Involvement of Phosphorylation of Myosin Phosphatase by ROCK in Trabecular Meshwork and Ciliary Muscle Contraction
The control of smooth muscle contraction is an important factor in maintaining normal intraoculer pressure. However, the specific factors causing changes in control by phosphorylation/dephosphorylation schemes in the eye are not well-defined. The purposes of this experiment were to (i) determine the...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2001-10, Vol.288 (2), p.296-300 |
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| creator | Fukiage, Chiho Mizutani, Kanako Kawamoto, Yoko Azuma, Mitsuyoshi Shearer, Thomas R. |
| description | The control of smooth muscle contraction is an important factor in maintaining normal intraoculer pressure. However, the specific factors causing changes in control by phosphorylation/dephosphorylation schemes in the eye are not well-defined. The purposes of this experiment were to (i) determine the localization of ROCK (Rho-associated, coiled coil-forming kinase) in monkey and rabbit eye tissues and (ii) measure phosphorylation of ROCK substrate during trabecular meshwork or ciliary muscle contraction induced by carbachol. We found that mRNAs for both ROCK I and II were expressed in most eye tissues from rabbit and monkey. Proteins for ROCK I and II were present in all eye tissues studied except lens. When trabecular meshwork or ciliary muscle were incubated with carbachol to induce contraction, phosphorylation of the myosin-binding subunit (MBS) of myosin phosphatase, a substrate for ROCK, started within 1 min and continued for at least 1 h. This phosphorylation was well correlated with contraction of trabecular meshwork or ciliary muscle. These results suggested that ROCK might regulate contraction of trabecular meshwork or ciliary muscle through phosphorylation of MBS of myosin phosphatase. |
| doi_str_mv | 10.1006/bbrc.2001.5751 |
| format | Article |
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However, the specific factors causing changes in control by phosphorylation/dephosphorylation schemes in the eye are not well-defined. The purposes of this experiment were to (i) determine the localization of ROCK (Rho-associated, coiled coil-forming kinase) in monkey and rabbit eye tissues and (ii) measure phosphorylation of ROCK substrate during trabecular meshwork or ciliary muscle contraction induced by carbachol. We found that mRNAs for both ROCK I and II were expressed in most eye tissues from rabbit and monkey. Proteins for ROCK I and II were present in all eye tissues studied except lens. When trabecular meshwork or ciliary muscle were incubated with carbachol to induce contraction, phosphorylation of the myosin-binding subunit (MBS) of myosin phosphatase, a substrate for ROCK, started within 1 min and continued for at least 1 h. This phosphorylation was well correlated with contraction of trabecular meshwork or ciliary muscle. These results suggested that ROCK might regulate contraction of trabecular meshwork or ciliary muscle through phosphorylation of MBS of myosin phosphatase.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1006/bbrc.2001.5751</identifier><identifier>PMID: 11606042</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Animals ; ciliary muscle contraction, trabecular meshwork contraction ; Intracellular Signaling Peptides and Proteins ; Macaca fascicularis ; Male ; Muscle Contraction - physiology ; Muscle, Smooth - physiology ; myosin phosphatase ; Myosin-Light-Chain Phosphatase ; Phosphoprotein Phosphatases - metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases - genetics ; Protein-Serine-Threonine Kinases - metabolism ; Rabbits ; rho-Associated Kinases ; Rho-associated protein kinase ; RNA, Messenger - metabolism ; Spasm - enzymology ; Spasm - metabolism ; Trabecular Meshwork - enzymology ; Trabecular Meshwork - metabolism</subject><ispartof>Biochemical and biophysical research communications, 2001-10, Vol.288 (2), p.296-300</ispartof><rights>2001 Academic Press</rights><rights>Copyright 2001 Academic Press.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c406t-9c8a0403d6845d422a1d58d364219cf9b8925e78112b8815c6bda3c697ecad0b3</citedby><cites>FETCH-LOGICAL-c406t-9c8a0403d6845d422a1d58d364219cf9b8925e78112b8815c6bda3c697ecad0b3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1006/bbrc.2001.5751$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3548,27923,27924,45994</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11606042$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Fukiage, Chiho</creatorcontrib><creatorcontrib>Mizutani, Kanako</creatorcontrib><creatorcontrib>Kawamoto, Yoko</creatorcontrib><creatorcontrib>Azuma, Mitsuyoshi</creatorcontrib><creatorcontrib>Shearer, Thomas R.</creatorcontrib><title>Involvement of Phosphorylation of Myosin Phosphatase by ROCK in Trabecular Meshwork and Ciliary Muscle Contraction</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The control of smooth muscle contraction is an important factor in maintaining normal intraoculer pressure. However, the specific factors causing changes in control by phosphorylation/dephosphorylation schemes in the eye are not well-defined. The purposes of this experiment were to (i) determine the localization of ROCK (Rho-associated, coiled coil-forming kinase) in monkey and rabbit eye tissues and (ii) measure phosphorylation of ROCK substrate during trabecular meshwork or ciliary muscle contraction induced by carbachol. We found that mRNAs for both ROCK I and II were expressed in most eye tissues from rabbit and monkey. Proteins for ROCK I and II were present in all eye tissues studied except lens. When trabecular meshwork or ciliary muscle were incubated with carbachol to induce contraction, phosphorylation of the myosin-binding subunit (MBS) of myosin phosphatase, a substrate for ROCK, started within 1 min and continued for at least 1 h. This phosphorylation was well correlated with contraction of trabecular meshwork or ciliary muscle. These results suggested that ROCK might regulate contraction of trabecular meshwork or ciliary muscle through phosphorylation of MBS of myosin phosphatase.</description><subject>Animals</subject><subject>ciliary muscle contraction, trabecular meshwork contraction</subject><subject>Intracellular Signaling Peptides and Proteins</subject><subject>Macaca fascicularis</subject><subject>Male</subject><subject>Muscle Contraction - physiology</subject><subject>Muscle, Smooth - physiology</subject><subject>myosin phosphatase</subject><subject>Myosin-Light-Chain Phosphatase</subject><subject>Phosphoprotein Phosphatases - metabolism</subject><subject>Phosphorylation</subject><subject>Protein-Serine-Threonine Kinases - genetics</subject><subject>Protein-Serine-Threonine Kinases - metabolism</subject><subject>Rabbits</subject><subject>rho-Associated Kinases</subject><subject>Rho-associated protein kinase</subject><subject>RNA, Messenger - metabolism</subject><subject>Spasm - enzymology</subject><subject>Spasm - metabolism</subject><subject>Trabecular Meshwork - enzymology</subject><subject>Trabecular Meshwork - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2001</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kE1rGzEQhkVJiN0k1x6LTrmtO5K12tWxLGkaGpNQXMhN6GOM1a5XjrTr4n-fXWzoqaeBmWdeZh5CPjFYMAD5xdrkFhyALcqqZB_InIGCgjMQF2QOI1FwxV5n5GPOv0eKCamuyIwxCRIEn5P02B1ie8Addj2NG_qyjXm_jenYmj7EbmqtjjGH7jwxvclI7ZH-fG5-0LG9TsaiG1qT6Arz9m9Mf6jpPG1CG0w60tWQXYu0iV2fjJsyb8jlxrQZb8_1mvz6dr9uvhdPzw-PzdenwgmQfaFcbUDA0stalF5wbpgva7-UgjPlNsrWipdY1YxxW9esdNJ6s3RSVeiMB7u8Jnen3H2KbwPmXu9Cdti2psM4ZF1xDqoqxQguTqBLMeeEG71PYTcerxnoybKeLOvJsp4sjwufz8mD3aH_h5-1jkB9AnD87xAw6ewCdg59SOh67WP4X_Y7CkuMlQ</recordid><startdate>20011026</startdate><enddate>20011026</enddate><creator>Fukiage, Chiho</creator><creator>Mizutani, Kanako</creator><creator>Kawamoto, Yoko</creator><creator>Azuma, Mitsuyoshi</creator><creator>Shearer, Thomas R.</creator><general>Elsevier Inc</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>7X8</scope></search><sort><creationdate>20011026</creationdate><title>Involvement of Phosphorylation of Myosin Phosphatase by ROCK in Trabecular Meshwork and Ciliary Muscle Contraction</title><author>Fukiage, Chiho ; Mizutani, Kanako ; Kawamoto, Yoko ; Azuma, Mitsuyoshi ; Shearer, Thomas R.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c406t-9c8a0403d6845d422a1d58d364219cf9b8925e78112b8815c6bda3c697ecad0b3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Animals</topic><topic>ciliary muscle contraction, trabecular meshwork contraction</topic><topic>Intracellular Signaling Peptides and Proteins</topic><topic>Macaca fascicularis</topic><topic>Male</topic><topic>Muscle Contraction - physiology</topic><topic>Muscle, Smooth - physiology</topic><topic>myosin phosphatase</topic><topic>Myosin-Light-Chain Phosphatase</topic><topic>Phosphoprotein Phosphatases - metabolism</topic><topic>Phosphorylation</topic><topic>Protein-Serine-Threonine Kinases - genetics</topic><topic>Protein-Serine-Threonine Kinases - metabolism</topic><topic>Rabbits</topic><topic>rho-Associated Kinases</topic><topic>Rho-associated protein kinase</topic><topic>RNA, Messenger - metabolism</topic><topic>Spasm - enzymology</topic><topic>Spasm - metabolism</topic><topic>Trabecular Meshwork - enzymology</topic><topic>Trabecular Meshwork - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Fukiage, Chiho</creatorcontrib><creatorcontrib>Mizutani, Kanako</creatorcontrib><creatorcontrib>Kawamoto, Yoko</creatorcontrib><creatorcontrib>Azuma, Mitsuyoshi</creatorcontrib><creatorcontrib>Shearer, Thomas R.</creatorcontrib><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><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Fukiage, Chiho</au><au>Mizutani, Kanako</au><au>Kawamoto, Yoko</au><au>Azuma, Mitsuyoshi</au><au>Shearer, Thomas R.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Involvement of Phosphorylation of Myosin Phosphatase by ROCK in Trabecular Meshwork and Ciliary Muscle Contraction</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2001-10-26</date><risdate>2001</risdate><volume>288</volume><issue>2</issue><spage>296</spage><epage>300</epage><pages>296-300</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The control of smooth muscle contraction is an important factor in maintaining normal intraoculer pressure. However, the specific factors causing changes in control by phosphorylation/dephosphorylation schemes in the eye are not well-defined. The purposes of this experiment were to (i) determine the localization of ROCK (Rho-associated, coiled coil-forming kinase) in monkey and rabbit eye tissues and (ii) measure phosphorylation of ROCK substrate during trabecular meshwork or ciliary muscle contraction induced by carbachol. We found that mRNAs for both ROCK I and II were expressed in most eye tissues from rabbit and monkey. Proteins for ROCK I and II were present in all eye tissues studied except lens. When trabecular meshwork or ciliary muscle were incubated with carbachol to induce contraction, phosphorylation of the myosin-binding subunit (MBS) of myosin phosphatase, a substrate for ROCK, started within 1 min and continued for at least 1 h. This phosphorylation was well correlated with contraction of trabecular meshwork or ciliary muscle. These results suggested that ROCK might regulate contraction of trabecular meshwork or ciliary muscle through phosphorylation of MBS of myosin phosphatase.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>11606042</pmid><doi>10.1006/bbrc.2001.5751</doi><tpages>5</tpages></addata></record> |
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| subjects | Animals ciliary muscle contraction, trabecular meshwork contraction Intracellular Signaling Peptides and Proteins Macaca fascicularis Male Muscle Contraction - physiology Muscle, Smooth - physiology myosin phosphatase Myosin-Light-Chain Phosphatase Phosphoprotein Phosphatases - metabolism Phosphorylation Protein-Serine-Threonine Kinases - genetics Protein-Serine-Threonine Kinases - metabolism Rabbits rho-Associated Kinases Rho-associated protein kinase RNA, Messenger - metabolism Spasm - enzymology Spasm - metabolism Trabecular Meshwork - enzymology Trabecular Meshwork - metabolism |
| title | Involvement of Phosphorylation of Myosin Phosphatase by ROCK in Trabecular Meshwork and Ciliary Muscle Contraction |
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