Monoclonal Antibody Assessment of Tissue- and Species-Specific Myosin Light Chain Kinase Isozymes
Monoclonal antibodies raised against chicken gizzard smooth muscle myosin light chain kinase were used for immunological and structural studies of this enzyme. Epitope mapping of trypsin-digested chicken gizzard enzyme showed that MM-1, 2, 3, 4, 5, 6, and 7 bind to 65 kDa (trypsin-digested) and 60 k...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1989, Vol.106 (1), p.71-75 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Hagiwara, Masatoshi Tokumitsu, Hiroshi Onoda, Koji Tanaka, Toshio Ito, Masaaki Kato, Nobuo Hidaka, Hiroyoshi |
| description | Monoclonal antibodies raised against chicken gizzard smooth muscle myosin light chain kinase were used for immunological and structural studies of this enzyme. Epitope mapping of trypsin-digested chicken gizzard enzyme showed that MM-1, 2, 3, 4, 5, 6, and 7 bind to 65 kDa (trypsin-digested) and 60 kDa (chymotrypsin-digested) fragments which contain the catalytic domain of the kinase. Kinetic analysis demonstrated that MM-7 inhibited kinase activity competitively with respect to ATP and noncompetitively with respect to myosin light chain, thereby indicating that MM-7 binds at or near the ATP binding site of the enzyme. Immunoblot analysis revealed that all these antibodies (MM-1 to 12) reacted with the enzyme (130 kDa) from intestinal and vascular smooth muscles, whereas 5 (MM-1, 3, 4, 6, and 9) or 3 (MM-1, 3, and 4) of 12 antibodies did not cross-react with chicken cardiac muscle or with blood platelet myosin light chain kinase (130 kDa), respectively. None of these antibodies showed cross-reactivity against skeletal muscle myosin light chain kinase. As for mammalian species, MM-11 and 12 reacted with myosin light chain kinase of vascular smooth muscle (140 kDa) and MM-11 cross-reacted with the enzyme (140 kDa) from cardiac muscle of rat and rabbit. These data suggest the existence of at least 4 subspecies of myosin light chain kinase in chicken tissues and the heterogeneity of tissue- and species-specific isozyme forms. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a122822 |
| format | Article |
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Epitope mapping of trypsin-digested chicken gizzard enzyme showed that MM-1, 2, 3, 4, 5, 6, and 7 bind to 65 kDa (trypsin-digested) and 60 kDa (chymotrypsin-digested) fragments which contain the catalytic domain of the kinase. Kinetic analysis demonstrated that MM-7 inhibited kinase activity competitively with respect to ATP and noncompetitively with respect to myosin light chain, thereby indicating that MM-7 binds at or near the ATP binding site of the enzyme. Immunoblot analysis revealed that all these antibodies (MM-1 to 12) reacted with the enzyme (130 kDa) from intestinal and vascular smooth muscles, whereas 5 (MM-1, 3, 4, 6, and 9) or 3 (MM-1, 3, and 4) of 12 antibodies did not cross-react with chicken cardiac muscle or with blood platelet myosin light chain kinase (130 kDa), respectively. None of these antibodies showed cross-reactivity against skeletal muscle myosin light chain kinase. As for mammalian species, MM-11 and 12 reacted with myosin light chain kinase of vascular smooth muscle (140 kDa) and MM-11 cross-reacted with the enzyme (140 kDa) from cardiac muscle of rat and rabbit. These data suggest the existence of at least 4 subspecies of myosin light chain kinase in chicken tissues and the heterogeneity of tissue- and species-specific isozyme forms.</description><identifier>ISSN: 0021-924X</identifier><identifier>EISSN: 1756-2651</identifier><identifier>DOI: 10.1093/oxfordjournals.jbchem.a122822</identifier><identifier>PMID: 2476431</identifier><identifier>CODEN: JOBIAO</identifier><language>eng</language><publisher>Oxford: Oxford University Press</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Antibodies, Monoclonal ; Biological and medical sciences ; Chickens ; Enzymes and enzyme inhibitors ; Epitopes - analysis ; Fundamental and applied biological sciences. Psychology ; Gizzard, Avian - enzymology ; Immunoblotting ; Isoenzymes - analysis ; Isoenzymes - immunology ; Kinetics ; Muscle, Smooth - enzymology ; Myosin-Light-Chain Kinase - analysis ; Myosin-Light-Chain Kinase - immunology ; Species Specificity ; Tissue Distribution ; Transferases</subject><ispartof>Journal of biochemistry (Tokyo), 1989, Vol.106 (1), p.71-75</ispartof><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,4010,27900,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19292342$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2476431$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hagiwara, Masatoshi</creatorcontrib><creatorcontrib>Tokumitsu, Hiroshi</creatorcontrib><creatorcontrib>Onoda, Koji</creatorcontrib><creatorcontrib>Tanaka, Toshio</creatorcontrib><creatorcontrib>Ito, Masaaki</creatorcontrib><creatorcontrib>Kato, Nobuo</creatorcontrib><creatorcontrib>Hidaka, Hiroyoshi</creatorcontrib><title>Monoclonal Antibody Assessment of Tissue- and Species-Specific Myosin Light Chain Kinase Isozymes</title><title>Journal of biochemistry (Tokyo)</title><addtitle>J Biochem</addtitle><description>Monoclonal antibodies raised against chicken gizzard smooth muscle myosin light chain kinase were used for immunological and structural studies of this enzyme. Epitope mapping of trypsin-digested chicken gizzard enzyme showed that MM-1, 2, 3, 4, 5, 6, and 7 bind to 65 kDa (trypsin-digested) and 60 kDa (chymotrypsin-digested) fragments which contain the catalytic domain of the kinase. Kinetic analysis demonstrated that MM-7 inhibited kinase activity competitively with respect to ATP and noncompetitively with respect to myosin light chain, thereby indicating that MM-7 binds at or near the ATP binding site of the enzyme. Immunoblot analysis revealed that all these antibodies (MM-1 to 12) reacted with the enzyme (130 kDa) from intestinal and vascular smooth muscles, whereas 5 (MM-1, 3, 4, 6, and 9) or 3 (MM-1, 3, and 4) of 12 antibodies did not cross-react with chicken cardiac muscle or with blood platelet myosin light chain kinase (130 kDa), respectively. None of these antibodies showed cross-reactivity against skeletal muscle myosin light chain kinase. As for mammalian species, MM-11 and 12 reacted with myosin light chain kinase of vascular smooth muscle (140 kDa) and MM-11 cross-reacted with the enzyme (140 kDa) from cardiac muscle of rat and rabbit. These data suggest the existence of at least 4 subspecies of myosin light chain kinase in chicken tissues and the heterogeneity of tissue- and species-specific isozyme forms.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Biological and medical sciences</subject><subject>Chickens</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Epitopes - analysis</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Gizzard, Avian - enzymology</subject><subject>Immunoblotting</subject><subject>Isoenzymes - analysis</subject><subject>Isoenzymes - immunology</subject><subject>Kinetics</subject><subject>Muscle, Smooth - enzymology</subject><subject>Myosin-Light-Chain Kinase - analysis</subject><subject>Myosin-Light-Chain Kinase - immunology</subject><subject>Species Specificity</subject><subject>Tissue Distribution</subject><subject>Transferases</subject><issn>0021-924X</issn><issn>1756-2651</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE9r3DAQxUVJSbdpP0JAl-TmjTX6Y-u4LM0mZEMLTSH0YiRbymprS1uPDbv59HGTJdee3gzvx2PeEHLB8jnLNb9Ke5_6ZpvGPpoW51tbb1w3NwygBPhAZqyQKgMl2QmZ5TmwTIN4_EQ-I27_rcD5KTkFUSjB2YyY-xRT3aYpiy7iEGxqDnSB6BA7FweaPH0IiKPLqIkN_blzdXCYvaoPNb0_JAyRrsPTZqDLjZnmuxANOnqL6fnQOfxCPvrpUPf1qGfk1_W3h-VNtv6-ul0u1lkAzYfMa24EM7axwL20oIwqhBSO54zl1pdca62kUIXihay5ZIwpDdZyD0rJUvAzcvmWu-vT39HhUHUBa9e2Jro0YlVoVmqRq_-CTHLgWsgJPD-Co-1cU-360Jn-UB2fN_kXR99gbVrfm1gHfMeYBg1cwMRlb1zAwe3ffdP_qVQxtaluHn9XdyWsV-WPVbXiL5w7kno</recordid><startdate>1989</startdate><enddate>1989</enddate><creator>Hagiwara, Masatoshi</creator><creator>Tokumitsu, Hiroshi</creator><creator>Onoda, Koji</creator><creator>Tanaka, Toshio</creator><creator>Ito, Masaaki</creator><creator>Kato, Nobuo</creator><creator>Hidaka, Hiroyoshi</creator><general>Oxford University Press</general><scope>BSCLL</scope><scope>IQODW</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7QL</scope><scope>8FD</scope><scope>C1K</scope><scope>FR3</scope><scope>M81</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>1989</creationdate><title>Monoclonal Antibody Assessment of Tissue- and Species-Specific Myosin Light Chain Kinase Isozymes</title><author>Hagiwara, Masatoshi ; Tokumitsu, Hiroshi ; Onoda, Koji ; Tanaka, Toshio ; Ito, Masaaki ; Kato, Nobuo ; Hidaka, Hiroyoshi</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-i293t-f93a41abdb23f5b26a67454e30110bf83999654676375c35111692bb3f2665843</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Biological and medical sciences</topic><topic>Chickens</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Epitopes - analysis</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Gizzard, Avian - enzymology</topic><topic>Immunoblotting</topic><topic>Isoenzymes - analysis</topic><topic>Isoenzymes - immunology</topic><topic>Kinetics</topic><topic>Muscle, Smooth - enzymology</topic><topic>Myosin-Light-Chain Kinase - analysis</topic><topic>Myosin-Light-Chain Kinase - immunology</topic><topic>Species Specificity</topic><topic>Tissue Distribution</topic><topic>Transferases</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hagiwara, Masatoshi</creatorcontrib><creatorcontrib>Tokumitsu, Hiroshi</creatorcontrib><creatorcontrib>Onoda, Koji</creatorcontrib><creatorcontrib>Tanaka, Toshio</creatorcontrib><creatorcontrib>Ito, Masaaki</creatorcontrib><creatorcontrib>Kato, Nobuo</creatorcontrib><creatorcontrib>Hidaka, Hiroyoshi</creatorcontrib><collection>Istex</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Technology Research Database</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 3</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hagiwara, Masatoshi</au><au>Tokumitsu, Hiroshi</au><au>Onoda, Koji</au><au>Tanaka, Toshio</au><au>Ito, Masaaki</au><au>Kato, Nobuo</au><au>Hidaka, Hiroyoshi</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Monoclonal Antibody Assessment of Tissue- and Species-Specific Myosin Light Chain Kinase Isozymes</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1989</date><risdate>1989</risdate><volume>106</volume><issue>1</issue><spage>71</spage><epage>75</epage><pages>71-75</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><coden>JOBIAO</coden><abstract>Monoclonal antibodies raised against chicken gizzard smooth muscle myosin light chain kinase were used for immunological and structural studies of this enzyme. Epitope mapping of trypsin-digested chicken gizzard enzyme showed that MM-1, 2, 3, 4, 5, 6, and 7 bind to 65 kDa (trypsin-digested) and 60 kDa (chymotrypsin-digested) fragments which contain the catalytic domain of the kinase. Kinetic analysis demonstrated that MM-7 inhibited kinase activity competitively with respect to ATP and noncompetitively with respect to myosin light chain, thereby indicating that MM-7 binds at or near the ATP binding site of the enzyme. Immunoblot analysis revealed that all these antibodies (MM-1 to 12) reacted with the enzyme (130 kDa) from intestinal and vascular smooth muscles, whereas 5 (MM-1, 3, 4, 6, and 9) or 3 (MM-1, 3, and 4) of 12 antibodies did not cross-react with chicken cardiac muscle or with blood platelet myosin light chain kinase (130 kDa), respectively. None of these antibodies showed cross-reactivity against skeletal muscle myosin light chain kinase. As for mammalian species, MM-11 and 12 reacted with myosin light chain kinase of vascular smooth muscle (140 kDa) and MM-11 cross-reacted with the enzyme (140 kDa) from cardiac muscle of rat and rabbit. These data suggest the existence of at least 4 subspecies of myosin light chain kinase in chicken tissues and the heterogeneity of tissue- and species-specific isozyme forms.</abstract><cop>Oxford</cop><pub>Oxford University Press</pub><pmid>2476431</pmid><doi>10.1093/oxfordjournals.jbchem.a122822</doi><tpages>5</tpages></addata></record> |
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| source | Oxford University Press Journals Digital Archive legacy; MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; Free Full-Text Journals in Chemistry |
| subjects | Analytical, structural and metabolic biochemistry Animals Antibodies, Monoclonal Biological and medical sciences Chickens Enzymes and enzyme inhibitors Epitopes - analysis Fundamental and applied biological sciences. Psychology Gizzard, Avian - enzymology Immunoblotting Isoenzymes - analysis Isoenzymes - immunology Kinetics Muscle, Smooth - enzymology Myosin-Light-Chain Kinase - analysis Myosin-Light-Chain Kinase - immunology Species Specificity Tissue Distribution Transferases |
| title | Monoclonal Antibody Assessment of Tissue- and Species-Specific Myosin Light Chain Kinase Isozymes |
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