Involvement of the cytoplasmic juxtamembrane region of matriptase in its exclusive localization to the basolateral membrane domain of Madin-Darby canine kidney epithelial cells
Matriptase is a type II transmembrane serine protease. This protease is strongly expressed in simple epithelial cells such as enterocytes and kidney tubular cells in which the plasma membranes are separated into apical and basolateral domains. Although matriptase was found previously to occur exclus...
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| Veröffentlicht in: | Cytotechnology (Dordrecht) 2009-04, Vol.59 (3), p.169-176 |
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| creator | Murai, Nobuhito Miyake, Yuka Tsuzuki, Satoshi Inouye, Kuniyo Fushiki, Tohru |
| description | Matriptase is a type II transmembrane serine protease. This protease is strongly expressed in simple epithelial cells such as enterocytes and kidney tubular cells in which the plasma membranes are separated into apical and basolateral domains. Although matriptase was found previously to occur exclusively on the basolateral membrane of enterocytes, the underlying mechanism of localization is unclear. In the present study, a full-length rat matriptase and a chimera consisting of the cytoplasmic and transmembrane regions of the protease and green fluorescent protein (designated as 1-86GFP) were found to localize exclusively to the basolateral membrane domain when expressed in Madin-Darby canine kidney epithelial cells. Mutagenesis analysis of 1-86GFP revealed that the matriptase cytoplasmic juxtamembrane amino acid residues (Lys45, Val47, and Arg50) play a role in mediating the localization in the cells. This study provides the first evidence that matriptase carries information for its localization in simple epithelia. |
| doi_str_mv | 10.1007/s10616-009-9205-0 |
| format | Article |
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This protease is strongly expressed in simple epithelial cells such as enterocytes and kidney tubular cells in which the plasma membranes are separated into apical and basolateral domains. Although matriptase was found previously to occur exclusively on the basolateral membrane of enterocytes, the underlying mechanism of localization is unclear. In the present study, a full-length rat matriptase and a chimera consisting of the cytoplasmic and transmembrane regions of the protease and green fluorescent protein (designated as 1-86GFP) were found to localize exclusively to the basolateral membrane domain when expressed in Madin-Darby canine kidney epithelial cells. Mutagenesis analysis of 1-86GFP revealed that the matriptase cytoplasmic juxtamembrane amino acid residues (Lys45, Val47, and Arg50) play a role in mediating the localization in the cells. This study provides the first evidence that matriptase carries information for its localization in simple epithelia.</description><identifier>ISSN: 0920-9069</identifier><identifier>EISSN: 1573-0778</identifier><identifier>DOI: 10.1007/s10616-009-9205-0</identifier><identifier>PMID: 19557537</identifier><language>eng</language><publisher>Dordrecht: Dordrecht : Springer Netherlands</publisher><subject>Amino acids ; Antibodies ; Biochemistry ; Biological and medical sciences ; Biomedicine ; Biotechnology ; Chemistry ; Chemistry and Materials Science ; Chimeras ; Enterocytes ; Epithelial cells ; Fundamental and applied biological sciences. Psychology ; Green fluorescent protein ; Growth factors ; JAACT Special Issue ; Kidneys ; Localization ; Membranes ; Mutagenesis ; Peptides ; Plasma membranes ; Plasmids ; Pore size ; Proteins ; Serine proteinase</subject><ispartof>Cytotechnology (Dordrecht), 2009-04, Vol.59 (3), p.169-176</ispartof><rights>Springer Science+Business Media B.V. 2009</rights><rights>2015 INIST-CNRS</rights><rights>Springer Science+Business Media B.V. 2009.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c589t-1cbf705e26bb7b45265693ba249dc3777c20e9e4e9a1db58362ce1192314d1213</citedby><cites>FETCH-LOGICAL-c589t-1cbf705e26bb7b45265693ba249dc3777c20e9e4e9a1db58362ce1192314d1213</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/PMC2774564/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.proquest.com/docview/2918262685?pq-origsite=primo$$EHTML$$P50$$Gproquest$$H</linktohtml><link.rule.ids>230,309,310,314,727,780,784,789,790,885,21388,23930,23931,25140,27924,27925,33744,41488,42557,43805,51319,53791,53793,64385,64389,72469</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=22250056$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19557537$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Murai, Nobuhito</creatorcontrib><creatorcontrib>Miyake, Yuka</creatorcontrib><creatorcontrib>Tsuzuki, Satoshi</creatorcontrib><creatorcontrib>Inouye, Kuniyo</creatorcontrib><creatorcontrib>Fushiki, Tohru</creatorcontrib><title>Involvement of the cytoplasmic juxtamembrane region of matriptase in its exclusive localization to the basolateral membrane domain of Madin-Darby canine kidney epithelial cells</title><title>Cytotechnology (Dordrecht)</title><addtitle>Cytotechnology</addtitle><addtitle>Cytotechnology</addtitle><description>Matriptase is a type II transmembrane serine protease. This protease is strongly expressed in simple epithelial cells such as enterocytes and kidney tubular cells in which the plasma membranes are separated into apical and basolateral domains. Although matriptase was found previously to occur exclusively on the basolateral membrane of enterocytes, the underlying mechanism of localization is unclear. In the present study, a full-length rat matriptase and a chimera consisting of the cytoplasmic and transmembrane regions of the protease and green fluorescent protein (designated as 1-86GFP) were found to localize exclusively to the basolateral membrane domain when expressed in Madin-Darby canine kidney epithelial cells. Mutagenesis analysis of 1-86GFP revealed that the matriptase cytoplasmic juxtamembrane amino acid residues (Lys45, Val47, and Arg50) play a role in mediating the localization in the cells. This study provides the first evidence that matriptase carries information for its localization in simple epithelia.</description><subject>Amino acids</subject><subject>Antibodies</subject><subject>Biochemistry</subject><subject>Biological and medical sciences</subject><subject>Biomedicine</subject><subject>Biotechnology</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Chimeras</subject><subject>Enterocytes</subject><subject>Epithelial cells</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Green fluorescent protein</subject><subject>Growth factors</subject><subject>JAACT Special Issue</subject><subject>Kidneys</subject><subject>Localization</subject><subject>Membranes</subject><subject>Mutagenesis</subject><subject>Peptides</subject><subject>Plasma membranes</subject><subject>Plasmids</subject><subject>Pore size</subject><subject>Proteins</subject><subject>Serine proteinase</subject><issn>0920-9069</issn><issn>1573-0778</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNp9kc1uEzEUhUcIRNPCA7ABS6jLAdsztuMNUlX-KhWxgK6tO547qYNnHGwnangqHhGniVLYsLLk-51zj-6pqheMvmGUqreJUclkTamuNaeipo-qGROqqalS88fVjJbfWlOpT6rTlJa0gIo1T6sTpoVQolGz6vfVtAl-gyNOmYSB5FskdpvDykManSXL9V2GEccuwoQk4sKFaceNkKNbZUhI3ERcTgTvrF8nt0HigwXvfkHesTnce3aQgoeMETw52vVhBHdv9wV6N9XvIXZbYmFyZfjD9RNuCa5c0XtXdBa9T8-qJwP4hM8P71l18_HD98vP9fXXT1eXF9e1FXOda2a7QVGBXHad6lrBpZC66YC3ureNUspyihpb1MD6TswbyS0ypnnD2p5x1pxV7_a-q3U3Ym_LfUp2s4puhLg1AZz5dzK5W7MIG8OVaoVsi8Hrg0EMP9eYslmGdZxKZsM1m3PJ5VwUiu0pG0NKEYfjBkbNrmSzL9mU7syuZEOL5uXf0R4Uh1YLcH4AIJUqhnJs69KR45wLSoUsHN9zqYymBcaHiP_b_movGiAYWMRifPONU9ZQJrVWkjV_AAMqzWU</recordid><startdate>20090401</startdate><enddate>20090401</enddate><creator>Murai, Nobuhito</creator><creator>Miyake, Yuka</creator><creator>Tsuzuki, Satoshi</creator><creator>Inouye, Kuniyo</creator><creator>Fushiki, Tohru</creator><general>Dordrecht : Springer Netherlands</general><general>Springer Netherlands</general><general>Springer</general><general>Springer Nature B.V</general><scope>FBQ</scope><scope>IQODW</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>8FE</scope><scope>8FH</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>LK8</scope><scope>M7P</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>5PM</scope></search><sort><creationdate>20090401</creationdate><title>Involvement of the cytoplasmic juxtamembrane region of matriptase in its exclusive localization to the basolateral membrane domain of Madin-Darby canine kidney epithelial cells</title><author>Murai, Nobuhito ; Miyake, Yuka ; Tsuzuki, Satoshi ; Inouye, Kuniyo ; Fushiki, Tohru</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c589t-1cbf705e26bb7b45265693ba249dc3777c20e9e4e9a1db58362ce1192314d1213</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Amino acids</topic><topic>Antibodies</topic><topic>Biochemistry</topic><topic>Biological and medical sciences</topic><topic>Biomedicine</topic><topic>Biotechnology</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Chimeras</topic><topic>Enterocytes</topic><topic>Epithelial cells</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Green fluorescent protein</topic><topic>Growth factors</topic><topic>JAACT Special Issue</topic><topic>Kidneys</topic><topic>Localization</topic><topic>Membranes</topic><topic>Mutagenesis</topic><topic>Peptides</topic><topic>Plasma membranes</topic><topic>Plasmids</topic><topic>Pore size</topic><topic>Proteins</topic><topic>Serine proteinase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Murai, Nobuhito</creatorcontrib><creatorcontrib>Miyake, Yuka</creatorcontrib><creatorcontrib>Tsuzuki, Satoshi</creatorcontrib><creatorcontrib>Inouye, Kuniyo</creatorcontrib><creatorcontrib>Fushiki, Tohru</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Biological Science Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Cytotechnology (Dordrecht)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Murai, Nobuhito</au><au>Miyake, Yuka</au><au>Tsuzuki, Satoshi</au><au>Inouye, Kuniyo</au><au>Fushiki, Tohru</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of the cytoplasmic juxtamembrane region of matriptase in its exclusive localization to the basolateral membrane domain of Madin-Darby canine kidney epithelial cells</atitle><jtitle>Cytotechnology (Dordrecht)</jtitle><stitle>Cytotechnology</stitle><addtitle>Cytotechnology</addtitle><date>2009-04-01</date><risdate>2009</risdate><volume>59</volume><issue>3</issue><spage>169</spage><epage>176</epage><pages>169-176</pages><issn>0920-9069</issn><eissn>1573-0778</eissn><abstract>Matriptase is a type II transmembrane serine protease. This protease is strongly expressed in simple epithelial cells such as enterocytes and kidney tubular cells in which the plasma membranes are separated into apical and basolateral domains. Although matriptase was found previously to occur exclusively on the basolateral membrane of enterocytes, the underlying mechanism of localization is unclear. In the present study, a full-length rat matriptase and a chimera consisting of the cytoplasmic and transmembrane regions of the protease and green fluorescent protein (designated as 1-86GFP) were found to localize exclusively to the basolateral membrane domain when expressed in Madin-Darby canine kidney epithelial cells. Mutagenesis analysis of 1-86GFP revealed that the matriptase cytoplasmic juxtamembrane amino acid residues (Lys45, Val47, and Arg50) play a role in mediating the localization in the cells. 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| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; ProQuest Central UK/Ireland; PubMed Central; SpringerLink Journals - AutoHoldings; ProQuest Central |
| subjects | Amino acids Antibodies Biochemistry Biological and medical sciences Biomedicine Biotechnology Chemistry Chemistry and Materials Science Chimeras Enterocytes Epithelial cells Fundamental and applied biological sciences. Psychology Green fluorescent protein Growth factors JAACT Special Issue Kidneys Localization Membranes Mutagenesis Peptides Plasma membranes Plasmids Pore size Proteins Serine proteinase |
| title | Involvement of the cytoplasmic juxtamembrane region of matriptase in its exclusive localization to the basolateral membrane domain of Madin-Darby canine kidney epithelial cells |
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