Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity
Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a zinc-dependent proteinase found in cholesterol-rich lipid rafts on the plasma membrane. MT1-MMP hydrolyzes extracellular matrix (ECM) proteins, activates pro-matrix metalloproteinase-2 (proMMP-2) and plays an important role in ECM remodeling, c...
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| Veröffentlicht in: | BMB reports 2008, 41(12), , pp.858-862 |
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| creator | Kim, H.N. (Hannam University, Daejeon, Republic of Korea) Chung, H.S. (Hannam University, Daejeon, Republic of Korea), E-mail: hschung@hnu.kr |
| description | Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a zinc-dependent proteinase found in cholesterol-rich lipid rafts on the plasma membrane. MT1-MMP hydrolyzes extracellular matrix (ECM) proteins, activates pro-matrix metalloproteinase-2 (proMMP-2) and plays an important role in ECM remodeling, cancer cell migration and metastasis. The role of caveolin-1, an integral protein of caveolae, in the activation of MT1-MMP remains largely unknown. Here, we show that the expression of caveolin-1 attenuates the activation of proMMP-2, reduces proteolytic cleavage of ECM and inhibits cell migration. We utilized the cytoplasmic tail domain deletion (ΔCT) or the E240A mutant of MT1-MMP. Co-expression of caveolin-1 with the wild-type or the ΔCT MT1-MMP decreased the proMMP-2 activation and inhibited collagen degradation and cell migration. Caveolin-1 had no effect on the catalytically inert E240A MT1-MMP. Our findings suggest that caveolin-1 is essential in the clown-regulation of MT1-MMP activity by promoting intemalization from the cell surface. |
| doi_str_mv | 10.5483/bmbrep.2008.41.12.858 |
| format | Article |
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(Hannam University, Daejeon, Republic of Korea) ; Chung, H.S. (Hannam University, Daejeon, Republic of Korea), E-mail: hschung@hnu.kr</creator><creatorcontrib>Kim, H.N. (Hannam University, Daejeon, Republic of Korea) ; Chung, H.S. (Hannam University, Daejeon, Republic of Korea), E-mail: hschung@hnu.kr</creatorcontrib><description>Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a zinc-dependent proteinase found in cholesterol-rich lipid rafts on the plasma membrane. MT1-MMP hydrolyzes extracellular matrix (ECM) proteins, activates pro-matrix metalloproteinase-2 (proMMP-2) and plays an important role in ECM remodeling, cancer cell migration and metastasis. The role of caveolin-1, an integral protein of caveolae, in the activation of MT1-MMP remains largely unknown. Here, we show that the expression of caveolin-1 attenuates the activation of proMMP-2, reduces proteolytic cleavage of ECM and inhibits cell migration. We utilized the cytoplasmic tail domain deletion (ΔCT) or the E240A mutant of MT1-MMP. Co-expression of caveolin-1 with the wild-type or the ΔCT MT1-MMP decreased the proMMP-2 activation and inhibited collagen degradation and cell migration. Caveolin-1 had no effect on the catalytically inert E240A MT1-MMP. Our findings suggest that caveolin-1 is essential in the clown-regulation of MT1-MMP activity by promoting intemalization from the cell surface.</description><identifier>ISSN: 1976-6696</identifier><identifier>ISSN: 1225-8687</identifier><identifier>EISSN: 1976-670X</identifier><identifier>EISSN: 0219-1024</identifier><identifier>DOI: 10.5483/bmbrep.2008.41.12.858</identifier><identifier>PMID: 19123976</identifier><language>eng</language><publisher>Korea (South): 생화학분자생물학회</publisher><subject>Amino Acid Substitution ; Animals ; Base Sequence ; Caveolin 1 - genetics ; Caveolin 1 - metabolism ; Caveolin-1 ; Cell migration ; Cell Movement - physiology ; CELLS ; CELLULE ; CELULAS ; Cercopithecus aethiops ; Collagen - metabolism ; Collagen degradation ; COS Cells ; DNA Primers - genetics ; Down-Regulation ; Enzyme Activation ; Enzyme Precursors - metabolism ; Extracellular Matrix - metabolism ; Gelatinases - metabolism ; Humans ; Matrix Metalloproteinase 14 - genetics ; Matrix Metalloproteinase 14 - metabolism ; Matrix Metalloproteinase Inhibitors ; MMP-2 ; MT1-MMP ; Mutagenesis, Site-Directed ; Recombinant Proteins - genetics ; Recombinant Proteins - metabolism ; Sequence Deletion ; Transfection ; 생물학</subject><ispartof>BMB reports, 2008, 41(12), , pp.858-862</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c459t-d9235daad88519376023ed33148e0383872871cd056c2df04b59a4504055b9973</citedby><cites>FETCH-LOGICAL-c459t-d9235daad88519376023ed33148e0383872871cd056c2df04b59a4504055b9973</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,864,885,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19123976$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink><backlink>$$Uhttps://www.kci.go.kr/kciportal/ci/sereArticleSearch/ciSereArtiView.kci?sereArticleSearchBean.artiId=ART001301138$$DAccess content in National Research Foundation of Korea (NRF)$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, H.N. (Hannam University, Daejeon, Republic of Korea)</creatorcontrib><creatorcontrib>Chung, H.S. (Hannam University, Daejeon, Republic of Korea), E-mail: hschung@hnu.kr</creatorcontrib><title>Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity</title><title>BMB reports</title><addtitle>BMB Reports</addtitle><description>Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a zinc-dependent proteinase found in cholesterol-rich lipid rafts on the plasma membrane. MT1-MMP hydrolyzes extracellular matrix (ECM) proteins, activates pro-matrix metalloproteinase-2 (proMMP-2) and plays an important role in ECM remodeling, cancer cell migration and metastasis. The role of caveolin-1, an integral protein of caveolae, in the activation of MT1-MMP remains largely unknown. Here, we show that the expression of caveolin-1 attenuates the activation of proMMP-2, reduces proteolytic cleavage of ECM and inhibits cell migration. We utilized the cytoplasmic tail domain deletion (ΔCT) or the E240A mutant of MT1-MMP. Co-expression of caveolin-1 with the wild-type or the ΔCT MT1-MMP decreased the proMMP-2 activation and inhibited collagen degradation and cell migration. Caveolin-1 had no effect on the catalytically inert E240A MT1-MMP. Our findings suggest that caveolin-1 is essential in the clown-regulation of MT1-MMP activity by promoting intemalization from the cell surface.</description><subject>Amino Acid Substitution</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Caveolin 1 - genetics</subject><subject>Caveolin 1 - metabolism</subject><subject>Caveolin-1</subject><subject>Cell migration</subject><subject>Cell Movement - physiology</subject><subject>CELLS</subject><subject>CELLULE</subject><subject>CELULAS</subject><subject>Cercopithecus aethiops</subject><subject>Collagen - metabolism</subject><subject>Collagen degradation</subject><subject>COS Cells</subject><subject>DNA Primers - genetics</subject><subject>Down-Regulation</subject><subject>Enzyme Activation</subject><subject>Enzyme Precursors - metabolism</subject><subject>Extracellular Matrix - metabolism</subject><subject>Gelatinases - metabolism</subject><subject>Humans</subject><subject>Matrix Metalloproteinase 14 - genetics</subject><subject>Matrix Metalloproteinase 14 - metabolism</subject><subject>Matrix Metalloproteinase Inhibitors</subject><subject>MMP-2</subject><subject>MT1-MMP</subject><subject>Mutagenesis, Site-Directed</subject><subject>Recombinant Proteins - genetics</subject><subject>Recombinant Proteins - metabolism</subject><subject>Sequence Deletion</subject><subject>Transfection</subject><subject>생물학</subject><issn>1976-6696</issn><issn>1225-8687</issn><issn>1976-670X</issn><issn>0219-1024</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>JDI</sourceid><recordid>eNpFkFtP3DAQhS1UVCjtL0BUeUHiJcHjS2w_LivuVEgrKvXNchKHupubbIPYf18v4fIwmpHPd2asg9AR4IIzSU-rvvJ2KgjGsmBQACkklztoH5Qo81LgP1_e51KVe-hbCP8wLoEI8hXtgQJCk7iPzpfm2Y6dG3LI3PDXVS6GrLdpuRlsHjeTzSDrTfTuJT1H03Xj5Mdo3WCCzUwd3bOLm-9otzVdsD_e-gH6fXH-sLzK7-4vr5eLu7xmXMW8UYTyxphGSg6KihITahtKgUmLqaRSECmgbjAva9K0mFVcGcYxw5xXSgl6gE7mvYNv9bp2ejTutT-Oeu31YvVwrYWgIGRCj2d07UJ0emhCp28Wt_fbwAADpoxwxXji-MzVfgzB21ZP3vXGbzRgvU1an_06W9lJb42agQaiU9LJ93P2TU9Vb5tP11u0CTj8-ED4kIlgnJQqqUez2ppRm0fvgr5dpRMKp1KS_gdS5ojB</recordid><startdate>20081231</startdate><enddate>20081231</enddate><creator>Kim, H.N. (Hannam University, Daejeon, Republic of Korea)</creator><creator>Chung, H.S. (Hannam University, Daejeon, Republic of Korea), E-mail: hschung@hnu.kr</creator><general>생화학분자생물학회</general><general>한국생화학분자생물학회</general><scope>FBQ</scope><scope>HZB</scope><scope>Q5X</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>JDI</scope><scope>ACYCR</scope></search><sort><creationdate>20081231</creationdate><title>Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity</title><author>Kim, H.N. (Hannam University, Daejeon, Republic of Korea) ; Chung, H.S. (Hannam University, Daejeon, Republic of Korea), E-mail: hschung@hnu.kr</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c459t-d9235daad88519376023ed33148e0383872871cd056c2df04b59a4504055b9973</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Substitution</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Caveolin 1 - genetics</topic><topic>Caveolin 1 - metabolism</topic><topic>Caveolin-1</topic><topic>Cell migration</topic><topic>Cell Movement - physiology</topic><topic>CELLS</topic><topic>CELLULE</topic><topic>CELULAS</topic><topic>Cercopithecus aethiops</topic><topic>Collagen - metabolism</topic><topic>Collagen degradation</topic><topic>COS Cells</topic><topic>DNA Primers - genetics</topic><topic>Down-Regulation</topic><topic>Enzyme Activation</topic><topic>Enzyme Precursors - metabolism</topic><topic>Extracellular Matrix - metabolism</topic><topic>Gelatinases - metabolism</topic><topic>Humans</topic><topic>Matrix Metalloproteinase 14 - genetics</topic><topic>Matrix Metalloproteinase 14 - metabolism</topic><topic>Matrix Metalloproteinase Inhibitors</topic><topic>MMP-2</topic><topic>MT1-MMP</topic><topic>Mutagenesis, Site-Directed</topic><topic>Recombinant Proteins - genetics</topic><topic>Recombinant Proteins - metabolism</topic><topic>Sequence Deletion</topic><topic>Transfection</topic><topic>생물학</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, H.N. (Hannam University, Daejeon, Republic of Korea)</creatorcontrib><creatorcontrib>Chung, H.S. (Hannam University, Daejeon, Republic of Korea), E-mail: hschung@hnu.kr</creatorcontrib><collection>AGRIS</collection><collection>Korean Studies Information Service System (KISS)</collection><collection>Korean Studies Information Service System (KISS) B-Type</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>KoreaScience</collection><collection>Korean Citation Index</collection><jtitle>BMB reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, H.N. (Hannam University, Daejeon, Republic of Korea)</au><au>Chung, H.S. (Hannam University, Daejeon, Republic of Korea), E-mail: hschung@hnu.kr</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity</atitle><jtitle>BMB reports</jtitle><addtitle>BMB Reports</addtitle><date>2008-12-31</date><risdate>2008</risdate><volume>41</volume><issue>12</issue><spage>858</spage><epage>862</epage><pages>858-862</pages><issn>1976-6696</issn><issn>1225-8687</issn><eissn>1976-670X</eissn><eissn>0219-1024</eissn><abstract>Membrane-type 1 matrix metalloproteinase (MT1-MMP) is a zinc-dependent proteinase found in cholesterol-rich lipid rafts on the plasma membrane. MT1-MMP hydrolyzes extracellular matrix (ECM) proteins, activates pro-matrix metalloproteinase-2 (proMMP-2) and plays an important role in ECM remodeling, cancer cell migration and metastasis. The role of caveolin-1, an integral protein of caveolae, in the activation of MT1-MMP remains largely unknown. Here, we show that the expression of caveolin-1 attenuates the activation of proMMP-2, reduces proteolytic cleavage of ECM and inhibits cell migration. We utilized the cytoplasmic tail domain deletion (ΔCT) or the E240A mutant of MT1-MMP. Co-expression of caveolin-1 with the wild-type or the ΔCT MT1-MMP decreased the proMMP-2 activation and inhibited collagen degradation and cell migration. Caveolin-1 had no effect on the catalytically inert E240A MT1-MMP. Our findings suggest that caveolin-1 is essential in the clown-regulation of MT1-MMP activity by promoting intemalization from the cell surface.</abstract><cop>Korea (South)</cop><pub>생화학분자생물학회</pub><pmid>19123976</pmid><doi>10.5483/bmbrep.2008.41.12.858</doi><tpages>5</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| subjects | Amino Acid Substitution Animals Base Sequence Caveolin 1 - genetics Caveolin 1 - metabolism Caveolin-1 Cell migration Cell Movement - physiology CELLS CELLULE CELULAS Cercopithecus aethiops Collagen - metabolism Collagen degradation COS Cells DNA Primers - genetics Down-Regulation Enzyme Activation Enzyme Precursors - metabolism Extracellular Matrix - metabolism Gelatinases - metabolism Humans Matrix Metalloproteinase 14 - genetics Matrix Metalloproteinase 14 - metabolism Matrix Metalloproteinase Inhibitors MMP-2 MT1-MMP Mutagenesis, Site-Directed Recombinant Proteins - genetics Recombinant Proteins - metabolism Sequence Deletion Transfection 생물학 |
| title | Caveolin-1 inhibits membrane-type 1 matrix metalloproteinase activity |
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