Distinct Distribution and Localization of Rho-kinase in Mouse Epithelial, Muscle and Neural Tissues
The small GTP-binding protein Rho plays a crucial role in a wide variety of cellular functions through various effector proteins. Rho-kinase is a key effector protein of Rho, which is composed of two isoforms, ROCK1 and ROCK2. To clarify the site of action of ROCK1 and ROCK2, we performed immunofluo...
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Veröffentlicht in: | Cell Structure and Function 2012, Vol.37(2), pp.155-175 |
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description | The small GTP-binding protein Rho plays a crucial role in a wide variety of cellular functions through various effector proteins. Rho-kinase is a key effector protein of Rho, which is composed of two isoforms, ROCK1 and ROCK2. To clarify the site of action of ROCK1 and ROCK2, we performed immunofluorescence and immunoelectron microscopic analyses using isoform-specific antibodies in mouse tissues. In the large and small intestines, ROCK1 immunoreactivity was predominantly identified in epithelial cells, and ROCK2 immunoreactivity was negligible. In these epithelial cells, ROCK1 immunoreactivity was distributed on plasma membranes, while ROCK1 immunogold signals were localized at cell-cell contacts and cell adhesion sites, especially at the adherens junctions at the ultrastructural level. In the bladder epithelium, however, ROCK1 and ROCK2 signals were identified at intermediate filaments, and ROCK2 signals were also observed in nuclei. In the three types of muscular cells—smooth, cardiac, and skeletal muscle cells—ROCK1 and ROCK2 also showed differential distribution. ROCK1 signals were localized at actin filaments, plasma membranes, and vesicles near plasma membranes in smooth muscle cells; at the lysosomes in skeletal muscle cells; and were undetectable in cardiac muscle cells. ROCK2 signals were localized at actin filaments and centrosomes in smooth muscle cells, at intercalated discs in cardiac muscle cells, and at Z-discs and sarcoplasmic reticulum in skeletal muscle cells. In the brain, ROCK1 immunoreactivity was distributed in glia, whereas ROCK2 immunoreactivity was observed in neurons. These results indicate that the two isoforms of Rho-kinase distribute differentially to accomplish their specific functions. |
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Rho-kinase is a key effector protein of Rho, which is composed of two isoforms, ROCK1 and ROCK2. To clarify the site of action of ROCK1 and ROCK2, we performed immunofluorescence and immunoelectron microscopic analyses using isoform-specific antibodies in mouse tissues. In the large and small intestines, ROCK1 immunoreactivity was predominantly identified in epithelial cells, and ROCK2 immunoreactivity was negligible. In these epithelial cells, ROCK1 immunoreactivity was distributed on plasma membranes, while ROCK1 immunogold signals were localized at cell-cell contacts and cell adhesion sites, especially at the adherens junctions at the ultrastructural level. In the bladder epithelium, however, ROCK1 and ROCK2 signals were identified at intermediate filaments, and ROCK2 signals were also observed in nuclei. In the three types of muscular cells—smooth, cardiac, and skeletal muscle cells—ROCK1 and ROCK2 also showed differential distribution. ROCK1 signals were localized at actin filaments, plasma membranes, and vesicles near plasma membranes in smooth muscle cells; at the lysosomes in skeletal muscle cells; and were undetectable in cardiac muscle cells. ROCK2 signals were localized at actin filaments and centrosomes in smooth muscle cells, at intercalated discs in cardiac muscle cells, and at Z-discs and sarcoplasmic reticulum in skeletal muscle cells. In the brain, ROCK1 immunoreactivity was distributed in glia, whereas ROCK2 immunoreactivity was observed in neurons. These results indicate that the two isoforms of Rho-kinase distribute differentially to accomplish their specific functions.</description><identifier>ISSN: 0386-7196</identifier><identifier>EISSN: 1347-3700</identifier><identifier>DOI: 10.1247/csf.12018</identifier><identifier>PMID: 22986902</identifier><language>eng</language><publisher>Japan: Japan Society for Cell Biology</publisher><subject>Animals ; Brain - cytology ; Brain - enzymology ; Epithelium - enzymology ; HeLa Cells ; Humans ; immunoelectron microscopy ; immunofluorescence ; Intracellular Space - enzymology ; Mice ; Mice, Inbred C57BL ; mouse tissues ; Muscles - cytology ; Muscles - enzymology ; Organ Specificity ; Protein Transport ; Rho ; rho-Associated Kinases - metabolism ; Rho-kinase</subject><ispartof>Cell Structure and Function, 2012, Vol.37(2), pp.155-175</ispartof><rights>2012 by Japan Society for Cell Biology</rights><rights>Copyright Japan Science and Technology Agency 2012</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c578t-98f63cc140b08429f55d3bc8bb649608c4bc105fc9843654fb636c811d91a7ed3</citedby><cites>FETCH-LOGICAL-c578t-98f63cc140b08429f55d3bc8bb649608c4bc105fc9843654fb636c811d91a7ed3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1883,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22986902$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Iizuka, Michiro</creatorcontrib><creatorcontrib>Kimura, Kazushi</creatorcontrib><creatorcontrib>Wang, Shujie</creatorcontrib><creatorcontrib>Kato, Katsuhiro</creatorcontrib><creatorcontrib>Amano, Mutsuki</creatorcontrib><creatorcontrib>Kaibuchi, Kozo</creatorcontrib><creatorcontrib>Mizoguchi, Akira</creatorcontrib><title>Distinct Distribution and Localization of Rho-kinase in Mouse Epithelial, Muscle and Neural Tissues</title><title>Cell Structure and Function</title><addtitle>Cell Struct. Funct.</addtitle><description>The small GTP-binding protein Rho plays a crucial role in a wide variety of cellular functions through various effector proteins. Rho-kinase is a key effector protein of Rho, which is composed of two isoforms, ROCK1 and ROCK2. To clarify the site of action of ROCK1 and ROCK2, we performed immunofluorescence and immunoelectron microscopic analyses using isoform-specific antibodies in mouse tissues. In the large and small intestines, ROCK1 immunoreactivity was predominantly identified in epithelial cells, and ROCK2 immunoreactivity was negligible. In these epithelial cells, ROCK1 immunoreactivity was distributed on plasma membranes, while ROCK1 immunogold signals were localized at cell-cell contacts and cell adhesion sites, especially at the adherens junctions at the ultrastructural level. In the bladder epithelium, however, ROCK1 and ROCK2 signals were identified at intermediate filaments, and ROCK2 signals were also observed in nuclei. In the three types of muscular cells—smooth, cardiac, and skeletal muscle cells—ROCK1 and ROCK2 also showed differential distribution. ROCK1 signals were localized at actin filaments, plasma membranes, and vesicles near plasma membranes in smooth muscle cells; at the lysosomes in skeletal muscle cells; and were undetectable in cardiac muscle cells. ROCK2 signals were localized at actin filaments and centrosomes in smooth muscle cells, at intercalated discs in cardiac muscle cells, and at Z-discs and sarcoplasmic reticulum in skeletal muscle cells. In the brain, ROCK1 immunoreactivity was distributed in glia, whereas ROCK2 immunoreactivity was observed in neurons. These results indicate that the two isoforms of Rho-kinase distribute differentially to accomplish their specific functions.</description><subject>Animals</subject><subject>Brain - cytology</subject><subject>Brain - enzymology</subject><subject>Epithelium - enzymology</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>immunoelectron microscopy</subject><subject>immunofluorescence</subject><subject>Intracellular Space - enzymology</subject><subject>Mice</subject><subject>Mice, Inbred C57BL</subject><subject>mouse tissues</subject><subject>Muscles - cytology</subject><subject>Muscles - enzymology</subject><subject>Organ Specificity</subject><subject>Protein Transport</subject><subject>Rho</subject><subject>rho-Associated Kinases - metabolism</subject><subject>Rho-kinase</subject><issn>0386-7196</issn><issn>1347-3700</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkM1O3DAUha0KVAbaRV-gitQNSIRe_9urqhp-pYFKFV1bjuN0PM0kg50s4OnxZIBKbOwj-_Px1YfQFwxnmDD53aUmB8DqA5phymRJJcAemgFVopRYiwN0mNIKgHAQ8iM6IEQroYHMkDsPaQidG4ptiKEah9B3he3qYtE724YnOx30TfF72Zf_QmeTL0JX3PZjDhebMCx9G2x7WtyOybV-enrnx2jb4j6kNPr0Ce03tk3-88t-hP5cXtzPr8vFr6ub-c9F6bhUQ6lVI6hzmEEFihHdcF7TyqmqEkwLUI5VDgNvnFaMCs6aSlDhFMa1xlb6mh6h413vJvYP-d_BrENyvm1t5_O0BhMCXAIDmdFv79BVP8YuT2cw45pLIQRk6mRHudinFH1jNjGsbXw0GMzWvMnmzWQ-s19fGsdq7es38lV1Bn7sgFUa7F__Btg4hOxtqqLSkO0yVf6_WdpofEefATMslDM</recordid><startdate>20120101</startdate><enddate>20120101</enddate><creator>Iizuka, Michiro</creator><creator>Kimura, Kazushi</creator><creator>Wang, Shujie</creator><creator>Kato, Katsuhiro</creator><creator>Amano, Mutsuki</creator><creator>Kaibuchi, Kozo</creator><creator>Mizoguchi, Akira</creator><general>Japan Society for Cell Biology</general><general>Japan Science and Technology Agency</general><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>7QP</scope><scope>7QR</scope><scope>7TK</scope><scope>8FD</scope><scope>FR3</scope><scope>K9.</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>20120101</creationdate><title>Distinct Distribution and Localization of Rho-kinase in Mouse Epithelial, Muscle and Neural Tissues</title><author>Iizuka, Michiro ; Kimura, Kazushi ; Wang, Shujie ; Kato, Katsuhiro ; Amano, Mutsuki ; Kaibuchi, Kozo ; Mizoguchi, Akira</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c578t-98f63cc140b08429f55d3bc8bb649608c4bc105fc9843654fb636c811d91a7ed3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Animals</topic><topic>Brain - cytology</topic><topic>Brain - enzymology</topic><topic>Epithelium - enzymology</topic><topic>HeLa Cells</topic><topic>Humans</topic><topic>immunoelectron microscopy</topic><topic>immunofluorescence</topic><topic>Intracellular Space - enzymology</topic><topic>Mice</topic><topic>Mice, Inbred C57BL</topic><topic>mouse tissues</topic><topic>Muscles - cytology</topic><topic>Muscles - enzymology</topic><topic>Organ Specificity</topic><topic>Protein Transport</topic><topic>Rho</topic><topic>rho-Associated Kinases - metabolism</topic><topic>Rho-kinase</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iizuka, Michiro</creatorcontrib><creatorcontrib>Kimura, Kazushi</creatorcontrib><creatorcontrib>Wang, Shujie</creatorcontrib><creatorcontrib>Kato, Katsuhiro</creatorcontrib><creatorcontrib>Amano, Mutsuki</creatorcontrib><creatorcontrib>Kaibuchi, Kozo</creatorcontrib><creatorcontrib>Mizoguchi, Akira</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Calcium & Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Cell Structure and Function</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iizuka, Michiro</au><au>Kimura, Kazushi</au><au>Wang, Shujie</au><au>Kato, Katsuhiro</au><au>Amano, Mutsuki</au><au>Kaibuchi, Kozo</au><au>Mizoguchi, Akira</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Distinct Distribution and Localization of Rho-kinase in Mouse Epithelial, Muscle and Neural Tissues</atitle><jtitle>Cell Structure and Function</jtitle><addtitle>Cell Struct. Funct.</addtitle><date>2012-01-01</date><risdate>2012</risdate><volume>37</volume><issue>2</issue><spage>155</spage><epage>175</epage><pages>155-175</pages><issn>0386-7196</issn><eissn>1347-3700</eissn><abstract>The small GTP-binding protein Rho plays a crucial role in a wide variety of cellular functions through various effector proteins. Rho-kinase is a key effector protein of Rho, which is composed of two isoforms, ROCK1 and ROCK2. To clarify the site of action of ROCK1 and ROCK2, we performed immunofluorescence and immunoelectron microscopic analyses using isoform-specific antibodies in mouse tissues. In the large and small intestines, ROCK1 immunoreactivity was predominantly identified in epithelial cells, and ROCK2 immunoreactivity was negligible. In these epithelial cells, ROCK1 immunoreactivity was distributed on plasma membranes, while ROCK1 immunogold signals were localized at cell-cell contacts and cell adhesion sites, especially at the adherens junctions at the ultrastructural level. In the bladder epithelium, however, ROCK1 and ROCK2 signals were identified at intermediate filaments, and ROCK2 signals were also observed in nuclei. In the three types of muscular cells—smooth, cardiac, and skeletal muscle cells—ROCK1 and ROCK2 also showed differential distribution. ROCK1 signals were localized at actin filaments, plasma membranes, and vesicles near plasma membranes in smooth muscle cells; at the lysosomes in skeletal muscle cells; and were undetectable in cardiac muscle cells. ROCK2 signals were localized at actin filaments and centrosomes in smooth muscle cells, at intercalated discs in cardiac muscle cells, and at Z-discs and sarcoplasmic reticulum in skeletal muscle cells. In the brain, ROCK1 immunoreactivity was distributed in glia, whereas ROCK2 immunoreactivity was observed in neurons. These results indicate that the two isoforms of Rho-kinase distribute differentially to accomplish their specific functions.</abstract><cop>Japan</cop><pub>Japan Society for Cell Biology</pub><pmid>22986902</pmid><doi>10.1247/csf.12018</doi><tpages>21</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Animals Brain - cytology Brain - enzymology Epithelium - enzymology HeLa Cells Humans immunoelectron microscopy immunofluorescence Intracellular Space - enzymology Mice Mice, Inbred C57BL mouse tissues Muscles - cytology Muscles - enzymology Organ Specificity Protein Transport Rho rho-Associated Kinases - metabolism Rho-kinase |
title | Distinct Distribution and Localization of Rho-kinase in Mouse Epithelial, Muscle and Neural Tissues |
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