Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes
Human heat shock protein Hsp70 was experimentally inserted into polyelectrolyte microcapsules. Encapsulated recombinant Hsp70 was studied in terms of its effects on neutrophil apoptosis, the production of reactive oxygen species, and the secretion of tumor necrosis factor alpha by promonocytic THP-1...
Gespeichert in:
| Veröffentlicht in: | Cell stress & chaperones 2017-01, Vol.22 (1), p.163-171 |
|---|---|
| Hauptverfasser: | , , , , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 171 |
|---|---|
| container_issue | 1 |
| container_start_page | 163 |
| container_title | Cell stress & chaperones |
| container_volume | 22 |
| creator | Yurinskaya, M.M. Kochetkova, O.Yu Shabarchina, L.I. Antonova, O.Yu Suslikov, A.V. Evgen'ev, M.B. Vinokurov, M.G. |
| description | Human heat shock protein Hsp70 was experimentally inserted into polyelectrolyte microcapsules. Encapsulated recombinant Hsp70 was studied in terms of its effects on neutrophil apoptosis, the production of reactive oxygen species, and the secretion of tumor necrosis factor alpha by promonocytic THP-1 cells. It was found that encapsulated Hsp70 effectively inhibits neutrophil apoptosis, unlike free exogenous protein used in solution. In THP-1 cells, encapsulated and free Hsp70 reduced LPS-induced tumor necrosis factor alpha production with a similar efficiency. Encapsulated Hsp70 reduces LPS-induced reactive oxygen species production by neutrophils in the course of its release from the microcapsules but not as much as free Hsp70. Thus, the polyelectrolyte microcapsules can be used as containers for the effective delivery of Hsp70 to neutrophils and monocytes to significantly improve the functioning of the innate immune system. |
| doi_str_mv | 10.1007/s12192-016-0743-z |
| format | Article |
| fullrecord | <record><control><sourceid>jstor_pubme</sourceid><recordid>TN_cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5225061</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><jstor_id>44848843</jstor_id><sourcerecordid>44848843</sourcerecordid><originalsourceid>FETCH-LOGICAL-c464t-fc04893cc4267c0493b882542520005ffcf6ac4f0cb36cedde2b0759a841efca3</originalsourceid><addsrcrecordid>eNp9kM1KJDEUhYMo48_MA7hQ8gLR_Ce9EUT8A1GYcbYT0qmku5rupEiqRH0rX8RnMlJOoxtX98A959zLB8A-wUcEY3VcCCUTijCRCCvO0PMG2CFcSkSo1JtVMyGQJlxsg91SFrhmlCI_wDZVSjOq-A74dx6d7cqwtL1v4FXpFIaNd9nb4gv0sUl9emwjamMzuOrocqqib1OEKcDfd3-gjQ28v714fYFthPNhZSPs5naW3FPvy0-wFeyy-F8fcw_8vTi_P7tCN3eX12enN8hxyXsUHOZ6wpzjVKqqJ2yqNRWcClqfFiG4IK3jAbspk_WNxtMpVmJiNSc-OMv2wMnY2w3TlW-cj322S9PldmXzk0m2NV83sZ2bWXowglKBJakFZCxwOZWSfVhnCTbvsM0I21TY5h22ea6Zw89H14n_dKuBjoZSV3Hms1mkIccK4tvWgzG0KH3K61LONdeaM_YG0iaXbA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype></control><display><type>article</type><title>Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes</title><source>Jstor Complete Legacy</source><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><source>Alma/SFX Local Collection</source><creator>Yurinskaya, M.M. ; Kochetkova, O.Yu ; Shabarchina, L.I. ; Antonova, O.Yu ; Suslikov, A.V. ; Evgen'ev, M.B. ; Vinokurov, M.G.</creator><creatorcontrib>Yurinskaya, M.M. ; Kochetkova, O.Yu ; Shabarchina, L.I. ; Antonova, O.Yu ; Suslikov, A.V. ; Evgen'ev, M.B. ; Vinokurov, M.G.</creatorcontrib><description>Human heat shock protein Hsp70 was experimentally inserted into polyelectrolyte microcapsules. Encapsulated recombinant Hsp70 was studied in terms of its effects on neutrophil apoptosis, the production of reactive oxygen species, and the secretion of tumor necrosis factor alpha by promonocytic THP-1 cells. It was found that encapsulated Hsp70 effectively inhibits neutrophil apoptosis, unlike free exogenous protein used in solution. In THP-1 cells, encapsulated and free Hsp70 reduced LPS-induced tumor necrosis factor alpha production with a similar efficiency. Encapsulated Hsp70 reduces LPS-induced reactive oxygen species production by neutrophils in the course of its release from the microcapsules but not as much as free Hsp70. Thus, the polyelectrolyte microcapsules can be used as containers for the effective delivery of Hsp70 to neutrophils and monocytes to significantly improve the functioning of the innate immune system.</description><identifier>ISSN: 1355-8145</identifier><identifier>EISSN: 1466-1268</identifier><identifier>DOI: 10.1007/s12192-016-0743-z</identifier><identifier>PMID: 27783274</identifier><language>eng</language><publisher>Dordrecht: Springer</publisher><subject>Apoptosis ; Biochemistry ; Biomedical and Life Sciences ; Biomedicine ; Cancer Research ; Capsules ; Cell Biology ; Cell lines ; Cells, Cultured ; Endotoxins ; Heat shock proteins ; HSP70 Heat-Shock Proteins - genetics ; HSP70 Heat-Shock Proteins - metabolism ; Humans ; Immunology ; Lipopolysaccharides - toxicity ; Microscopy, Confocal ; Monocytes - cytology ; Monocytes - drug effects ; Monocytes - metabolism ; Neurosciences ; Neutrophils ; Neutrophils - cytology ; Neutrophils - drug effects ; Neutrophils - metabolism ; Phagocytes ; Phagocytes - drug effects ; Phagocytosis ; Protective effects ; Reactive oxygen species ; Reactive Oxygen Species - metabolism ; Recombinant Proteins - biosynthesis ; Recombinant Proteins - isolation & purification ; SHORT COMMUNICATION ; Tumor Necrosis Factor-alpha - metabolism</subject><ispartof>Cell stress & chaperones, 2017-01, Vol.22 (1), p.163-171</ispartof><rights>Cell Stress Society International 2017</rights><rights>Cell Stress Society International 2016</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c464t-fc04893cc4267c0493b882542520005ffcf6ac4f0cb36cedde2b0759a841efca3</citedby><cites>FETCH-LOGICAL-c464t-fc04893cc4267c0493b882542520005ffcf6ac4f0cb36cedde2b0759a841efca3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/44848843$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/44848843$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>230,314,723,776,780,799,881,27901,27902,41464,42533,51294,53766,53768,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/27783274$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Yurinskaya, M.M.</creatorcontrib><creatorcontrib>Kochetkova, O.Yu</creatorcontrib><creatorcontrib>Shabarchina, L.I.</creatorcontrib><creatorcontrib>Antonova, O.Yu</creatorcontrib><creatorcontrib>Suslikov, A.V.</creatorcontrib><creatorcontrib>Evgen'ev, M.B.</creatorcontrib><creatorcontrib>Vinokurov, M.G.</creatorcontrib><title>Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes</title><title>Cell stress & chaperones</title><addtitle>Cell Stress and Chaperones</addtitle><addtitle>Cell Stress Chaperones</addtitle><description>Human heat shock protein Hsp70 was experimentally inserted into polyelectrolyte microcapsules. Encapsulated recombinant Hsp70 was studied in terms of its effects on neutrophil apoptosis, the production of reactive oxygen species, and the secretion of tumor necrosis factor alpha by promonocytic THP-1 cells. It was found that encapsulated Hsp70 effectively inhibits neutrophil apoptosis, unlike free exogenous protein used in solution. In THP-1 cells, encapsulated and free Hsp70 reduced LPS-induced tumor necrosis factor alpha production with a similar efficiency. Encapsulated Hsp70 reduces LPS-induced reactive oxygen species production by neutrophils in the course of its release from the microcapsules but not as much as free Hsp70. Thus, the polyelectrolyte microcapsules can be used as containers for the effective delivery of Hsp70 to neutrophils and monocytes to significantly improve the functioning of the innate immune system.</description><subject>Apoptosis</subject><subject>Biochemistry</subject><subject>Biomedical and Life Sciences</subject><subject>Biomedicine</subject><subject>Cancer Research</subject><subject>Capsules</subject><subject>Cell Biology</subject><subject>Cell lines</subject><subject>Cells, Cultured</subject><subject>Endotoxins</subject><subject>Heat shock proteins</subject><subject>HSP70 Heat-Shock Proteins - genetics</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Humans</subject><subject>Immunology</subject><subject>Lipopolysaccharides - toxicity</subject><subject>Microscopy, Confocal</subject><subject>Monocytes - cytology</subject><subject>Monocytes - drug effects</subject><subject>Monocytes - metabolism</subject><subject>Neurosciences</subject><subject>Neutrophils</subject><subject>Neutrophils - cytology</subject><subject>Neutrophils - drug effects</subject><subject>Neutrophils - metabolism</subject><subject>Phagocytes</subject><subject>Phagocytes - drug effects</subject><subject>Phagocytosis</subject><subject>Protective effects</subject><subject>Reactive oxygen species</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>Recombinant Proteins - biosynthesis</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>SHORT COMMUNICATION</subject><subject>Tumor Necrosis Factor-alpha - metabolism</subject><issn>1355-8145</issn><issn>1466-1268</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2017</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM1KJDEUhYMo48_MA7hQ8gLR_Ce9EUT8A1GYcbYT0qmku5rupEiqRH0rX8RnMlJOoxtX98A959zLB8A-wUcEY3VcCCUTijCRCCvO0PMG2CFcSkSo1JtVMyGQJlxsg91SFrhmlCI_wDZVSjOq-A74dx6d7cqwtL1v4FXpFIaNd9nb4gv0sUl9emwjamMzuOrocqqib1OEKcDfd3-gjQ28v714fYFthPNhZSPs5naW3FPvy0-wFeyy-F8fcw_8vTi_P7tCN3eX12enN8hxyXsUHOZ6wpzjVKqqJ2yqNRWcClqfFiG4IK3jAbspk_WNxtMpVmJiNSc-OMv2wMnY2w3TlW-cj322S9PldmXzk0m2NV83sZ2bWXowglKBJakFZCxwOZWSfVhnCTbvsM0I21TY5h22ea6Zw89H14n_dKuBjoZSV3Hms1mkIccK4tvWgzG0KH3K61LONdeaM_YG0iaXbA</recordid><startdate>20170101</startdate><enddate>20170101</enddate><creator>Yurinskaya, M.M.</creator><creator>Kochetkova, O.Yu</creator><creator>Shabarchina, L.I.</creator><creator>Antonova, O.Yu</creator><creator>Suslikov, A.V.</creator><creator>Evgen'ev, M.B.</creator><creator>Vinokurov, M.G.</creator><general>Springer</general><general>Springer Netherlands</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>5PM</scope></search><sort><creationdate>20170101</creationdate><title>Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes</title><author>Yurinskaya, M.M. ; Kochetkova, O.Yu ; Shabarchina, L.I. ; Antonova, O.Yu ; Suslikov, A.V. ; Evgen'ev, M.B. ; Vinokurov, M.G.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c464t-fc04893cc4267c0493b882542520005ffcf6ac4f0cb36cedde2b0759a841efca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2017</creationdate><topic>Apoptosis</topic><topic>Biochemistry</topic><topic>Biomedical and Life Sciences</topic><topic>Biomedicine</topic><topic>Cancer Research</topic><topic>Capsules</topic><topic>Cell Biology</topic><topic>Cell lines</topic><topic>Cells, Cultured</topic><topic>Endotoxins</topic><topic>Heat shock proteins</topic><topic>HSP70 Heat-Shock Proteins - genetics</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Humans</topic><topic>Immunology</topic><topic>Lipopolysaccharides - toxicity</topic><topic>Microscopy, Confocal</topic><topic>Monocytes - cytology</topic><topic>Monocytes - drug effects</topic><topic>Monocytes - metabolism</topic><topic>Neurosciences</topic><topic>Neutrophils</topic><topic>Neutrophils - cytology</topic><topic>Neutrophils - drug effects</topic><topic>Neutrophils - metabolism</topic><topic>Phagocytes</topic><topic>Phagocytes - drug effects</topic><topic>Phagocytosis</topic><topic>Protective effects</topic><topic>Reactive oxygen species</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>Recombinant Proteins - biosynthesis</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>SHORT COMMUNICATION</topic><topic>Tumor Necrosis Factor-alpha - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Yurinskaya, M.M.</creatorcontrib><creatorcontrib>Kochetkova, O.Yu</creatorcontrib><creatorcontrib>Shabarchina, L.I.</creatorcontrib><creatorcontrib>Antonova, O.Yu</creatorcontrib><creatorcontrib>Suslikov, A.V.</creatorcontrib><creatorcontrib>Evgen'ev, M.B.</creatorcontrib><creatorcontrib>Vinokurov, M.G.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cell stress & chaperones</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Yurinskaya, M.M.</au><au>Kochetkova, O.Yu</au><au>Shabarchina, L.I.</au><au>Antonova, O.Yu</au><au>Suslikov, A.V.</au><au>Evgen'ev, M.B.</au><au>Vinokurov, M.G.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes</atitle><jtitle>Cell stress & chaperones</jtitle><stitle>Cell Stress and Chaperones</stitle><addtitle>Cell Stress Chaperones</addtitle><date>2017-01-01</date><risdate>2017</risdate><volume>22</volume><issue>1</issue><spage>163</spage><epage>171</epage><pages>163-171</pages><issn>1355-8145</issn><eissn>1466-1268</eissn><abstract>Human heat shock protein Hsp70 was experimentally inserted into polyelectrolyte microcapsules. Encapsulated recombinant Hsp70 was studied in terms of its effects on neutrophil apoptosis, the production of reactive oxygen species, and the secretion of tumor necrosis factor alpha by promonocytic THP-1 cells. It was found that encapsulated Hsp70 effectively inhibits neutrophil apoptosis, unlike free exogenous protein used in solution. In THP-1 cells, encapsulated and free Hsp70 reduced LPS-induced tumor necrosis factor alpha production with a similar efficiency. Encapsulated Hsp70 reduces LPS-induced reactive oxygen species production by neutrophils in the course of its release from the microcapsules but not as much as free Hsp70. Thus, the polyelectrolyte microcapsules can be used as containers for the effective delivery of Hsp70 to neutrophils and monocytes to significantly improve the functioning of the innate immune system.</abstract><cop>Dordrecht</cop><pub>Springer</pub><pmid>27783274</pmid><doi>10.1007/s12192-016-0743-z</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 1355-8145 |
| ispartof | Cell stress & chaperones, 2017-01, Vol.22 (1), p.163-171 |
| issn | 1355-8145 1466-1268 |
| language | eng |
| recordid | cdi_pubmedcentral_primary_oai_pubmedcentral_nih_gov_5225061 |
| source | Jstor Complete Legacy; MEDLINE; Springer Nature - Complete Springer Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central; Alma/SFX Local Collection |
| subjects | Apoptosis Biochemistry Biomedical and Life Sciences Biomedicine Cancer Research Capsules Cell Biology Cell lines Cells, Cultured Endotoxins Heat shock proteins HSP70 Heat-Shock Proteins - genetics HSP70 Heat-Shock Proteins - metabolism Humans Immunology Lipopolysaccharides - toxicity Microscopy, Confocal Monocytes - cytology Monocytes - drug effects Monocytes - metabolism Neurosciences Neutrophils Neutrophils - cytology Neutrophils - drug effects Neutrophils - metabolism Phagocytes Phagocytes - drug effects Phagocytosis Protective effects Reactive oxygen species Reactive Oxygen Species - metabolism Recombinant Proteins - biosynthesis Recombinant Proteins - isolation & purification SHORT COMMUNICATION Tumor Necrosis Factor-alpha - metabolism |
| title | Encapsulated Hsp70 decreases endotoxin-induced production of ROS and TNFα in human phagocytes |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-21T21%3A22%3A17IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-jstor_pubme&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Encapsulated%20Hsp70%20decreases%20endotoxin-induced%20production%20of%20ROS%20and%20TNF%CE%B1%20in%20human%20phagocytes&rft.jtitle=Cell%20stress%20&%20chaperones&rft.au=Yurinskaya,%20M.M.&rft.date=2017-01-01&rft.volume=22&rft.issue=1&rft.spage=163&rft.epage=171&rft.pages=163-171&rft.issn=1355-8145&rft.eissn=1466-1268&rft_id=info:doi/10.1007/s12192-016-0743-z&rft_dat=%3Cjstor_pubme%3E44848843%3C/jstor_pubme%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_id=info:pmid/27783274&rft_jstor_id=44848843&rfr_iscdi=true |