Ubiquitin C-terminal hydrolase-L1 plays a key role in angiogenesis by regulating hydrogen peroxide generated by NADPH oxidase 4
Ubiquitin C-terminal hydrolase-L1 (UCH-L1), which catalyzes the hydrolysis of ubiquitin esters and amides, is highly expressed in brain. Recently, UCH-L1 has been found to increase cancer cell migration and invasion by modulating hydrogen peroxide generated by NADPH oxidase 4 (NOX4). Because angioge...
Gespeichert in:
| Veröffentlicht in: | Biochemical and biophysical research communications 2018-01, Vol.495 (1), p.1567-1572 |
|---|---|
| Hauptverfasser: | , , , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 1572 |
|---|---|
| container_issue | 1 |
| container_start_page | 1567 |
| container_title | Biochemical and biophysical research communications |
| container_volume | 495 |
| creator | Song, In-Kang Kim, Hyun Jung Magesh, Venkataraman Lee, Kong-Joo |
| description | Ubiquitin C-terminal hydrolase-L1 (UCH-L1), which catalyzes the hydrolysis of ubiquitin esters and amides, is highly expressed in brain. Recently, UCH-L1 has been found to increase cancer cell migration and invasion by modulating hydrogen peroxide generated by NADPH oxidase 4 (NOX4). Because angiogenesis is also mediated by hydrogen peroxide, we explored the role of UCH-L1 in angiogenesis in human umbilical vein endothelial cells (HUVECs). Silencing UCH-L1 suppressed tubule formation in HUVECs, indicating that UCH-L1 promotes angiogenesis in vitro. This was confirmed using in vivo Matrigel plug studies of HUVECs, after overexpressing or silencing UCH-L1. Silencing UCH-L1 significantly suppressed VEGF-induced ROS levels as well as activation of VEGFR, both of which are required for angiogenesis. This study also showed that UCH-L1 promotes angiogenesis of HUVECs, as well as invasion in cancer cells, by up-regulating ROS by deubiquitination of NOX4, suggesting that UCH-L1 plays a key role in angiogenesis of HUVECS by regulating ROS levels by deubiquitination of NOX4. |
| doi_str_mv | 10.1016/j.bbrc.2017.11.051 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_osti_</sourceid><recordid>TN_cdi_osti_scitechconnect_23134408</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><els_id>S0006291X17322295</els_id><sourcerecordid>1963468496</sourcerecordid><originalsourceid>FETCH-LOGICAL-c450t-25f2e76ab72454c8959eafa97a9f39aa10f48bf61918bd0a5cca09015aacd8403</originalsourceid><addsrcrecordid>eNp9kUFv1DAQhS0EotuFP8ABWeLCJcHjONlY4lJtgSKtgAOVuFkTZ7L1ko23doLYE3-9jlI4chrpzfeeRvMYewUiBwHVu0PeNMHmUsAmB8hFCU_YCoQWmQShnrKVEKLKpIYfF-wyxoMQAKrSz9lF0mRdlHrF_tw27n5yoxv4NhspHN2APb87t8H3GCnbAT_1eI4c-U8686QSTywOe-f3NFB0kTdJp_3UY0rZL9604icK_rdric9cwJHamfxydf3ths-LFM_VC_aswz7Sy8e5ZrcfP3zf3mS7r58-b692mVWlGDNZdpI2FTYbqUpla11qwg71BnVXaEQQnaqbrgINddMKLK3F9AgoEW1bK1Gs2Zsl18fRmWjdSPbO-mEgOxpZQKGUqBP1dqFOwd9PFEdzdNFS3-NAfooGdFWoqlZprJlcUBt8jIE6cwruiOFsQJi5HnMwcz1mrscAmFRPMr1-zJ-aI7X_LH_7SMD7BaD0i1-OwnwqDZZaF-ZLW-_-l_8AwKShXA</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1963468496</pqid></control><display><type>article</type><title>Ubiquitin C-terminal hydrolase-L1 plays a key role in angiogenesis by regulating hydrogen peroxide generated by NADPH oxidase 4</title><source>MEDLINE</source><source>Elsevier ScienceDirect Journals</source><creator>Song, In-Kang ; Kim, Hyun Jung ; Magesh, Venkataraman ; Lee, Kong-Joo</creator><creatorcontrib>Song, In-Kang ; Kim, Hyun Jung ; Magesh, Venkataraman ; Lee, Kong-Joo</creatorcontrib><description>Ubiquitin C-terminal hydrolase-L1 (UCH-L1), which catalyzes the hydrolysis of ubiquitin esters and amides, is highly expressed in brain. Recently, UCH-L1 has been found to increase cancer cell migration and invasion by modulating hydrogen peroxide generated by NADPH oxidase 4 (NOX4). Because angiogenesis is also mediated by hydrogen peroxide, we explored the role of UCH-L1 in angiogenesis in human umbilical vein endothelial cells (HUVECs). Silencing UCH-L1 suppressed tubule formation in HUVECs, indicating that UCH-L1 promotes angiogenesis in vitro. This was confirmed using in vivo Matrigel plug studies of HUVECs, after overexpressing or silencing UCH-L1. Silencing UCH-L1 significantly suppressed VEGF-induced ROS levels as well as activation of VEGFR, both of which are required for angiogenesis. This study also showed that UCH-L1 promotes angiogenesis of HUVECs, as well as invasion in cancer cells, by up-regulating ROS by deubiquitination of NOX4, suggesting that UCH-L1 plays a key role in angiogenesis of HUVECS by regulating ROS levels by deubiquitination of NOX4.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/j.bbrc.2017.11.051</identifier><identifier>PMID: 29128359</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>60 APPLIED LIFE SCIENCES ; ANGIOGENESIS ; BRAIN ; Cells, Cultured ; Deubiquitination ; Endothelial cells ; Endothelial Cells - cytology ; Endothelial Cells - physiology ; Gene Expression Regulation, Enzymologic - physiology ; HUMAN POPULATIONS ; Humans ; HYDROGEN PEROXIDE ; Hydrogen Peroxide - metabolism ; HYDROLASES ; HYDROLYSIS ; NADPH oxidase 4 ; NADPH Oxidase 4 - metabolism ; Neovascularization, Physiologic - physiology ; OXIDASES ; Reactive Oxygen Species - metabolism ; Receptors, Vascular Endothelial Growth Factor - metabolism ; TUBULES ; Ubiquitin Thiolesterase - metabolism ; Ubiquitination - physiology ; UCH-L1 ; Vascular Endothelial Growth Factor A - metabolism ; VEINS</subject><ispartof>Biochemical and biophysical research communications, 2018-01, Vol.495 (1), p.1567-1572</ispartof><rights>2017 Elsevier Inc.</rights><rights>Copyright © 2017 Elsevier Inc. All rights reserved.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c450t-25f2e76ab72454c8959eafa97a9f39aa10f48bf61918bd0a5cca09015aacd8403</citedby><cites>FETCH-LOGICAL-c450t-25f2e76ab72454c8959eafa97a9f39aa10f48bf61918bd0a5cca09015aacd8403</cites><orcidid>0000-0001-7972-6020</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X17322295$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29128359$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.osti.gov/biblio/23134408$$D View this record in Osti.gov$$Hfree_for_read</backlink></links><search><creatorcontrib>Song, In-Kang</creatorcontrib><creatorcontrib>Kim, Hyun Jung</creatorcontrib><creatorcontrib>Magesh, Venkataraman</creatorcontrib><creatorcontrib>Lee, Kong-Joo</creatorcontrib><title>Ubiquitin C-terminal hydrolase-L1 plays a key role in angiogenesis by regulating hydrogen peroxide generated by NADPH oxidase 4</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>Ubiquitin C-terminal hydrolase-L1 (UCH-L1), which catalyzes the hydrolysis of ubiquitin esters and amides, is highly expressed in brain. Recently, UCH-L1 has been found to increase cancer cell migration and invasion by modulating hydrogen peroxide generated by NADPH oxidase 4 (NOX4). Because angiogenesis is also mediated by hydrogen peroxide, we explored the role of UCH-L1 in angiogenesis in human umbilical vein endothelial cells (HUVECs). Silencing UCH-L1 suppressed tubule formation in HUVECs, indicating that UCH-L1 promotes angiogenesis in vitro. This was confirmed using in vivo Matrigel plug studies of HUVECs, after overexpressing or silencing UCH-L1. Silencing UCH-L1 significantly suppressed VEGF-induced ROS levels as well as activation of VEGFR, both of which are required for angiogenesis. This study also showed that UCH-L1 promotes angiogenesis of HUVECs, as well as invasion in cancer cells, by up-regulating ROS by deubiquitination of NOX4, suggesting that UCH-L1 plays a key role in angiogenesis of HUVECS by regulating ROS levels by deubiquitination of NOX4.</description><subject>60 APPLIED LIFE SCIENCES</subject><subject>ANGIOGENESIS</subject><subject>BRAIN</subject><subject>Cells, Cultured</subject><subject>Deubiquitination</subject><subject>Endothelial cells</subject><subject>Endothelial Cells - cytology</subject><subject>Endothelial Cells - physiology</subject><subject>Gene Expression Regulation, Enzymologic - physiology</subject><subject>HUMAN POPULATIONS</subject><subject>Humans</subject><subject>HYDROGEN PEROXIDE</subject><subject>Hydrogen Peroxide - metabolism</subject><subject>HYDROLASES</subject><subject>HYDROLYSIS</subject><subject>NADPH oxidase 4</subject><subject>NADPH Oxidase 4 - metabolism</subject><subject>Neovascularization, Physiologic - physiology</subject><subject>OXIDASES</subject><subject>Reactive Oxygen Species - metabolism</subject><subject>Receptors, Vascular Endothelial Growth Factor - metabolism</subject><subject>TUBULES</subject><subject>Ubiquitin Thiolesterase - metabolism</subject><subject>Ubiquitination - physiology</subject><subject>UCH-L1</subject><subject>Vascular Endothelial Growth Factor A - metabolism</subject><subject>VEINS</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kUFv1DAQhS0EotuFP8ABWeLCJcHjONlY4lJtgSKtgAOVuFkTZ7L1ko23doLYE3-9jlI4chrpzfeeRvMYewUiBwHVu0PeNMHmUsAmB8hFCU_YCoQWmQShnrKVEKLKpIYfF-wyxoMQAKrSz9lF0mRdlHrF_tw27n5yoxv4NhspHN2APb87t8H3GCnbAT_1eI4c-U8686QSTywOe-f3NFB0kTdJp_3UY0rZL9604icK_rdric9cwJHamfxydf3ths-LFM_VC_aswz7Sy8e5ZrcfP3zf3mS7r58-b692mVWlGDNZdpI2FTYbqUpla11qwg71BnVXaEQQnaqbrgINddMKLK3F9AgoEW1bK1Gs2Zsl18fRmWjdSPbO-mEgOxpZQKGUqBP1dqFOwd9PFEdzdNFS3-NAfooGdFWoqlZprJlcUBt8jIE6cwruiOFsQJi5HnMwcz1mrscAmFRPMr1-zJ-aI7X_LH_7SMD7BaD0i1-OwnwqDZZaF-ZLW-_-l_8AwKShXA</recordid><startdate>20180101</startdate><enddate>20180101</enddate><creator>Song, In-Kang</creator><creator>Kim, Hyun Jung</creator><creator>Magesh, Venkataraman</creator><creator>Lee, Kong-Joo</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>OTOTI</scope><orcidid>https://orcid.org/0000-0001-7972-6020</orcidid></search><sort><creationdate>20180101</creationdate><title>Ubiquitin C-terminal hydrolase-L1 plays a key role in angiogenesis by regulating hydrogen peroxide generated by NADPH oxidase 4</title><author>Song, In-Kang ; Kim, Hyun Jung ; Magesh, Venkataraman ; Lee, Kong-Joo</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c450t-25f2e76ab72454c8959eafa97a9f39aa10f48bf61918bd0a5cca09015aacd8403</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>60 APPLIED LIFE SCIENCES</topic><topic>ANGIOGENESIS</topic><topic>BRAIN</topic><topic>Cells, Cultured</topic><topic>Deubiquitination</topic><topic>Endothelial cells</topic><topic>Endothelial Cells - cytology</topic><topic>Endothelial Cells - physiology</topic><topic>Gene Expression Regulation, Enzymologic - physiology</topic><topic>HUMAN POPULATIONS</topic><topic>Humans</topic><topic>HYDROGEN PEROXIDE</topic><topic>Hydrogen Peroxide - metabolism</topic><topic>HYDROLASES</topic><topic>HYDROLYSIS</topic><topic>NADPH oxidase 4</topic><topic>NADPH Oxidase 4 - metabolism</topic><topic>Neovascularization, Physiologic - physiology</topic><topic>OXIDASES</topic><topic>Reactive Oxygen Species - metabolism</topic><topic>Receptors, Vascular Endothelial Growth Factor - metabolism</topic><topic>TUBULES</topic><topic>Ubiquitin Thiolesterase - metabolism</topic><topic>Ubiquitination - physiology</topic><topic>UCH-L1</topic><topic>Vascular Endothelial Growth Factor A - metabolism</topic><topic>VEINS</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Song, In-Kang</creatorcontrib><creatorcontrib>Kim, Hyun Jung</creatorcontrib><creatorcontrib>Magesh, Venkataraman</creatorcontrib><creatorcontrib>Lee, Kong-Joo</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>OSTI.GOV</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Song, In-Kang</au><au>Kim, Hyun Jung</au><au>Magesh, Venkataraman</au><au>Lee, Kong-Joo</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ubiquitin C-terminal hydrolase-L1 plays a key role in angiogenesis by regulating hydrogen peroxide generated by NADPH oxidase 4</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2018-01-01</date><risdate>2018</risdate><volume>495</volume><issue>1</issue><spage>1567</spage><epage>1572</epage><pages>1567-1572</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>Ubiquitin C-terminal hydrolase-L1 (UCH-L1), which catalyzes the hydrolysis of ubiquitin esters and amides, is highly expressed in brain. Recently, UCH-L1 has been found to increase cancer cell migration and invasion by modulating hydrogen peroxide generated by NADPH oxidase 4 (NOX4). Because angiogenesis is also mediated by hydrogen peroxide, we explored the role of UCH-L1 in angiogenesis in human umbilical vein endothelial cells (HUVECs). Silencing UCH-L1 suppressed tubule formation in HUVECs, indicating that UCH-L1 promotes angiogenesis in vitro. This was confirmed using in vivo Matrigel plug studies of HUVECs, after overexpressing or silencing UCH-L1. Silencing UCH-L1 significantly suppressed VEGF-induced ROS levels as well as activation of VEGFR, both of which are required for angiogenesis. This study also showed that UCH-L1 promotes angiogenesis of HUVECs, as well as invasion in cancer cells, by up-regulating ROS by deubiquitination of NOX4, suggesting that UCH-L1 plays a key role in angiogenesis of HUVECS by regulating ROS levels by deubiquitination of NOX4.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>29128359</pmid><doi>10.1016/j.bbrc.2017.11.051</doi><tpages>6</tpages><orcidid>https://orcid.org/0000-0001-7972-6020</orcidid></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 2018-01, Vol.495 (1), p.1567-1572 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_osti_scitechconnect_23134408 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | 60 APPLIED LIFE SCIENCES ANGIOGENESIS BRAIN Cells, Cultured Deubiquitination Endothelial cells Endothelial Cells - cytology Endothelial Cells - physiology Gene Expression Regulation, Enzymologic - physiology HUMAN POPULATIONS Humans HYDROGEN PEROXIDE Hydrogen Peroxide - metabolism HYDROLASES HYDROLYSIS NADPH oxidase 4 NADPH Oxidase 4 - metabolism Neovascularization, Physiologic - physiology OXIDASES Reactive Oxygen Species - metabolism Receptors, Vascular Endothelial Growth Factor - metabolism TUBULES Ubiquitin Thiolesterase - metabolism Ubiquitination - physiology UCH-L1 Vascular Endothelial Growth Factor A - metabolism VEINS |
| title | Ubiquitin C-terminal hydrolase-L1 plays a key role in angiogenesis by regulating hydrogen peroxide generated by NADPH oxidase 4 |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-02-05T09%3A12%3A55IST&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=Ubiquitin%20C-terminal%20hydrolase-L1%20plays%20a%20key%20role%20in%20angiogenesis%20by%20regulating%20hydrogen%20peroxide%20generated%20by%20NADPH%20oxidase%204&rft.jtitle=Biochemical%20and%20biophysical%20research%20communications&rft.au=Song,%20In-Kang&rft.date=2018-01-01&rft.volume=495&rft.issue=1&rft.spage=1567&rft.epage=1572&rft.pages=1567-1572&rft.issn=0006-291X&rft.eissn=1090-2104&rft_id=info:doi/10.1016/j.bbrc.2017.11.051&rft_dat=%3Cproquest_osti_%3E1963468496%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=1963468496&rft_id=info:pmid/29128359&rft_els_id=S0006291X17322295&rfr_iscdi=true |