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Reduction of Membrane Protein CRIM1 Decreases E-Cadherin and Increases Claudin-1 and MMPs, Enhancing the Migration and Invasion of Renal Carcinoma Cells
CRIM1 is a membrane protein that has been reported to be related to cell proliferation. CRIM1 is expressed in renal carcinoma cells, but its involvement in proliferation and malignant transformation remains unclear. We analyzed whether alterations in the characteristics of cancer cells are observed...
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Published in: | Biological & pharmaceutical bulletin 2018/04/01, Vol.41(4), pp.604-611 |
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description | CRIM1 is a membrane protein that has been reported to be related to cell proliferation. CRIM1 is expressed in renal carcinoma cells, but its involvement in proliferation and malignant transformation remains unclear. We analyzed whether alterations in the characteristics of cancer cells are observed following knockdown of CRIM1. Decreased expression of CRIM1 did not affect proliferation or anchorage-independent growth. The results of wound healing and invasion assays showed that reduced expression of CRIM1 increased cells’ migratory and invasive abilities. Expression analysis of factors involved in migration and invasion in CRIM1-knockdown cells revealed that expression of the cell adhesion factor E-cadherin declined and expression of claudin-1, which is upregulated in metastatic cancer cells, increased. In addition, increased expression of matrix metalloproteinase (MMP) 2 and MMP9, protease essential for cancer cell invasiveness, was observed. Furthermore, an increase in phosphorylated focal adhesion kinase (FAK), which increases cell migration, was observed. Increased expression of the E-cadherin transcription repressors Snail, Slug, and ZEB-1 were observed, and mRNA levels of E-cadherin were decreased. Therefore, expression of E-cadherin is thought to be decreased by both suppression of E-cadherin mRNA expression and promotion of degradation of the E-cadherin protein. In addition, expression of CRIM1 was decreased in renal cancer cells undergoing epithelial–mesenchymal transition (EMT) stimulated by tumor necrosis factor alpha (TNF-α). Thus, CRIM1 regulates the expression of several EMT-related factors and appears to play a role in suppressing migration and invasion through control of EMT. |
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CRIM1 is expressed in renal carcinoma cells, but its involvement in proliferation and malignant transformation remains unclear. We analyzed whether alterations in the characteristics of cancer cells are observed following knockdown of CRIM1. Decreased expression of CRIM1 did not affect proliferation or anchorage-independent growth. The results of wound healing and invasion assays showed that reduced expression of CRIM1 increased cells’ migratory and invasive abilities. Expression analysis of factors involved in migration and invasion in CRIM1-knockdown cells revealed that expression of the cell adhesion factor E-cadherin declined and expression of claudin-1, which is upregulated in metastatic cancer cells, increased. In addition, increased expression of matrix metalloproteinase (MMP) 2 and MMP9, protease essential for cancer cell invasiveness, was observed. Furthermore, an increase in phosphorylated focal adhesion kinase (FAK), which increases cell migration, was observed. Increased expression of the E-cadherin transcription repressors Snail, Slug, and ZEB-1 were observed, and mRNA levels of E-cadherin were decreased. Therefore, expression of E-cadherin is thought to be decreased by both suppression of E-cadherin mRNA expression and promotion of degradation of the E-cadherin protein. In addition, expression of CRIM1 was decreased in renal cancer cells undergoing epithelial–mesenchymal transition (EMT) stimulated by tumor necrosis factor alpha (TNF-α). Thus, CRIM1 regulates the expression of several EMT-related factors and appears to play a role in suppressing migration and invasion through control of EMT.</description><identifier>ISSN: 0918-6158</identifier><identifier>EISSN: 1347-5215</identifier><identifier>DOI: 10.1248/bpb.b17-00990</identifier><identifier>PMID: 29607933</identifier><language>eng</language><publisher>Japan: The Pharmaceutical Society of Japan</publisher><subject>Adhesion ; Cancer ; Cell adhesion ; Cell adhesion & migration ; Cell migration ; Cell proliferation ; claudin-1 ; CRIM1 ; E-cadherin ; epithelial–mesenchymal transition ; Focal adhesion kinase ; Gelatinase B ; Gene expression ; Invasiveness ; Kidney cancer ; Kinases ; Matrix metalloproteinase ; Membrane proteins ; Mesenchyme ; Metalloproteinase ; Metastases ; Proteins ; Renal cell carcinoma ; Repressors ; Snail protein ; Transcription factors ; tumor necrosis factor alpha ; Tumor necrosis factor-TNF ; Tumor necrosis factor-α ; Wound healing</subject><ispartof>Biological and Pharmaceutical Bulletin, 2018/04/01, Vol.41(4), pp.604-611</ispartof><rights>2018 The Pharmaceutical Society of Japan</rights><rights>Copyright Japan Science and Technology Agency 2018</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c702t-eb4ffd688631edbdbf3cb897c2b03b9a3d1d8f8f333ad6cf188e8ec15db8f3953</citedby><cites>FETCH-LOGICAL-c702t-eb4ffd688631edbdbf3cb897c2b03b9a3d1d8f8f333ad6cf188e8ec15db8f3953</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,4024,27923,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29607933$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Ogasawara, Nobutaka</creatorcontrib><creatorcontrib>Kudo, Tamami</creatorcontrib><creatorcontrib>Sato, Masaki</creatorcontrib><creatorcontrib>Kawasaki, Yasushi</creatorcontrib><creatorcontrib>Yonezawa, Sei</creatorcontrib><creatorcontrib>Takahashi, Satoru</creatorcontrib><creatorcontrib>Miyagi, Yohei</creatorcontrib><creatorcontrib>Natori, Yasuhiro</creatorcontrib><creatorcontrib>Sugiyama, Akinori</creatorcontrib><creatorcontrib>bDepartment of Immunobiology</creatorcontrib><creatorcontrib>and (cDivision of Molecular Pathology and Genetics</creatorcontrib><creatorcontrib>School of Pharmacy</creatorcontrib><creatorcontrib>Kanagawa Cancer Center Research Institute</creatorcontrib><creatorcontrib>Mukogawa Women's University</creatorcontrib><creatorcontrib>Iwate Medical University</creatorcontrib><creatorcontrib>School of Pharmacy and Pharmaceutical Science</creatorcontrib><creatorcontrib>aDepartment of Health Chemistry</creatorcontrib><title>Reduction of Membrane Protein CRIM1 Decreases E-Cadherin and Increases Claudin-1 and MMPs, Enhancing the Migration and Invasion of Renal Carcinoma Cells</title><title>Biological & pharmaceutical bulletin</title><addtitle>Biol Pharm Bull</addtitle><description>CRIM1 is a membrane protein that has been reported to be related to cell proliferation. CRIM1 is expressed in renal carcinoma cells, but its involvement in proliferation and malignant transformation remains unclear. We analyzed whether alterations in the characteristics of cancer cells are observed following knockdown of CRIM1. Decreased expression of CRIM1 did not affect proliferation or anchorage-independent growth. The results of wound healing and invasion assays showed that reduced expression of CRIM1 increased cells’ migratory and invasive abilities. Expression analysis of factors involved in migration and invasion in CRIM1-knockdown cells revealed that expression of the cell adhesion factor E-cadherin declined and expression of claudin-1, which is upregulated in metastatic cancer cells, increased. In addition, increased expression of matrix metalloproteinase (MMP) 2 and MMP9, protease essential for cancer cell invasiveness, was observed. Furthermore, an increase in phosphorylated focal adhesion kinase (FAK), which increases cell migration, was observed. Increased expression of the E-cadherin transcription repressors Snail, Slug, and ZEB-1 were observed, and mRNA levels of E-cadherin were decreased. Therefore, expression of E-cadherin is thought to be decreased by both suppression of E-cadherin mRNA expression and promotion of degradation of the E-cadherin protein. In addition, expression of CRIM1 was decreased in renal cancer cells undergoing epithelial–mesenchymal transition (EMT) stimulated by tumor necrosis factor alpha (TNF-α). Thus, CRIM1 regulates the expression of several EMT-related factors and appears to play a role in suppressing migration and invasion through control of EMT.</description><subject>Adhesion</subject><subject>Cancer</subject><subject>Cell adhesion</subject><subject>Cell adhesion & migration</subject><subject>Cell migration</subject><subject>Cell proliferation</subject><subject>claudin-1</subject><subject>CRIM1</subject><subject>E-cadherin</subject><subject>epithelial–mesenchymal transition</subject><subject>Focal adhesion kinase</subject><subject>Gelatinase B</subject><subject>Gene expression</subject><subject>Invasiveness</subject><subject>Kidney cancer</subject><subject>Kinases</subject><subject>Matrix metalloproteinase</subject><subject>Membrane proteins</subject><subject>Mesenchyme</subject><subject>Metalloproteinase</subject><subject>Metastases</subject><subject>Proteins</subject><subject>Renal cell carcinoma</subject><subject>Repressors</subject><subject>Snail protein</subject><subject>Transcription factors</subject><subject>tumor necrosis factor alpha</subject><subject>Tumor necrosis factor-TNF</subject><subject>Tumor necrosis factor-α</subject><subject>Wound healing</subject><issn>0918-6158</issn><issn>1347-5215</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNpdkUtvEzEUhUcIRENhyRZZYsOCKb7jedhLNKQlUiOqCNaWH3eSiSZ2sGcq8U_4uXUeDRIb27r387nHPln2HugNFCX_ovf6RkOTUyoEfZHNgJVNXhVQvcxmVADPa6j4VfYmxi2ltKEFe51dFaKmjWBslv1doZ3M2HtHfEeWuNNBOSQPwY_YO9KuFksg39AEVBEjmeetshsMqaWcJQv33GgHNdne5XCsL5cP8TOZu41ypndrMm6QLPt1UMdBp5uPKp6nrtCpgbQqJNbvFGlxGOLb7FWnhojvzvt19ut2_rP9nt__uFu0X-9zk94y5qjLrrM15zUDtNrqjhnNRWMKTZkWilmwvOMdY0zZ2nTAOXI0UFmdiqJi19mnk-4--N8TxlHu-miSg_QNfoqyoAXlnFWCJ_Tjf-jWTyF5P1IFAIjiQOUnygQfY8BO7kO_U-GPBCoPkckUmUyRyWNkif9wVp30Du2Ffs4oAXcnIHV7owbvht7hv9kmNrr3g08mgCfREmgpk2tJ68OhBmC0SmIiKbUnpW0c1Rovo1QYezPg0VgJsjwsF4OXrtmoINGxJ3lVwFw</recordid><startdate>2018</startdate><enddate>2018</enddate><creator>Ogasawara, Nobutaka</creator><creator>Kudo, Tamami</creator><creator>Sato, Masaki</creator><creator>Kawasaki, Yasushi</creator><creator>Yonezawa, Sei</creator><creator>Takahashi, Satoru</creator><creator>Miyagi, Yohei</creator><creator>Natori, Yasuhiro</creator><creator>Sugiyama, Akinori</creator><general>The Pharmaceutical Society of Japan</general><general>Pharmaceutical Society of Japan</general><general>Japan Science and Technology Agency</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>FR3</scope><scope>H94</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>2018</creationdate><title>Reduction of Membrane Protein CRIM1 Decreases E-Cadherin and Increases Claudin-1 and MMPs, Enhancing the Migration and Invasion of Renal Carcinoma Cells</title><author>Ogasawara, Nobutaka ; Kudo, Tamami ; Sato, Masaki ; Kawasaki, Yasushi ; Yonezawa, Sei ; Takahashi, Satoru ; Miyagi, Yohei ; Natori, Yasuhiro ; Sugiyama, Akinori</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c702t-eb4ffd688631edbdbf3cb897c2b03b9a3d1d8f8f333ad6cf188e8ec15db8f3953</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Adhesion</topic><topic>Cancer</topic><topic>Cell adhesion</topic><topic>Cell adhesion & migration</topic><topic>Cell migration</topic><topic>Cell proliferation</topic><topic>claudin-1</topic><topic>CRIM1</topic><topic>E-cadherin</topic><topic>epithelial–mesenchymal transition</topic><topic>Focal adhesion kinase</topic><topic>Gelatinase B</topic><topic>Gene expression</topic><topic>Invasiveness</topic><topic>Kidney cancer</topic><topic>Kinases</topic><topic>Matrix metalloproteinase</topic><topic>Membrane proteins</topic><topic>Mesenchyme</topic><topic>Metalloproteinase</topic><topic>Metastases</topic><topic>Proteins</topic><topic>Renal cell carcinoma</topic><topic>Repressors</topic><topic>Snail protein</topic><topic>Transcription factors</topic><topic>tumor necrosis factor alpha</topic><topic>Tumor necrosis factor-TNF</topic><topic>Tumor necrosis factor-α</topic><topic>Wound healing</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ogasawara, Nobutaka</creatorcontrib><creatorcontrib>Kudo, Tamami</creatorcontrib><creatorcontrib>Sato, Masaki</creatorcontrib><creatorcontrib>Kawasaki, Yasushi</creatorcontrib><creatorcontrib>Yonezawa, Sei</creatorcontrib><creatorcontrib>Takahashi, Satoru</creatorcontrib><creatorcontrib>Miyagi, Yohei</creatorcontrib><creatorcontrib>Natori, Yasuhiro</creatorcontrib><creatorcontrib>Sugiyama, Akinori</creatorcontrib><creatorcontrib>bDepartment of Immunobiology</creatorcontrib><creatorcontrib>and (cDivision of Molecular Pathology and Genetics</creatorcontrib><creatorcontrib>School of Pharmacy</creatorcontrib><creatorcontrib>Kanagawa Cancer Center Research Institute</creatorcontrib><creatorcontrib>Mukogawa Women's University</creatorcontrib><creatorcontrib>Iwate Medical University</creatorcontrib><creatorcontrib>School of Pharmacy and Pharmaceutical Science</creatorcontrib><creatorcontrib>aDepartment of Health Chemistry</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biological & pharmaceutical bulletin</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ogasawara, Nobutaka</au><au>Kudo, Tamami</au><au>Sato, Masaki</au><au>Kawasaki, Yasushi</au><au>Yonezawa, Sei</au><au>Takahashi, Satoru</au><au>Miyagi, Yohei</au><au>Natori, Yasuhiro</au><au>Sugiyama, Akinori</au><aucorp>bDepartment of Immunobiology</aucorp><aucorp>and (cDivision of Molecular Pathology and Genetics</aucorp><aucorp>School of Pharmacy</aucorp><aucorp>Kanagawa Cancer Center Research Institute</aucorp><aucorp>Mukogawa Women's University</aucorp><aucorp>Iwate Medical University</aucorp><aucorp>School of Pharmacy and Pharmaceutical Science</aucorp><aucorp>aDepartment of Health Chemistry</aucorp><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Reduction of Membrane Protein CRIM1 Decreases E-Cadherin and Increases Claudin-1 and MMPs, Enhancing the Migration and Invasion of Renal Carcinoma Cells</atitle><jtitle>Biological & pharmaceutical bulletin</jtitle><addtitle>Biol Pharm Bull</addtitle><date>2018</date><risdate>2018</risdate><volume>41</volume><issue>4</issue><spage>604</spage><epage>611</epage><pages>604-611</pages><issn>0918-6158</issn><eissn>1347-5215</eissn><abstract>CRIM1 is a membrane protein that has been reported to be related to cell proliferation. CRIM1 is expressed in renal carcinoma cells, but its involvement in proliferation and malignant transformation remains unclear. We analyzed whether alterations in the characteristics of cancer cells are observed following knockdown of CRIM1. Decreased expression of CRIM1 did not affect proliferation or anchorage-independent growth. The results of wound healing and invasion assays showed that reduced expression of CRIM1 increased cells’ migratory and invasive abilities. Expression analysis of factors involved in migration and invasion in CRIM1-knockdown cells revealed that expression of the cell adhesion factor E-cadherin declined and expression of claudin-1, which is upregulated in metastatic cancer cells, increased. In addition, increased expression of matrix metalloproteinase (MMP) 2 and MMP9, protease essential for cancer cell invasiveness, was observed. Furthermore, an increase in phosphorylated focal adhesion kinase (FAK), which increases cell migration, was observed. Increased expression of the E-cadherin transcription repressors Snail, Slug, and ZEB-1 were observed, and mRNA levels of E-cadherin were decreased. Therefore, expression of E-cadherin is thought to be decreased by both suppression of E-cadherin mRNA expression and promotion of degradation of the E-cadherin protein. In addition, expression of CRIM1 was decreased in renal cancer cells undergoing epithelial–mesenchymal transition (EMT) stimulated by tumor necrosis factor alpha (TNF-α). Thus, CRIM1 regulates the expression of several EMT-related factors and appears to play a role in suppressing migration and invasion through control of EMT.</abstract><cop>Japan</cop><pub>The Pharmaceutical Society of Japan</pub><pmid>29607933</pmid><doi>10.1248/bpb.b17-00990</doi><tpages>8</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Adhesion Cancer Cell adhesion Cell adhesion & migration Cell migration Cell proliferation claudin-1 CRIM1 E-cadherin epithelial–mesenchymal transition Focal adhesion kinase Gelatinase B Gene expression Invasiveness Kidney cancer Kinases Matrix metalloproteinase Membrane proteins Mesenchyme Metalloproteinase Metastases Proteins Renal cell carcinoma Repressors Snail protein Transcription factors tumor necrosis factor alpha Tumor necrosis factor-TNF Tumor necrosis factor-α Wound healing |
title | Reduction of Membrane Protein CRIM1 Decreases E-Cadherin and Increases Claudin-1 and MMPs, Enhancing the Migration and Invasion of Renal Carcinoma Cells |
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