MT1-MMP-Mediated Cleavage of Decorin in Corneal Angiogenesis

Background/Aims: Decorin has been shown to have antiangiogenic properties. In this study, we evaluate the involvement of membrane type 1-matrix metalloproteinase (MT1-MMP), a proangiogenic enzyme, in decorin cleavage in the cornea. Methods: MT1-MMP expression was confirmed immunohistochemically in k...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Journal of vascular research 2009-01, Vol.46 (6), p.541-550
Hauptverfasser: Mimura, Tatsuya, Han, Kyu Yeon, Onguchi, Tatsuya, Chang, Jin-Hong, Kim, Tae-im, Kojima, Takashi, Zhou, Zhongjun, Azar, Dimitri T.
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 550
container_issue 6
container_start_page 541
container_title Journal of vascular research
container_volume 46
creator Mimura, Tatsuya
Han, Kyu Yeon
Onguchi, Tatsuya
Chang, Jin-Hong
Kim, Tae-im
Kojima, Takashi
Zhou, Zhongjun
Azar, Dimitri T.
description Background/Aims: Decorin has been shown to have antiangiogenic properties. In this study, we evaluate the involvement of membrane type 1-matrix metalloproteinase (MT1-MMP), a proangiogenic enzyme, in decorin cleavage in the cornea. Methods: MT1-MMP expression was confirmed immunohistochemically in keratocytes and immortalized corneal fibroblast cell lines. Corneal micropockets of bFGF were used to assess the expression of decorin and MT1-MMP. Western blotting was used to evaluate decorin degradation by MT1-MMP. Aortic ring tube formation assays were used to assay the inhibitory effect of decorin and stimulatory effect of MT1-MMP on vascular endothelial cells in vitro. Results: We show that MT1-MMP expression is upregulated following bFGF pellet implantation in the cornea in vivo, and that MT1-MMP cleaves decorin in a time- and concentration-dependent manner in vitro. Furthermore, the addition of MT1-MMP reduces the inhibitory effects of decorin on aortic ring tube formation in vitro. Cleavage of decorin by MT1-MMP-deficient corneal cell lysates is diminished relative to that by wild-type corneal cell lysates, and an MT1-MMP knockin restores decorin processing in vitro. Conclusion: The proangiogenic role of MT1-MMP in the cornea may be mediated, in part, by facilitated cleavage of corneal decorin.
doi_str_mv 10.1159/000226222
format Article
fullrecord <record><control><sourceid>proquest_pasca</sourceid><recordid>TN_cdi_pascalfrancis_primary_22010191</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>1887289911</sourcerecordid><originalsourceid>FETCH-LOGICAL-c517t-7b9172228fb524b1cece79fc2611c09708dfd0c31a84f92f995360a5c7b911d93</originalsourceid><addsrcrecordid>eNpVkc1LxDAQxYMofh-8ixTBg4fqzLRpGxBB1k_YRQ96Dtk0qdXaaLIr-N-bdZdVYSAD-eW9xwtjewgniFycAgBRQUQrbBNzylLAjK_GHbBKEUvaYFshvABgLqpinW2g4CXyMt9kZ6NHTEejh3Rk6lZNTJ0MOqM-VWMSZ5NLo51v-yTOwPneqC656JvWNaY3oQ07bM2qLpjdxbnNnq6vHge36fD-5m5wMUw1x3KSlmMRMxBVdswpH6M22pTCaioQNYgSqtrWoDNUVW4FWSF4VoDievYQa5Fts_O57vt0_GZqbfqJV5189-2b8l_SqVb-v-nbZ9m4T5mVIIB4FDhcCHj3MTVhIl_c1PcxsyTKeZ4DFhE6nkPauxC8sUsDBDnrWS57juzB30S_5KLYCBwtABW06qxXvW7DkiOC-DkCI7c_516Vb4z_A_z4fAOk_Yuq</addsrcrecordid><sourcetype>Open Access Repository</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>224544016</pqid></control><display><type>article</type><title>MT1-MMP-Mediated Cleavage of Decorin in Corneal Angiogenesis</title><source>MEDLINE</source><source>Karger Journals</source><source>Alma/SFX Local Collection</source><creator>Mimura, Tatsuya ; Han, Kyu Yeon ; Onguchi, Tatsuya ; Chang, Jin-Hong ; Kim, Tae-im ; Kojima, Takashi ; Zhou, Zhongjun ; Azar, Dimitri T.</creator><creatorcontrib>Mimura, Tatsuya ; Han, Kyu Yeon ; Onguchi, Tatsuya ; Chang, Jin-Hong ; Kim, Tae-im ; Kojima, Takashi ; Zhou, Zhongjun ; Azar, Dimitri T.</creatorcontrib><description>Background/Aims: Decorin has been shown to have antiangiogenic properties. In this study, we evaluate the involvement of membrane type 1-matrix metalloproteinase (MT1-MMP), a proangiogenic enzyme, in decorin cleavage in the cornea. Methods: MT1-MMP expression was confirmed immunohistochemically in keratocytes and immortalized corneal fibroblast cell lines. Corneal micropockets of bFGF were used to assess the expression of decorin and MT1-MMP. Western blotting was used to evaluate decorin degradation by MT1-MMP. Aortic ring tube formation assays were used to assay the inhibitory effect of decorin and stimulatory effect of MT1-MMP on vascular endothelial cells in vitro. Results: We show that MT1-MMP expression is upregulated following bFGF pellet implantation in the cornea in vivo, and that MT1-MMP cleaves decorin in a time- and concentration-dependent manner in vitro. Furthermore, the addition of MT1-MMP reduces the inhibitory effects of decorin on aortic ring tube formation in vitro. Cleavage of decorin by MT1-MMP-deficient corneal cell lysates is diminished relative to that by wild-type corneal cell lysates, and an MT1-MMP knockin restores decorin processing in vitro. Conclusion: The proangiogenic role of MT1-MMP in the cornea may be mediated, in part, by facilitated cleavage of corneal decorin.</description><identifier>ISSN: 1018-1172</identifier><identifier>EISSN: 1423-0135</identifier><identifier>DOI: 10.1159/000226222</identifier><identifier>PMID: 19571574</identifier><identifier>CODEN: JVREE9</identifier><language>eng</language><publisher>Basel, Switzerland: Karger</publisher><subject>Animals ; Aorta - enzymology ; Biological and medical sciences ; Cell Line ; Cornea - enzymology ; Corneal Neovascularization - chemically induced ; Corneal Neovascularization - enzymology ; Culture Media, Conditioned - metabolism ; Decorin ; Dipeptides - pharmacology ; Disease Models, Animal ; Extracellular Matrix Proteins - metabolism ; Fibroblast Growth Factor 2 ; Fundamental and applied biological sciences. Psychology ; Kinetics ; Matrix Metalloproteinase 14 - deficiency ; Matrix Metalloproteinase 14 - genetics ; Matrix Metalloproteinase 14 - metabolism ; Matrix Metalloproteinase Inhibitors ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Protease Inhibitors - pharmacology ; Proteoglycans - metabolism ; Recombinant Proteins - metabolism ; Research Paper ; Tissue Culture Techniques ; Transfection ; Vertebrates: cardiovascular system</subject><ispartof>Journal of vascular research, 2009-01, Vol.46 (6), p.541-550</ispartof><rights>2009 S. Karger AG, Basel</rights><rights>2009 INIST-CNRS</rights><rights>Copyright 2009 S. Karger AG, Basel.</rights><rights>Copyright (c) 2009 S. Karger AG, Basel</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c517t-7b9172228fb524b1cece79fc2611c09708dfd0c31a84f92f995360a5c7b911d93</citedby><cites>FETCH-LOGICAL-c517t-7b9172228fb524b1cece79fc2611c09708dfd0c31a84f92f995360a5c7b911d93</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,2427,27915,27916</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=22010191$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19571574$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Mimura, Tatsuya</creatorcontrib><creatorcontrib>Han, Kyu Yeon</creatorcontrib><creatorcontrib>Onguchi, Tatsuya</creatorcontrib><creatorcontrib>Chang, Jin-Hong</creatorcontrib><creatorcontrib>Kim, Tae-im</creatorcontrib><creatorcontrib>Kojima, Takashi</creatorcontrib><creatorcontrib>Zhou, Zhongjun</creatorcontrib><creatorcontrib>Azar, Dimitri T.</creatorcontrib><title>MT1-MMP-Mediated Cleavage of Decorin in Corneal Angiogenesis</title><title>Journal of vascular research</title><addtitle>J Vasc Res</addtitle><description>Background/Aims: Decorin has been shown to have antiangiogenic properties. In this study, we evaluate the involvement of membrane type 1-matrix metalloproteinase (MT1-MMP), a proangiogenic enzyme, in decorin cleavage in the cornea. Methods: MT1-MMP expression was confirmed immunohistochemically in keratocytes and immortalized corneal fibroblast cell lines. Corneal micropockets of bFGF were used to assess the expression of decorin and MT1-MMP. Western blotting was used to evaluate decorin degradation by MT1-MMP. Aortic ring tube formation assays were used to assay the inhibitory effect of decorin and stimulatory effect of MT1-MMP on vascular endothelial cells in vitro. Results: We show that MT1-MMP expression is upregulated following bFGF pellet implantation in the cornea in vivo, and that MT1-MMP cleaves decorin in a time- and concentration-dependent manner in vitro. Furthermore, the addition of MT1-MMP reduces the inhibitory effects of decorin on aortic ring tube formation in vitro. Cleavage of decorin by MT1-MMP-deficient corneal cell lysates is diminished relative to that by wild-type corneal cell lysates, and an MT1-MMP knockin restores decorin processing in vitro. Conclusion: The proangiogenic role of MT1-MMP in the cornea may be mediated, in part, by facilitated cleavage of corneal decorin.</description><subject>Animals</subject><subject>Aorta - enzymology</subject><subject>Biological and medical sciences</subject><subject>Cell Line</subject><subject>Cornea - enzymology</subject><subject>Corneal Neovascularization - chemically induced</subject><subject>Corneal Neovascularization - enzymology</subject><subject>Culture Media, Conditioned - metabolism</subject><subject>Decorin</subject><subject>Dipeptides - pharmacology</subject><subject>Disease Models, Animal</subject><subject>Extracellular Matrix Proteins - metabolism</subject><subject>Fibroblast Growth Factor 2</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Kinetics</subject><subject>Matrix Metalloproteinase 14 - deficiency</subject><subject>Matrix Metalloproteinase 14 - genetics</subject><subject>Matrix Metalloproteinase 14 - metabolism</subject><subject>Matrix Metalloproteinase Inhibitors</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>Mice, Knockout</subject><subject>Protease Inhibitors - pharmacology</subject><subject>Proteoglycans - metabolism</subject><subject>Recombinant Proteins - metabolism</subject><subject>Research Paper</subject><subject>Tissue Culture Techniques</subject><subject>Transfection</subject><subject>Vertebrates: cardiovascular system</subject><issn>1018-1172</issn><issn>1423-0135</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNpVkc1LxDAQxYMofh-8ixTBg4fqzLRpGxBB1k_YRQ96Dtk0qdXaaLIr-N-bdZdVYSAD-eW9xwtjewgniFycAgBRQUQrbBNzylLAjK_GHbBKEUvaYFshvABgLqpinW2g4CXyMt9kZ6NHTEejh3Rk6lZNTJ0MOqM-VWMSZ5NLo51v-yTOwPneqC656JvWNaY3oQ07bM2qLpjdxbnNnq6vHge36fD-5m5wMUw1x3KSlmMRMxBVdswpH6M22pTCaioQNYgSqtrWoDNUVW4FWSF4VoDievYQa5Fts_O57vt0_GZqbfqJV5189-2b8l_SqVb-v-nbZ9m4T5mVIIB4FDhcCHj3MTVhIl_c1PcxsyTKeZ4DFhE6nkPauxC8sUsDBDnrWS57juzB30S_5KLYCBwtABW06qxXvW7DkiOC-DkCI7c_516Vb4z_A_z4fAOk_Yuq</recordid><startdate>20090101</startdate><enddate>20090101</enddate><creator>Mimura, Tatsuya</creator><creator>Han, Kyu Yeon</creator><creator>Onguchi, Tatsuya</creator><creator>Chang, Jin-Hong</creator><creator>Kim, Tae-im</creator><creator>Kojima, Takashi</creator><creator>Zhou, Zhongjun</creator><creator>Azar, Dimitri T.</creator><general>Karger</general><general>S. Karger AG</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>3V.</scope><scope>7QL</scope><scope>7T7</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8FD</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BENPR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7N</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>S0X</scope><scope>5PM</scope></search><sort><creationdate>20090101</creationdate><title>MT1-MMP-Mediated Cleavage of Decorin in Corneal Angiogenesis</title><author>Mimura, Tatsuya ; Han, Kyu Yeon ; Onguchi, Tatsuya ; Chang, Jin-Hong ; Kim, Tae-im ; Kojima, Takashi ; Zhou, Zhongjun ; Azar, Dimitri T.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c517t-7b9172228fb524b1cece79fc2611c09708dfd0c31a84f92f995360a5c7b911d93</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Aorta - enzymology</topic><topic>Biological and medical sciences</topic><topic>Cell Line</topic><topic>Cornea - enzymology</topic><topic>Corneal Neovascularization - chemically induced</topic><topic>Corneal Neovascularization - enzymology</topic><topic>Culture Media, Conditioned - metabolism</topic><topic>Decorin</topic><topic>Dipeptides - pharmacology</topic><topic>Disease Models, Animal</topic><topic>Extracellular Matrix Proteins - metabolism</topic><topic>Fibroblast Growth Factor 2</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Kinetics</topic><topic>Matrix Metalloproteinase 14 - deficiency</topic><topic>Matrix Metalloproteinase 14 - genetics</topic><topic>Matrix Metalloproteinase 14 - metabolism</topic><topic>Matrix Metalloproteinase Inhibitors</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>Mice, Knockout</topic><topic>Protease Inhibitors - pharmacology</topic><topic>Proteoglycans - metabolism</topic><topic>Recombinant Proteins - metabolism</topic><topic>Research Paper</topic><topic>Tissue Culture Techniques</topic><topic>Transfection</topic><topic>Vertebrates: cardiovascular system</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Mimura, Tatsuya</creatorcontrib><creatorcontrib>Han, Kyu Yeon</creatorcontrib><creatorcontrib>Onguchi, Tatsuya</creatorcontrib><creatorcontrib>Chang, Jin-Hong</creatorcontrib><creatorcontrib>Kim, Tae-im</creatorcontrib><creatorcontrib>Kojima, Takashi</creatorcontrib><creatorcontrib>Zhou, Zhongjun</creatorcontrib><creatorcontrib>Azar, Dimitri T.</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>ProQuest Central (Corporate)</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Virology and AIDS Abstracts</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>ProQuest Central</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>SIRS Editorial</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of vascular research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Mimura, Tatsuya</au><au>Han, Kyu Yeon</au><au>Onguchi, Tatsuya</au><au>Chang, Jin-Hong</au><au>Kim, Tae-im</au><au>Kojima, Takashi</au><au>Zhou, Zhongjun</au><au>Azar, Dimitri T.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>MT1-MMP-Mediated Cleavage of Decorin in Corneal Angiogenesis</atitle><jtitle>Journal of vascular research</jtitle><addtitle>J Vasc Res</addtitle><date>2009-01-01</date><risdate>2009</risdate><volume>46</volume><issue>6</issue><spage>541</spage><epage>550</epage><pages>541-550</pages><issn>1018-1172</issn><eissn>1423-0135</eissn><coden>JVREE9</coden><abstract>Background/Aims: Decorin has been shown to have antiangiogenic properties. In this study, we evaluate the involvement of membrane type 1-matrix metalloproteinase (MT1-MMP), a proangiogenic enzyme, in decorin cleavage in the cornea. Methods: MT1-MMP expression was confirmed immunohistochemically in keratocytes and immortalized corneal fibroblast cell lines. Corneal micropockets of bFGF were used to assess the expression of decorin and MT1-MMP. Western blotting was used to evaluate decorin degradation by MT1-MMP. Aortic ring tube formation assays were used to assay the inhibitory effect of decorin and stimulatory effect of MT1-MMP on vascular endothelial cells in vitro. Results: We show that MT1-MMP expression is upregulated following bFGF pellet implantation in the cornea in vivo, and that MT1-MMP cleaves decorin in a time- and concentration-dependent manner in vitro. Furthermore, the addition of MT1-MMP reduces the inhibitory effects of decorin on aortic ring tube formation in vitro. Cleavage of decorin by MT1-MMP-deficient corneal cell lysates is diminished relative to that by wild-type corneal cell lysates, and an MT1-MMP knockin restores decorin processing in vitro. Conclusion: The proangiogenic role of MT1-MMP in the cornea may be mediated, in part, by facilitated cleavage of corneal decorin.</abstract><cop>Basel, Switzerland</cop><pub>Karger</pub><pmid>19571574</pmid><doi>10.1159/000226222</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record>
fulltext fulltext
identifier ISSN: 1018-1172
ispartof Journal of vascular research, 2009-01, Vol.46 (6), p.541-550
issn 1018-1172
1423-0135
language eng
recordid cdi_pascalfrancis_primary_22010191
source MEDLINE; Karger Journals; Alma/SFX Local Collection
subjects Animals
Aorta - enzymology
Biological and medical sciences
Cell Line
Cornea - enzymology
Corneal Neovascularization - chemically induced
Corneal Neovascularization - enzymology
Culture Media, Conditioned - metabolism
Decorin
Dipeptides - pharmacology
Disease Models, Animal
Extracellular Matrix Proteins - metabolism
Fibroblast Growth Factor 2
Fundamental and applied biological sciences. Psychology
Kinetics
Matrix Metalloproteinase 14 - deficiency
Matrix Metalloproteinase 14 - genetics
Matrix Metalloproteinase 14 - metabolism
Matrix Metalloproteinase Inhibitors
Mice
Mice, Inbred C57BL
Mice, Knockout
Protease Inhibitors - pharmacology
Proteoglycans - metabolism
Recombinant Proteins - metabolism
Research Paper
Tissue Culture Techniques
Transfection
Vertebrates: cardiovascular system
title MT1-MMP-Mediated Cleavage of Decorin in Corneal Angiogenesis
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-14T22%3A07%3A18IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_pasca&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=MT1-MMP-Mediated%20Cleavage%20of%20Decorin%20in%20Corneal%20Angiogenesis&rft.jtitle=Journal%20of%20vascular%20research&rft.au=Mimura,%20Tatsuya&rft.date=2009-01-01&rft.volume=46&rft.issue=6&rft.spage=541&rft.epage=550&rft.pages=541-550&rft.issn=1018-1172&rft.eissn=1423-0135&rft.coden=JVREE9&rft_id=info:doi/10.1159/000226222&rft_dat=%3Cproquest_pasca%3E1887289911%3C/proquest_pasca%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=224544016&rft_id=info:pmid/19571574&rfr_iscdi=true