USP10 exacerbates neointima formation by stabilizing Skp2 protein in vascular smooth muscle cells
The underlying mechanism of neointima formation remains unclear. Ubiquitin-specific peptidase 10 (USP10) is a deubiquitinase that plays a major role in cancer development and progression. However, the function of USP10 in arterial restenosis is unknown. Herein, USP10 expression was detected in mouse...
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| Veröffentlicht in: | The Journal of biological chemistry 2021-11, Vol.297 (5), p.101258-101258, Article 101258 |
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| creator | Xia, Xiaohong Liu, Xiaolin Chai, Renjie Xu, Qiong Luo, Zhenyu Gu, Jielei Jin, Yangshuo Hu, Tumei Yu, Cuifu Du, Bijun Huang, Hongbiao Ou, Wenchao Liu, Shiming Liu, Ningning |
| description | The underlying mechanism of neointima formation remains unclear. Ubiquitin-specific peptidase 10 (USP10) is a deubiquitinase that plays a major role in cancer development and progression. However, the function of USP10 in arterial restenosis is unknown. Herein, USP10 expression was detected in mouse arteries and increased after carotid ligation. The inhibition of USP10 exhibited thinner neointima in the model of mouse carotid ligation. In vitro data showed that USP10 deficiency reduced proliferation and migration of rat thoracic aorta smooth muscle cells (A7r5) and human aortic smooth muscle cells (HASMCs). Mechanically, USP10 can bind to Skp2 and stabilize its protein level by removing polyubiquitin on Skp2 in the cytoplasm. The overexpression of Skp2 abrogated cell cycle arrest induced by USP10 inhibition. Overall, the current study demonstrated that USP10 is involved in vascular remodeling by directly promoting VSMC proliferation and migration via stabilization of Skp2 protein expression. |
| doi_str_mv | 10.1016/j.jbc.2021.101258 |
| format | Article |
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Ubiquitin-specific peptidase 10 (USP10) is a deubiquitinase that plays a major role in cancer development and progression. However, the function of USP10 in arterial restenosis is unknown. Herein, USP10 expression was detected in mouse arteries and increased after carotid ligation. The inhibition of USP10 exhibited thinner neointima in the model of mouse carotid ligation. In vitro data showed that USP10 deficiency reduced proliferation and migration of rat thoracic aorta smooth muscle cells (A7r5) and human aortic smooth muscle cells (HASMCs). Mechanically, USP10 can bind to Skp2 and stabilize its protein level by removing polyubiquitin on Skp2 in the cytoplasm. The overexpression of Skp2 abrogated cell cycle arrest induced by USP10 inhibition. Overall, the current study demonstrated that USP10 is involved in vascular remodeling by directly promoting VSMC proliferation and migration via stabilization of Skp2 protein expression.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/j.jbc.2021.101258</identifier><identifier>PMID: 34599966</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>carotid ligation ; Cell Line ; Cell Movement ; Cell Proliferation ; Humans ; Muscle, Smooth, Vascular - metabolism ; Myocytes, Smooth Muscle - metabolism ; Neointima - genetics ; Neointima - metabolism ; proliferation ; Protein Stability ; S-Phase Kinase-Associated Proteins - genetics ; S-Phase Kinase-Associated Proteins - metabolism ; Skp2 ; Ubiquitin Thiolesterase - genetics ; Ubiquitin Thiolesterase - metabolism ; ubiquitin-specific peptidase 10 (USP10) ; vascular smooth muscle cell (VSMC)</subject><ispartof>The Journal of biological chemistry, 2021-11, Vol.297 (5), p.101258-101258, Article 101258</ispartof><rights>2021 The Authors</rights><rights>Copyright © 2021 The Authors. Published by Elsevier Inc. All rights reserved.</rights><rights>2021 The Authors 2021</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c451t-f321352d5cde25413a305943fd341c64a1f4f8b908f51947ea232ce4df0f99123</citedby><cites>FETCH-LOGICAL-c451t-f321352d5cde25413a305943fd341c64a1f4f8b908f51947ea232ce4df0f99123</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8524199/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC8524199/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,727,780,784,864,885,27923,27924,53790,53792</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/34599966$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Xia, Xiaohong</creatorcontrib><creatorcontrib>Liu, Xiaolin</creatorcontrib><creatorcontrib>Chai, Renjie</creatorcontrib><creatorcontrib>Xu, Qiong</creatorcontrib><creatorcontrib>Luo, Zhenyu</creatorcontrib><creatorcontrib>Gu, Jielei</creatorcontrib><creatorcontrib>Jin, Yangshuo</creatorcontrib><creatorcontrib>Hu, Tumei</creatorcontrib><creatorcontrib>Yu, Cuifu</creatorcontrib><creatorcontrib>Du, Bijun</creatorcontrib><creatorcontrib>Huang, Hongbiao</creatorcontrib><creatorcontrib>Ou, Wenchao</creatorcontrib><creatorcontrib>Liu, Shiming</creatorcontrib><creatorcontrib>Liu, Ningning</creatorcontrib><title>USP10 exacerbates neointima formation by stabilizing Skp2 protein in vascular smooth muscle cells</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>The underlying mechanism of neointima formation remains unclear. Ubiquitin-specific peptidase 10 (USP10) is a deubiquitinase that plays a major role in cancer development and progression. However, the function of USP10 in arterial restenosis is unknown. Herein, USP10 expression was detected in mouse arteries and increased after carotid ligation. The inhibition of USP10 exhibited thinner neointima in the model of mouse carotid ligation. In vitro data showed that USP10 deficiency reduced proliferation and migration of rat thoracic aorta smooth muscle cells (A7r5) and human aortic smooth muscle cells (HASMCs). Mechanically, USP10 can bind to Skp2 and stabilize its protein level by removing polyubiquitin on Skp2 in the cytoplasm. The overexpression of Skp2 abrogated cell cycle arrest induced by USP10 inhibition. Overall, the current study demonstrated that USP10 is involved in vascular remodeling by directly promoting VSMC proliferation and migration via stabilization of Skp2 protein expression.</description><subject>carotid ligation</subject><subject>Cell Line</subject><subject>Cell Movement</subject><subject>Cell Proliferation</subject><subject>Humans</subject><subject>Muscle, Smooth, Vascular - metabolism</subject><subject>Myocytes, Smooth Muscle - metabolism</subject><subject>Neointima - genetics</subject><subject>Neointima - metabolism</subject><subject>proliferation</subject><subject>Protein Stability</subject><subject>S-Phase Kinase-Associated Proteins - genetics</subject><subject>S-Phase Kinase-Associated Proteins - metabolism</subject><subject>Skp2</subject><subject>Ubiquitin Thiolesterase - genetics</subject><subject>Ubiquitin Thiolesterase - metabolism</subject><subject>ubiquitin-specific peptidase 10 (USP10)</subject><subject>vascular smooth muscle cell (VSMC)</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2021</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kd9rFDEQx4Mo9lr9A3yRPPqyZyY_9jYIghS1QkGhFnwL2eykzbm7OZPsYf3rzXG16IshEJL5zjcz8yHkBbA1MGhfb9fb3q0543C4c9U9IitgnWiEgm-PyYrVSKPr-wk5zXnL6pIanpITIZXWum1XxF5ffQFG8ad1mHpbMNMZY5hLmCz1MU22hDjT_o7mYvswhl9hvqFX33ec7lIsGGZa995mt4w20TzFWG7ptGQ3InU4jvkZeeLtmPH5_XlGrj-8_3p-0Vx-_vjp_N1l46SC0njBQSg-KDcgVxKEFUxpKfwgJLhWWvDSd71mnVeg5QYtF9yhHDzzWgMXZ-Tt0Xe39BMODueS7Gh2qXaS7ky0wfwbmcOtuYl70ykuQetq8OreIMUfC-ZippAPLdg6kSUbrjbdpq0FbKoUjlKXYs4J_cM3wMwBjdmaisYc0Jgjmprz8u_6HjL-sKiCN0cB1intAyaTXcDZ4RASumKGGP5j_xuo0KA9</recordid><startdate>20211101</startdate><enddate>20211101</enddate><creator>Xia, Xiaohong</creator><creator>Liu, Xiaolin</creator><creator>Chai, Renjie</creator><creator>Xu, Qiong</creator><creator>Luo, Zhenyu</creator><creator>Gu, Jielei</creator><creator>Jin, Yangshuo</creator><creator>Hu, Tumei</creator><creator>Yu, Cuifu</creator><creator>Du, Bijun</creator><creator>Huang, Hongbiao</creator><creator>Ou, Wenchao</creator><creator>Liu, Shiming</creator><creator>Liu, Ningning</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><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>5PM</scope></search><sort><creationdate>20211101</creationdate><title>USP10 exacerbates neointima formation by stabilizing Skp2 protein in vascular smooth muscle cells</title><author>Xia, Xiaohong ; Liu, Xiaolin ; Chai, Renjie ; Xu, Qiong ; Luo, Zhenyu ; Gu, Jielei ; Jin, Yangshuo ; Hu, Tumei ; Yu, Cuifu ; Du, Bijun ; Huang, Hongbiao ; Ou, Wenchao ; Liu, Shiming ; Liu, Ningning</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c451t-f321352d5cde25413a305943fd341c64a1f4f8b908f51947ea232ce4df0f99123</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2021</creationdate><topic>carotid ligation</topic><topic>Cell Line</topic><topic>Cell Movement</topic><topic>Cell Proliferation</topic><topic>Humans</topic><topic>Muscle, Smooth, Vascular - metabolism</topic><topic>Myocytes, Smooth Muscle - metabolism</topic><topic>Neointima - genetics</topic><topic>Neointima - metabolism</topic><topic>proliferation</topic><topic>Protein Stability</topic><topic>S-Phase Kinase-Associated Proteins - genetics</topic><topic>S-Phase Kinase-Associated Proteins - metabolism</topic><topic>Skp2</topic><topic>Ubiquitin Thiolesterase - genetics</topic><topic>Ubiquitin Thiolesterase - metabolism</topic><topic>ubiquitin-specific peptidase 10 (USP10)</topic><topic>vascular smooth muscle cell (VSMC)</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Xia, Xiaohong</creatorcontrib><creatorcontrib>Liu, Xiaolin</creatorcontrib><creatorcontrib>Chai, Renjie</creatorcontrib><creatorcontrib>Xu, Qiong</creatorcontrib><creatorcontrib>Luo, Zhenyu</creatorcontrib><creatorcontrib>Gu, Jielei</creatorcontrib><creatorcontrib>Jin, Yangshuo</creatorcontrib><creatorcontrib>Hu, Tumei</creatorcontrib><creatorcontrib>Yu, Cuifu</creatorcontrib><creatorcontrib>Du, Bijun</creatorcontrib><creatorcontrib>Huang, Hongbiao</creatorcontrib><creatorcontrib>Ou, Wenchao</creatorcontrib><creatorcontrib>Liu, Shiming</creatorcontrib><creatorcontrib>Liu, Ningning</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Xia, Xiaohong</au><au>Liu, Xiaolin</au><au>Chai, Renjie</au><au>Xu, Qiong</au><au>Luo, Zhenyu</au><au>Gu, Jielei</au><au>Jin, Yangshuo</au><au>Hu, Tumei</au><au>Yu, Cuifu</au><au>Du, Bijun</au><au>Huang, Hongbiao</au><au>Ou, Wenchao</au><au>Liu, Shiming</au><au>Liu, Ningning</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>USP10 exacerbates neointima formation by stabilizing Skp2 protein in vascular smooth muscle cells</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2021-11-01</date><risdate>2021</risdate><volume>297</volume><issue>5</issue><spage>101258</spage><epage>101258</epage><pages>101258-101258</pages><artnum>101258</artnum><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>The underlying mechanism of neointima formation remains unclear. Ubiquitin-specific peptidase 10 (USP10) is a deubiquitinase that plays a major role in cancer development and progression. However, the function of USP10 in arterial restenosis is unknown. Herein, USP10 expression was detected in mouse arteries and increased after carotid ligation. The inhibition of USP10 exhibited thinner neointima in the model of mouse carotid ligation. In vitro data showed that USP10 deficiency reduced proliferation and migration of rat thoracic aorta smooth muscle cells (A7r5) and human aortic smooth muscle cells (HASMCs). Mechanically, USP10 can bind to Skp2 and stabilize its protein level by removing polyubiquitin on Skp2 in the cytoplasm. The overexpression of Skp2 abrogated cell cycle arrest induced by USP10 inhibition. Overall, the current study demonstrated that USP10 is involved in vascular remodeling by directly promoting VSMC proliferation and migration via stabilization of Skp2 protein expression.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>34599966</pmid><doi>10.1016/j.jbc.2021.101258</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | carotid ligation Cell Line Cell Movement Cell Proliferation Humans Muscle, Smooth, Vascular - metabolism Myocytes, Smooth Muscle - metabolism Neointima - genetics Neointima - metabolism proliferation Protein Stability S-Phase Kinase-Associated Proteins - genetics S-Phase Kinase-Associated Proteins - metabolism Skp2 Ubiquitin Thiolesterase - genetics Ubiquitin Thiolesterase - metabolism ubiquitin-specific peptidase 10 (USP10) vascular smooth muscle cell (VSMC) |
| title | USP10 exacerbates neointima formation by stabilizing Skp2 protein in vascular smooth muscle cells |
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