultured</topic><topic>CYTOPLASM</topic><topic>Histone Acetyltransferases - metabolism</topic><topic>HMGB1</topic><topic>HMGB1 Protein - metabolism</topic><topic>IN VITRO</topic><topic>INFLAMMATION</topic><topic>PATHOGENESIS</topic><topic>PROTEINS</topic><topic>SCHISTOSOMA</topic><topic>Schistosoma mansoni</topic><topic>Schistosoma mansoni - metabolism</topic><topic>SCHISTOSOMIASIS</topic><topic>Schistosomiasis mansoni - parasitology</topic><topic>SECRETION</topic><topic>SODIUM</topic><topic>SUBSTRATES</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Carneiro, Vitor Coutinho</creatorcontrib><creatorcontrib>de Moraes Maciel, Renata</creatorcontrib><creatorcontrib>de Abreu da Silva, Isabel Caetano</creatorcontrib><creatorcontrib>da Costa, Rodrigo Furtado Madeira</creatorcontrib><creatorcontrib>Paiva, Claudia Neto</creatorcontrib><creatorcontrib>Bozza, Marcelo Torres</creatorcontrib><creatorcontrib>Fantappié, Marcelo Rosado</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ASFA: Aquatic Sciences and Fisheries Abstracts</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 1: Biological Sciences & Living Resources</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) 3: Aquatic Pollution & Environmental Quality</collection><collection>Aquatic Science & Fisheries Abstracts (ASFA) Professional</collection><collection>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Carneiro, Vitor Coutinho</au><au>de Moraes Maciel, Renata</au><au>de Abreu da Silva, Isabel Caetano</au><au>da Costa, Rodrigo Furtado Madeira</au><au>Paiva, Claudia Neto</au><au>Bozza, Marcelo Torres</au><au>Fantappié, Marcelo Rosado</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The extracellular release of Schistosoma mansoni HMGB1 nuclear protein is mediated by acetylation</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2009-12-25</date><risdate>2009</risdate><volume>390</volume><issue>4</issue><spage>1245</spage><epage>1249</epage><pages>1245-1249</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Schistosoma mansoni HMGB1 (SmHMGB1) was revealed to be a substrate for the parasite histone acetyltransferases SmGCN5 and SmCBP1. We found that full-length SmHMGB1, as well as its HMG-box B (but not HMG-box A) were acetylated
in vitro by SmGCN5 and SmCBP1. However, SmCBP1 was able to acetylate both substrates more efficiently than SmGCN5. Interestingly, the removal of the C-terminal acidic tail of SmHMGB1 (SmHMGB1ΔC) resulted in increased acetylation of the protein. We showed by mammalian cell transfection assays that SmHMGB1 and SmHMGB1ΔC were transported from the nucleus to the cytoplasm after sodium butyrate (NaB) treatment. Importantly, after NaB treatment, SmHMGB1 was also present outside the cell. Together, our data suggest that acetylation of SmHMGB1 plays a role in cellular trafficking, culminating with its secretion to the extracellular milieu. The possible role of SmHMGB1 acetylation in the pathogenesis of schistosomiasis is discussed.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>19879244</pmid><doi>10.1016/j.bbrc.2009.10.129</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2009-12, Vol.390 (4), p.1245-1249 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_osti_scitechconnect_22199937 |
| source | MEDLINE; ScienceDirect Journals (5 years ago - present) |
| subjects | 60 APPLIED LIFE SCIENCES ACETYLATION Active Transport, Cell Nucleus Animals Cell Nucleus - metabolism Cells, Cultured CYTOPLASM Histone Acetyltransferases - metabolism HMGB1 HMGB1 Protein - metabolism IN VITRO INFLAMMATION PATHOGENESIS PROTEINS SCHISTOSOMA Schistosoma mansoni Schistosoma mansoni - metabolism SCHISTOSOMIASIS Schistosomiasis mansoni - parasitology SECRETION SODIUM SUBSTRATES |
| title | The extracellular release of Schistosoma mansoni HMGB1 nuclear protein is mediated by acetylation |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-10T06%3A11%3A13IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_osti_&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=The%20extracellular%20release%20of%20Schistosoma%20mansoni%20HMGB1%20nuclear%20protein%20is%20mediated%20by%20acetylation&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Carneiro,%20Vitor%20Coutinho&rft.date=2009-12-25&rft.volume=390&rft.issue=4&rft.spage=1245&rft.epage=1249&rft.pages=1245-1249&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2009.10.129&rft_dat=%3Cproquest_osti_%3E877570183%3C/proquest_osti_%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=734160653&rft_id=info:pmid/19879244&rft_els_id=S0006291X09021202&rfr_iscdi=true |