Matriptase activates stromelysin (MMP‐3) and promotes tumor growth and angiogenesis
Matriptase/MT‐SP1, a type II membrane serine protease widely expressed in normal epithelial cells and human carcinoma cells, is thought to be involved in cancer progression. To clarify this possibility, we overexpressed exogenous matriptase in the human stomach cancer cell line AZ521. In vitro, the...
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| Veröffentlicht in: | Cancer science 2006-12, Vol.97 (12), p.1327-1334 |
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| creator | Jin, Xinlian Yagi, Motoki Akiyama, Nagisa Hirosaki, Tomomi Higashi, Shouichi Lin, Chen‐Yong Dickson, Robert B. Kitamura, Hitoshi Miyazaki, Kaoru |
| description | Matriptase/MT‐SP1, a type II membrane serine protease widely expressed in normal epithelial cells and human carcinoma cells, is thought to be involved in cancer progression. To clarify this possibility, we overexpressed exogenous matriptase in the human stomach cancer cell line AZ521. In vitro, the matriptase transfectant (Mat‐AZ521) and the control transfectant (Mock‐AZ521) showed a similar growth rate, although the saturation cell density was significantly higher with the Mat‐AZ521. When implanted into nude mice subcutaneously or intraperitoneally, Mat‐AZ521 cells grew faster and produced much larger solid tumors than Mock‐AZ521 cells. The overexpression of matriptase in AZ521 cells shortened the survival time of tumor‐bearing mice. Histological analysis showed that both the number and the size of blood vessels in tumor tissues were significantly higher in the Mat‐AZ521 tumors than the Mock‐AZ521 ones. Moreover, it was found that purified matriptase activated one of the important matrix metalloproteinases, stromelysin (MMP‐3). These results suggest the possibility that the matriptase‐dependent activation of MMP‐3, as well as the direct activity of matriptase, promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments. (Cancer Sci 2006; 97: 1327–1334) |
| doi_str_mv | 10.1111/j.1349-7006.2006.00328.x |
| format | Article |
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To clarify this possibility, we overexpressed exogenous matriptase in the human stomach cancer cell line AZ521. In vitro, the matriptase transfectant (Mat‐AZ521) and the control transfectant (Mock‐AZ521) showed a similar growth rate, although the saturation cell density was significantly higher with the Mat‐AZ521. When implanted into nude mice subcutaneously or intraperitoneally, Mat‐AZ521 cells grew faster and produced much larger solid tumors than Mock‐AZ521 cells. The overexpression of matriptase in AZ521 cells shortened the survival time of tumor‐bearing mice. Histological analysis showed that both the number and the size of blood vessels in tumor tissues were significantly higher in the Mat‐AZ521 tumors than the Mock‐AZ521 ones. Moreover, it was found that purified matriptase activated one of the important matrix metalloproteinases, stromelysin (MMP‐3). These results suggest the possibility that the matriptase‐dependent activation of MMP‐3, as well as the direct activity of matriptase, promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments. (Cancer Sci 2006; 97: 1327–1334)</description><identifier>ISSN: 1347-9032</identifier><identifier>EISSN: 1349-7006</identifier><identifier>DOI: 10.1111/j.1349-7006.2006.00328.x</identifier><identifier>PMID: 16999819</identifier><language>eng</language><publisher>Melbourne, Australia: Blackwell Publishing Asia</publisher><subject>Animals ; Biological and medical sciences ; Carcinogenesis, carcinogens and anticarcinogens ; Enzyme Activation ; Gene Expression Regulation, Neoplastic ; General aspects ; Humans ; Immunoblotting ; Immunoenzyme Techniques ; Male ; Matrix Metalloproteinase 3 - metabolism ; Medical sciences ; Mice ; Mice, Inbred BALB C ; Mice, Nude ; Neovascularization, Pathologic - metabolism ; Neovascularization, Pathologic - pathology ; Original ; Reverse Transcriptase Polymerase Chain Reaction ; Serine Endopeptidases - pharmacology ; Stomach Neoplasms - blood supply ; Stomach Neoplasms - metabolism ; Stomach Neoplasms - pathology ; Tumor Cells, Cultured - drug effects ; Tumor Cells, Cultured - enzymology ; Tumors ; Up-Regulation</subject><ispartof>Cancer science, 2006-12, Vol.97 (12), p.1327-1334</ispartof><rights>2007 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5718-1e8532924a71bfe03c2b27c45894bc094979fbc656e3db4be4414ca5325294ca3</citedby><cites>FETCH-LOGICAL-c5718-1e8532924a71bfe03c2b27c45894bc094979fbc656e3db4be4414ca5325294ca3</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/PMC11158936/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC11158936/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,1411,11541,27901,27902,45550,45551,46027,46451,53766,53768</link.rule.ids><linktorsrc>$$Uhttps://onlinelibrary.wiley.com/doi/abs/10.1111%2Fj.1349-7006.2006.00328.x$$EView_record_in_Wiley-Blackwell$$FView_record_in_$$GWiley-Blackwell</linktorsrc><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18323305$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16999819$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Jin, Xinlian</creatorcontrib><creatorcontrib>Yagi, Motoki</creatorcontrib><creatorcontrib>Akiyama, Nagisa</creatorcontrib><creatorcontrib>Hirosaki, Tomomi</creatorcontrib><creatorcontrib>Higashi, Shouichi</creatorcontrib><creatorcontrib>Lin, Chen‐Yong</creatorcontrib><creatorcontrib>Dickson, Robert B.</creatorcontrib><creatorcontrib>Kitamura, Hitoshi</creatorcontrib><creatorcontrib>Miyazaki, Kaoru</creatorcontrib><title>Matriptase activates stromelysin (MMP‐3) and promotes tumor growth and angiogenesis</title><title>Cancer science</title><addtitle>Cancer Sci</addtitle><description>Matriptase/MT‐SP1, a type II membrane serine protease widely expressed in normal epithelial cells and human carcinoma cells, is thought to be involved in cancer progression. To clarify this possibility, we overexpressed exogenous matriptase in the human stomach cancer cell line AZ521. In vitro, the matriptase transfectant (Mat‐AZ521) and the control transfectant (Mock‐AZ521) showed a similar growth rate, although the saturation cell density was significantly higher with the Mat‐AZ521. When implanted into nude mice subcutaneously or intraperitoneally, Mat‐AZ521 cells grew faster and produced much larger solid tumors than Mock‐AZ521 cells. The overexpression of matriptase in AZ521 cells shortened the survival time of tumor‐bearing mice. Histological analysis showed that both the number and the size of blood vessels in tumor tissues were significantly higher in the Mat‐AZ521 tumors than the Mock‐AZ521 ones. Moreover, it was found that purified matriptase activated one of the important matrix metalloproteinases, stromelysin (MMP‐3). These results suggest the possibility that the matriptase‐dependent activation of MMP‐3, as well as the direct activity of matriptase, promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments. (Cancer Sci 2006; 97: 1327–1334)</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carcinogenesis, carcinogens and anticarcinogens</subject><subject>Enzyme Activation</subject><subject>Gene Expression Regulation, Neoplastic</subject><subject>General aspects</subject><subject>Humans</subject><subject>Immunoblotting</subject><subject>Immunoenzyme Techniques</subject><subject>Male</subject><subject>Matrix Metalloproteinase 3 - metabolism</subject><subject>Medical sciences</subject><subject>Mice</subject><subject>Mice, Inbred BALB C</subject><subject>Mice, Nude</subject><subject>Neovascularization, Pathologic - metabolism</subject><subject>Neovascularization, Pathologic - pathology</subject><subject>Original</subject><subject>Reverse Transcriptase Polymerase Chain Reaction</subject><subject>Serine Endopeptidases - pharmacology</subject><subject>Stomach Neoplasms - blood supply</subject><subject>Stomach Neoplasms - metabolism</subject><subject>Stomach Neoplasms - pathology</subject><subject>Tumor Cells, Cultured - drug effects</subject><subject>Tumor Cells, Cultured - enzymology</subject><subject>Tumors</subject><subject>Up-Regulation</subject><issn>1347-9032</issn><issn>1349-7006</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNkc1OGzEQxy1UBCnwCtVeWpXDBn_th6VKVRRRQCJqJeBseZ3Z4Gh3ndpOILc-Qp-RJ8GbRITe6sN4pP9v_jOaQSgheEjiu5gPCeMiLTDOh7QPGDNaDp8P0OBN-LDJi1RE6Rh99H4eoZwLfoSOSS6EKIkYoIeJCs4sgvKQKB3MSgXwiQ_OttCsvemSr5PJr5c_f9l5orppsoiC7ZGwbK1LZs4-hceNorqZsTPowBt_ig5r1Xg42_0n6OHH5f34Or39eXUzHt2mOitImRIoM0YF5aogVQ2YaVrRQvOsFLzSWHBRiLrSeZYDm1a8As4J1yrWZFTEhJ2g71vfxbJqYaqhC041cuFMq9xaWmXkv0pnHuXMrmRcYmzC8ujwZefg7O8l-CBb4zU0jerALr3MS0IoISKC5RbUznrvoH7rQnBvR-Rc9ruX_e5lfxS5OYp8jqWf3k-5L9xdIQKfd4DyWjW1U502fs-VjDKGs8h923JPpoH1fw8gx6O7mLBXemCpwQ</recordid><startdate>200612</startdate><enddate>200612</enddate><creator>Jin, Xinlian</creator><creator>Yagi, Motoki</creator><creator>Akiyama, Nagisa</creator><creator>Hirosaki, Tomomi</creator><creator>Higashi, Shouichi</creator><creator>Lin, Chen‐Yong</creator><creator>Dickson, Robert B.</creator><creator>Kitamura, Hitoshi</creator><creator>Miyazaki, Kaoru</creator><general>Blackwell Publishing Asia</general><general>Blackwell</general><scope>IQODW</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>200612</creationdate><title>Matriptase activates stromelysin (MMP‐3) and promotes tumor growth and angiogenesis</title><author>Jin, Xinlian ; Yagi, Motoki ; Akiyama, Nagisa ; Hirosaki, Tomomi ; Higashi, Shouichi ; Lin, Chen‐Yong ; Dickson, Robert B. ; Kitamura, Hitoshi ; Miyazaki, Kaoru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5718-1e8532924a71bfe03c2b27c45894bc094979fbc656e3db4be4414ca5325294ca3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carcinogenesis, carcinogens and anticarcinogens</topic><topic>Enzyme Activation</topic><topic>Gene Expression Regulation, Neoplastic</topic><topic>General aspects</topic><topic>Humans</topic><topic>Immunoblotting</topic><topic>Immunoenzyme Techniques</topic><topic>Male</topic><topic>Matrix Metalloproteinase 3 - metabolism</topic><topic>Medical sciences</topic><topic>Mice</topic><topic>Mice, Inbred BALB C</topic><topic>Mice, Nude</topic><topic>Neovascularization, Pathologic - metabolism</topic><topic>Neovascularization, Pathologic - pathology</topic><topic>Original</topic><topic>Reverse Transcriptase Polymerase Chain Reaction</topic><topic>Serine Endopeptidases - pharmacology</topic><topic>Stomach Neoplasms - blood supply</topic><topic>Stomach Neoplasms - metabolism</topic><topic>Stomach Neoplasms - pathology</topic><topic>Tumor Cells, Cultured - drug effects</topic><topic>Tumor Cells, Cultured - enzymology</topic><topic>Tumors</topic><topic>Up-Regulation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jin, Xinlian</creatorcontrib><creatorcontrib>Yagi, Motoki</creatorcontrib><creatorcontrib>Akiyama, Nagisa</creatorcontrib><creatorcontrib>Hirosaki, Tomomi</creatorcontrib><creatorcontrib>Higashi, Shouichi</creatorcontrib><creatorcontrib>Lin, Chen‐Yong</creatorcontrib><creatorcontrib>Dickson, Robert B.</creatorcontrib><creatorcontrib>Kitamura, Hitoshi</creatorcontrib><creatorcontrib>Miyazaki, Kaoru</creatorcontrib><collection>Pascal-Francis</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>Cancer science</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext_linktorsrc</fulltext></delivery><addata><au>Jin, Xinlian</au><au>Yagi, Motoki</au><au>Akiyama, Nagisa</au><au>Hirosaki, Tomomi</au><au>Higashi, Shouichi</au><au>Lin, Chen‐Yong</au><au>Dickson, Robert B.</au><au>Kitamura, Hitoshi</au><au>Miyazaki, Kaoru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Matriptase activates stromelysin (MMP‐3) and promotes tumor growth and angiogenesis</atitle><jtitle>Cancer science</jtitle><addtitle>Cancer Sci</addtitle><date>2006-12</date><risdate>2006</risdate><volume>97</volume><issue>12</issue><spage>1327</spage><epage>1334</epage><pages>1327-1334</pages><issn>1347-9032</issn><eissn>1349-7006</eissn><abstract>Matriptase/MT‐SP1, a type II membrane serine protease widely expressed in normal epithelial cells and human carcinoma cells, is thought to be involved in cancer progression. To clarify this possibility, we overexpressed exogenous matriptase in the human stomach cancer cell line AZ521. In vitro, the matriptase transfectant (Mat‐AZ521) and the control transfectant (Mock‐AZ521) showed a similar growth rate, although the saturation cell density was significantly higher with the Mat‐AZ521. When implanted into nude mice subcutaneously or intraperitoneally, Mat‐AZ521 cells grew faster and produced much larger solid tumors than Mock‐AZ521 cells. The overexpression of matriptase in AZ521 cells shortened the survival time of tumor‐bearing mice. Histological analysis showed that both the number and the size of blood vessels in tumor tissues were significantly higher in the Mat‐AZ521 tumors than the Mock‐AZ521 ones. Moreover, it was found that purified matriptase activated one of the important matrix metalloproteinases, stromelysin (MMP‐3). These results suggest the possibility that the matriptase‐dependent activation of MMP‐3, as well as the direct activity of matriptase, promotes tumor growth and angiogenesis by enhancing extracellular matrix degradation in tumor cell microenvironments. (Cancer Sci 2006; 97: 1327–1334)</abstract><cop>Melbourne, Australia</cop><pub>Blackwell Publishing Asia</pub><pmid>16999819</pmid><doi>10.1111/j.1349-7006.2006.00328.x</doi><tpages>8</tpages></addata></record> |
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| subjects | Animals Biological and medical sciences Carcinogenesis, carcinogens and anticarcinogens Enzyme Activation Gene Expression Regulation, Neoplastic General aspects Humans Immunoblotting Immunoenzyme Techniques Male Matrix Metalloproteinase 3 - metabolism Medical sciences Mice Mice, Inbred BALB C Mice, Nude Neovascularization, Pathologic - metabolism Neovascularization, Pathologic - pathology Original Reverse Transcriptase Polymerase Chain Reaction Serine Endopeptidases - pharmacology Stomach Neoplasms - blood supply Stomach Neoplasms - metabolism Stomach Neoplasms - pathology Tumor Cells, Cultured - drug effects Tumor Cells, Cultured - enzymology Tumors Up-Regulation |
| title | Matriptase activates stromelysin (MMP‐3) and promotes tumor growth and angiogenesis |
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