The intranuclear PEX domain of MMP involves proliferation, migration, and metastasis of aggressive adenocarcinoma cells
Members of matrix metalloproteinase (MMP) family promote cancer cell migration, invasion, and metastasis through alteration of the tumor milieu, intracellular signaling pathways, and transcription. We examined gene expression signatures of colon adenocarcinoma cell lines with different metastatic po...
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| Veröffentlicht in: | Journal of cellular biochemistry 2018-09, Vol.119 (9), p.7363-7376 |
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| container_title | Journal of cellular biochemistry |
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| creator | Okusha, Yuka Eguchi, Takanori Sogawa, Chiharu Okui, Tatsuo Nakano, Keisuke Okamoto, Kuniaki Kozaki, Ken‐Ichi |
| description | Members of matrix metalloproteinase (MMP) family promote cancer cell migration, invasion, and metastasis through alteration of the tumor milieu, intracellular signaling pathways, and transcription. We examined gene expression signatures of colon adenocarcinoma cell lines with different metastatic potentials and found that rapidly metastatic cells powerfully expressed genes encoding MMP3 and MMP9. The non‐proteolytic PEX isoform and proteolytic isoforms of MMPs were significantly expressed in the metastatic cells in vitro. Knockdown of MMP3 attenuated cancer cell migration and invasion in vitro and lung metastasis in vivo. Profound nuclear localization of MMP3/PEX was found in tumor‐stroma marginal area. In contrast, MMP9 was localized in central area of subcutaneous tumors. Overexpression of the PEX isoform of MMP3 promoted proliferation and migration of the rapidly metastatic cells in vitro. Taken together, the non‐proteolytic PEX isoform of MMPs locating in cell nuclei involves proliferation, migration, and subsequent metastasis of aggressive adenocarcinoma cells.
Profound nuclear localization of MMP3/PEX was found in tumor‐stroma marginal area. Overexpression of the PEX isoform of MMP3 promoted proliferation and migration of the rapidly metastatic cells in vitro. The non‐proteolytic PEX isoform of MMPs locating in cell nuclei involves proliferation, migration, and subsequent metastasis of aggressive adenocarcinoma cells. |
| doi_str_mv | 10.1002/jcb.27040 |
| format | Article |
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Profound nuclear localization of MMP3/PEX was found in tumor‐stroma marginal area. Overexpression of the PEX isoform of MMP3 promoted proliferation and migration of the rapidly metastatic cells in vitro. The non‐proteolytic PEX isoform of MMPs locating in cell nuclei involves proliferation, migration, and subsequent metastasis of aggressive adenocarcinoma cells.</description><identifier>ISSN: 0730-2312</identifier><identifier>EISSN: 1097-4644</identifier><identifier>DOI: 10.1002/jcb.27040</identifier><identifier>PMID: 29761931</identifier><language>eng</language><publisher>United States: Wiley Subscription Services, Inc</publisher><subject>Adenocarcinoma ; Cancer ; cancer metastasis ; Cell adhesion & migration ; Cell migration ; Cell proliferation ; Colon ; Gelatinase B ; Gene expression ; Intracellular signalling ; Isoforms ; Localization ; Lungs ; Matrix metalloproteinase ; Metalloproteinase ; Metastases ; Metastasis ; non‐proteolytic MMP ; nuclear MMP ; Nuclei (cytology) ; PEX domain ; Proteolysis ; Stroma ; Stromelysin 1 ; Transcription ; Tumor cell lines ; tumor stroma ; Tumors</subject><ispartof>Journal of cellular biochemistry, 2018-09, Vol.119 (9), p.7363-7376</ispartof><rights>2018 Wiley Periodicals, Inc.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><cites>FETCH-LOGICAL-c4580-ba44cb14b9194766cd72c4c790abe2b41c187a58aa56e3c6cd6b480ef6e658243</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://onlinelibrary.wiley.com/doi/pdf/10.1002%2Fjcb.27040$$EPDF$$P50$$Gwiley$$H</linktopdf><linktohtml>$$Uhttps://onlinelibrary.wiley.com/doi/full/10.1002%2Fjcb.27040$$EHTML$$P50$$Gwiley$$H</linktohtml><link.rule.ids>314,780,784,1417,27924,27925,45574,45575</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/29761931$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Okusha, Yuka</creatorcontrib><creatorcontrib>Eguchi, Takanori</creatorcontrib><creatorcontrib>Sogawa, Chiharu</creatorcontrib><creatorcontrib>Okui, Tatsuo</creatorcontrib><creatorcontrib>Nakano, Keisuke</creatorcontrib><creatorcontrib>Okamoto, Kuniaki</creatorcontrib><creatorcontrib>Kozaki, Ken‐Ichi</creatorcontrib><title>The intranuclear PEX domain of MMP involves proliferation, migration, and metastasis of aggressive adenocarcinoma cells</title><title>Journal of cellular biochemistry</title><addtitle>J Cell Biochem</addtitle><description>Members of matrix metalloproteinase (MMP) family promote cancer cell migration, invasion, and metastasis through alteration of the tumor milieu, intracellular signaling pathways, and transcription. We examined gene expression signatures of colon adenocarcinoma cell lines with different metastatic potentials and found that rapidly metastatic cells powerfully expressed genes encoding MMP3 and MMP9. The non‐proteolytic PEX isoform and proteolytic isoforms of MMPs were significantly expressed in the metastatic cells in vitro. Knockdown of MMP3 attenuated cancer cell migration and invasion in vitro and lung metastasis in vivo. Profound nuclear localization of MMP3/PEX was found in tumor‐stroma marginal area. In contrast, MMP9 was localized in central area of subcutaneous tumors. Overexpression of the PEX isoform of MMP3 promoted proliferation and migration of the rapidly metastatic cells in vitro. Taken together, the non‐proteolytic PEX isoform of MMPs locating in cell nuclei involves proliferation, migration, and subsequent metastasis of aggressive adenocarcinoma cells.
Profound nuclear localization of MMP3/PEX was found in tumor‐stroma marginal area. Overexpression of the PEX isoform of MMP3 promoted proliferation and migration of the rapidly metastatic cells in vitro. The non‐proteolytic PEX isoform of MMPs locating in cell nuclei involves proliferation, migration, and subsequent metastasis of aggressive adenocarcinoma cells.</description><subject>Adenocarcinoma</subject><subject>Cancer</subject><subject>cancer metastasis</subject><subject>Cell adhesion & migration</subject><subject>Cell migration</subject><subject>Cell proliferation</subject><subject>Colon</subject><subject>Gelatinase B</subject><subject>Gene expression</subject><subject>Intracellular signalling</subject><subject>Isoforms</subject><subject>Localization</subject><subject>Lungs</subject><subject>Matrix metalloproteinase</subject><subject>Metalloproteinase</subject><subject>Metastases</subject><subject>Metastasis</subject><subject>non‐proteolytic MMP</subject><subject>nuclear MMP</subject><subject>Nuclei (cytology)</subject><subject>PEX domain</subject><subject>Proteolysis</subject><subject>Stroma</subject><subject>Stromelysin 1</subject><subject>Transcription</subject><subject>Tumor cell lines</subject><subject>tumor stroma</subject><subject>Tumors</subject><issn>0730-2312</issn><issn>1097-4644</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2018</creationdate><recordtype>article</recordtype><recordid>eNp1kdFKHDEUhoNYdLW96AuUgDcVHD3JZGcml-2itkWpFxZ6F85kzmyzzCQ22Vnx7c12tReFwoEEzpePn_yMvRdwLgDkxcq257IGBXtsJkDXhaqU2mczqEsoZCnkITtKaQUAWpfygB1KXVdCl2LGHu9_EXd-HdFPdiCM_O7yJ-_CiM7z0PPb27u83oRhQ4k_xDC4niKuXfBnfHTL1yv6jo-0xpTHpe1DXC4jpeQ2xLEjHyxG63z2ckvDkN6yNz0Oid69nMfsx9Xl_eJLcfP9-uvi001h1byBokWlbCtUq4VWdVXZrpZW2VoDtiRbJaxoapw3iPOKSpv3VasaoL6iat5IVR6zjztvzv57orQ2o0vbBOgpTMlIKLVs8oiMnvyDrsIUfU5npBAgt5jM1OmOsjGkFKk3D9GNGJ-MALNtw-Q2zJ82MvvhxTi1I3V_ydfvz8DFDnh0Az3932S-LT7vlM-obZPp</recordid><startdate>201809</startdate><enddate>201809</enddate><creator>Okusha, Yuka</creator><creator>Eguchi, Takanori</creator><creator>Sogawa, Chiharu</creator><creator>Okui, Tatsuo</creator><creator>Nakano, Keisuke</creator><creator>Okamoto, Kuniaki</creator><creator>Kozaki, Ken‐Ichi</creator><general>Wiley Subscription Services, Inc</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7T7</scope><scope>7TK</scope><scope>7U9</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>H94</scope><scope>K9.</scope><scope>M7N</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>201809</creationdate><title>The intranuclear PEX domain of MMP involves proliferation, migration, and metastasis of aggressive adenocarcinoma cells</title><author>Okusha, Yuka ; Eguchi, Takanori ; Sogawa, Chiharu ; Okui, Tatsuo ; Nakano, Keisuke ; Okamoto, Kuniaki ; Kozaki, Ken‐Ichi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4580-ba44cb14b9194766cd72c4c790abe2b41c187a58aa56e3c6cd6b480ef6e658243</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2018</creationdate><topic>Adenocarcinoma</topic><topic>Cancer</topic><topic>cancer metastasis</topic><topic>Cell adhesion & migration</topic><topic>Cell migration</topic><topic>Cell proliferation</topic><topic>Colon</topic><topic>Gelatinase B</topic><topic>Gene expression</topic><topic>Intracellular signalling</topic><topic>Isoforms</topic><topic>Localization</topic><topic>Lungs</topic><topic>Matrix metalloproteinase</topic><topic>Metalloproteinase</topic><topic>Metastases</topic><topic>Metastasis</topic><topic>non‐proteolytic MMP</topic><topic>nuclear MMP</topic><topic>Nuclei (cytology)</topic><topic>PEX domain</topic><topic>Proteolysis</topic><topic>Stroma</topic><topic>Stromelysin 1</topic><topic>Transcription</topic><topic>Tumor cell lines</topic><topic>tumor stroma</topic><topic>Tumors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Okusha, Yuka</creatorcontrib><creatorcontrib>Eguchi, Takanori</creatorcontrib><creatorcontrib>Sogawa, Chiharu</creatorcontrib><creatorcontrib>Okui, Tatsuo</creatorcontrib><creatorcontrib>Nakano, Keisuke</creatorcontrib><creatorcontrib>Okamoto, Kuniaki</creatorcontrib><creatorcontrib>Kozaki, Ken‐Ichi</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Neurosciences Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Okusha, Yuka</au><au>Eguchi, Takanori</au><au>Sogawa, Chiharu</au><au>Okui, Tatsuo</au><au>Nakano, Keisuke</au><au>Okamoto, Kuniaki</au><au>Kozaki, Ken‐Ichi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The intranuclear PEX domain of MMP involves proliferation, migration, and metastasis of aggressive adenocarcinoma cells</atitle><jtitle>Journal of cellular biochemistry</jtitle><addtitle>J Cell Biochem</addtitle><date>2018-09</date><risdate>2018</risdate><volume>119</volume><issue>9</issue><spage>7363</spage><epage>7376</epage><pages>7363-7376</pages><issn>0730-2312</issn><eissn>1097-4644</eissn><abstract>Members of matrix metalloproteinase (MMP) family promote cancer cell migration, invasion, and metastasis through alteration of the tumor milieu, intracellular signaling pathways, and transcription. We examined gene expression signatures of colon adenocarcinoma cell lines with different metastatic potentials and found that rapidly metastatic cells powerfully expressed genes encoding MMP3 and MMP9. The non‐proteolytic PEX isoform and proteolytic isoforms of MMPs were significantly expressed in the metastatic cells in vitro. Knockdown of MMP3 attenuated cancer cell migration and invasion in vitro and lung metastasis in vivo. Profound nuclear localization of MMP3/PEX was found in tumor‐stroma marginal area. In contrast, MMP9 was localized in central area of subcutaneous tumors. Overexpression of the PEX isoform of MMP3 promoted proliferation and migration of the rapidly metastatic cells in vitro. Taken together, the non‐proteolytic PEX isoform of MMPs locating in cell nuclei involves proliferation, migration, and subsequent metastasis of aggressive adenocarcinoma cells.
Profound nuclear localization of MMP3/PEX was found in tumor‐stroma marginal area. Overexpression of the PEX isoform of MMP3 promoted proliferation and migration of the rapidly metastatic cells in vitro. The non‐proteolytic PEX isoform of MMPs locating in cell nuclei involves proliferation, migration, and subsequent metastasis of aggressive adenocarcinoma cells.</abstract><cop>United States</cop><pub>Wiley Subscription Services, Inc</pub><pmid>29761931</pmid><doi>10.1002/jcb.27040</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | Adenocarcinoma Cancer cancer metastasis Cell adhesion & migration Cell migration Cell proliferation Colon Gelatinase B Gene expression Intracellular signalling Isoforms Localization Lungs Matrix metalloproteinase Metalloproteinase Metastases Metastasis non‐proteolytic MMP nuclear MMP Nuclei (cytology) PEX domain Proteolysis Stroma Stromelysin 1 Transcription Tumor cell lines tumor stroma Tumors |
| title | The intranuclear PEX domain of MMP involves proliferation, migration, and metastasis of aggressive adenocarcinoma cells |
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