Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists
A number of different protein kinases phosphorylate purified heavy chains or the 20-kDa light chain of smooth muscle myosin. The physiological significance of these phosphorylation reactions has been examined in intact smooth muscle. Myosin heavy chain was slightly phosphorylated (0.08 mol of phosph...
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| Veröffentlicht in: | The Journal of biological chemistry 1989-12, Vol.264 (35), p.21223-21229 |
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| description | A number of different protein kinases phosphorylate purified heavy chains or the 20-kDa light chain of smooth muscle myosin.
The physiological significance of these phosphorylation reactions has been examined in intact smooth muscle. Myosin heavy
chain was slightly phosphorylated (0.08 mol of phosphate/mol) under control conditions in bovine tracheal tissue. Treatment
with carbachol, isoproterenol, or phorbol 12,13-dibutyrate resulted in no significant change. In contrast, heavy chain was
phosphorylated to 0.30 mol of phosphate/mol of heavy chain in tracheal smooth muscle cells in culture. This value increased
significantly with ionomycin treatment. In control tissues, 9% of the light chain was monophosphorylated with 32P in the serine
site phosphorylated by myosin light chain kinase. Carbachol (0.1 microM) alone resulted in contraction and 42% monophosphorylated
light chain with 32P only in the serine site phosphorylated by myosin light chain kinase. Similarly, stimulation with histamine,
5-hydroxytryptamine, or KCl resulted in 32P incorporation into only the myosin light chain kinase serine site. Phorbol 12,13-dibutyrate
(1 microM) alone resulted in 22% monophosphorylated light chain. However, only 25% of the 32P was in the myosin light chain
kinase serine site, whereas 75% was in a serine site phosphorylated by protein kinase C. Phorbol 12,13-dibutyrate plus carbachol
resulted in 27% monophosphorylated light chain; 75% of the 32P was in the myosin light chain kinase serine site, with the
remainder in the protein kinase C serine site. These results indicate that phorbol esters act to increase phosphorylation
of myosin light chain by protein kinase C. However, receptor-mediated stimulation or depolarization leading to tracheal smooth
muscle contraction results in phosphorylation of myosin light chain by myosin light chain kinase alone. |
| format | Article |
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The physiological significance of these phosphorylation reactions has been examined in intact smooth muscle. Myosin heavy
chain was slightly phosphorylated (0.08 mol of phosphate/mol) under control conditions in bovine tracheal tissue. Treatment
with carbachol, isoproterenol, or phorbol 12,13-dibutyrate resulted in no significant change. In contrast, heavy chain was
phosphorylated to 0.30 mol of phosphate/mol of heavy chain in tracheal smooth muscle cells in culture. This value increased
significantly with ionomycin treatment. In control tissues, 9% of the light chain was monophosphorylated with 32P in the serine
site phosphorylated by myosin light chain kinase. Carbachol (0.1 microM) alone resulted in contraction and 42% monophosphorylated
light chain with 32P only in the serine site phosphorylated by myosin light chain kinase. Similarly, stimulation with histamine,
5-hydroxytryptamine, or KCl resulted in 32P incorporation into only the myosin light chain kinase serine site. Phorbol 12,13-dibutyrate
(1 microM) alone resulted in 22% monophosphorylated light chain. However, only 25% of the 32P was in the myosin light chain
kinase serine site, whereas 75% was in a serine site phosphorylated by protein kinase C. Phorbol 12,13-dibutyrate plus carbachol
resulted in 27% monophosphorylated light chain; 75% of the 32P was in the myosin light chain kinase serine site, with the
remainder in the protein kinase C serine site. These results indicate that phorbol esters act to increase phosphorylation
of myosin light chain by protein kinase C. However, receptor-mediated stimulation or depolarization leading to tracheal smooth
muscle contraction results in phosphorylation of myosin light chain by myosin light chain kinase alone.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>PMID: 2592371</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>Animals ; Biological and medical sciences ; Carbachol - pharmacology ; Cattle ; Cell physiology ; Cells, Cultured ; Electrophoresis, Gel, Two-Dimensional ; Fundamental and applied biological sciences. Psychology ; In Vitro Techniques ; Isoproterenol - pharmacology ; Kinetics ; Molecular and cellular biology ; Muscle contraction ; Muscle Contraction - drug effects ; Muscle, Smooth - drug effects ; Muscle, Smooth - metabolism ; Muscle, Smooth - physiology ; Myosin Subfragments - metabolism ; Peptide Mapping ; Phorbol 12,13-Dibutyrate - pharmacology ; phorbol dibutyrate ; Phosphopeptides - isolation & purification ; Phosphorylation ; smooth muscle ; trachea ; Trachea - drug effects ; Trachea - metabolism ; Trachea - physiology</subject><ispartof>The Journal of biological chemistry, 1989-12, Vol.264 (35), p.21223-21229</ispartof><rights>1990 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=6692906$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2592371$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>KAMM, K. E</creatorcontrib><creatorcontrib>LI-CHU HSU</creatorcontrib><creatorcontrib>KUBOTA, Y</creatorcontrib><creatorcontrib>STULL, J. T</creatorcontrib><title>Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>A number of different protein kinases phosphorylate purified heavy chains or the 20-kDa light chain of smooth muscle myosin.
The physiological significance of these phosphorylation reactions has been examined in intact smooth muscle. Myosin heavy
chain was slightly phosphorylated (0.08 mol of phosphate/mol) under control conditions in bovine tracheal tissue. Treatment
with carbachol, isoproterenol, or phorbol 12,13-dibutyrate resulted in no significant change. In contrast, heavy chain was
phosphorylated to 0.30 mol of phosphate/mol of heavy chain in tracheal smooth muscle cells in culture. This value increased
significantly with ionomycin treatment. In control tissues, 9% of the light chain was monophosphorylated with 32P in the serine
site phosphorylated by myosin light chain kinase. Carbachol (0.1 microM) alone resulted in contraction and 42% monophosphorylated
light chain with 32P only in the serine site phosphorylated by myosin light chain kinase. Similarly, stimulation with histamine,
5-hydroxytryptamine, or KCl resulted in 32P incorporation into only the myosin light chain kinase serine site. Phorbol 12,13-dibutyrate
(1 microM) alone resulted in 22% monophosphorylated light chain. However, only 25% of the 32P was in the myosin light chain
kinase serine site, whereas 75% was in a serine site phosphorylated by protein kinase C. Phorbol 12,13-dibutyrate plus carbachol
resulted in 27% monophosphorylated light chain; 75% of the 32P was in the myosin light chain kinase serine site, with the
remainder in the protein kinase C serine site. These results indicate that phorbol esters act to increase phosphorylation
of myosin light chain by protein kinase C. However, receptor-mediated stimulation or depolarization leading to tracheal smooth
muscle contraction results in phosphorylation of myosin light chain by myosin light chain kinase alone.</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Carbachol - pharmacology</subject><subject>Cattle</subject><subject>Cell physiology</subject><subject>Cells, Cultured</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>In Vitro Techniques</subject><subject>Isoproterenol - pharmacology</subject><subject>Kinetics</subject><subject>Molecular and cellular biology</subject><subject>Muscle contraction</subject><subject>Muscle Contraction - drug effects</subject><subject>Muscle, Smooth - drug effects</subject><subject>Muscle, Smooth - metabolism</subject><subject>Muscle, Smooth - physiology</subject><subject>Myosin Subfragments - metabolism</subject><subject>Peptide Mapping</subject><subject>Phorbol 12,13-Dibutyrate - pharmacology</subject><subject>phorbol dibutyrate</subject><subject>Phosphopeptides - isolation & purification</subject><subject>Phosphorylation</subject><subject>smooth muscle</subject><subject>trachea</subject><subject>Trachea - drug effects</subject><subject>Trachea - metabolism</subject><subject>Trachea - physiology</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkM1KxDAAhIMo67r6CEIO4q3SJE3aHGVZf0DQg4K3kKbJJkvarE2q9O3tatG5zGG-mcMcgSXKK5IRit6PwTLPMco4ptUpOItxl08qOFqABaYckxItwe7Fhri3oR-9TC50MBgY2xCShe0QldewHUN0HbRafo5Qdg30bmsTVFa6Lt7AjTFapXjoHWbq4GHj6iGNvUz6h5fb0LmY4jk4MdJHfTH7CrzdbV7XD9nT8_3j-vYps5jTlCktZc3KnHCmuJJlhTmiShtUc0qLyjBcVUjnBMmSc1M2nGlqsEK1KuvJG7IC17-7-z58DDom0bqotPey02GIAtGCkoKVE3g5g0Pd6kbse9fKfhTzOVN-NecyKulNLzvl4h_GGMc8Z_-YnY75cr0WtQvK6lZgVghCBUYYE_INiWt74w</recordid><startdate>19891215</startdate><enddate>19891215</enddate><creator>KAMM, K. E</creator><creator>LI-CHU HSU</creator><creator>KUBOTA, Y</creator><creator>STULL, J. T</creator><general>American Society for Biochemistry and Molecular Biology</general><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></search><sort><creationdate>19891215</creationdate><title>Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists</title><author>KAMM, K. E ; LI-CHU HSU ; KUBOTA, Y ; STULL, J. T</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h295t-ceaab670396c9ca782915cef1b95548f62881e031a799f7d96e5f2c1bc7bf2cd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Carbachol - pharmacology</topic><topic>Cattle</topic><topic>Cell physiology</topic><topic>Cells, Cultured</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>In Vitro Techniques</topic><topic>Isoproterenol - pharmacology</topic><topic>Kinetics</topic><topic>Molecular and cellular biology</topic><topic>Muscle contraction</topic><topic>Muscle Contraction - drug effects</topic><topic>Muscle, Smooth - drug effects</topic><topic>Muscle, Smooth - metabolism</topic><topic>Muscle, Smooth - physiology</topic><topic>Myosin Subfragments - metabolism</topic><topic>Peptide Mapping</topic><topic>Phorbol 12,13-Dibutyrate - pharmacology</topic><topic>phorbol dibutyrate</topic><topic>Phosphopeptides - isolation & purification</topic><topic>Phosphorylation</topic><topic>smooth muscle</topic><topic>trachea</topic><topic>Trachea - drug effects</topic><topic>Trachea - metabolism</topic><topic>Trachea - physiology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>KAMM, K. E</creatorcontrib><creatorcontrib>LI-CHU HSU</creatorcontrib><creatorcontrib>KUBOTA, Y</creatorcontrib><creatorcontrib>STULL, J. 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>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><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>KAMM, K. E</au><au>LI-CHU HSU</au><au>KUBOTA, Y</au><au>STULL, J. T</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1989-12-15</date><risdate>1989</risdate><volume>264</volume><issue>35</issue><spage>21223</spage><epage>21229</epage><pages>21223-21229</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>A number of different protein kinases phosphorylate purified heavy chains or the 20-kDa light chain of smooth muscle myosin.
The physiological significance of these phosphorylation reactions has been examined in intact smooth muscle. Myosin heavy
chain was slightly phosphorylated (0.08 mol of phosphate/mol) under control conditions in bovine tracheal tissue. Treatment
with carbachol, isoproterenol, or phorbol 12,13-dibutyrate resulted in no significant change. In contrast, heavy chain was
phosphorylated to 0.30 mol of phosphate/mol of heavy chain in tracheal smooth muscle cells in culture. This value increased
significantly with ionomycin treatment. In control tissues, 9% of the light chain was monophosphorylated with 32P in the serine
site phosphorylated by myosin light chain kinase. Carbachol (0.1 microM) alone resulted in contraction and 42% monophosphorylated
light chain with 32P only in the serine site phosphorylated by myosin light chain kinase. Similarly, stimulation with histamine,
5-hydroxytryptamine, or KCl resulted in 32P incorporation into only the myosin light chain kinase serine site. Phorbol 12,13-dibutyrate
(1 microM) alone resulted in 22% monophosphorylated light chain. However, only 25% of the 32P was in the myosin light chain
kinase serine site, whereas 75% was in a serine site phosphorylated by protein kinase C. Phorbol 12,13-dibutyrate plus carbachol
resulted in 27% monophosphorylated light chain; 75% of the 32P was in the myosin light chain kinase serine site, with the
remainder in the protein kinase C serine site. These results indicate that phorbol esters act to increase phosphorylation
of myosin light chain by protein kinase C. However, receptor-mediated stimulation or depolarization leading to tracheal smooth
muscle contraction results in phosphorylation of myosin light chain by myosin light chain kinase alone.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>2592371</pmid><tpages>7</tpages></addata></record> |
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| identifier | ISSN: 0021-9258 |
| ispartof | The Journal of biological chemistry, 1989-12, Vol.264 (35), p.21223-21229 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_proquest_miscellaneous_15453467 |
| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | Animals Biological and medical sciences Carbachol - pharmacology Cattle Cell physiology Cells, Cultured Electrophoresis, Gel, Two-Dimensional Fundamental and applied biological sciences. Psychology In Vitro Techniques Isoproterenol - pharmacology Kinetics Molecular and cellular biology Muscle contraction Muscle Contraction - drug effects Muscle, Smooth - drug effects Muscle, Smooth - metabolism Muscle, Smooth - physiology Myosin Subfragments - metabolism Peptide Mapping Phorbol 12,13-Dibutyrate - pharmacology phorbol dibutyrate Phosphopeptides - isolation & purification Phosphorylation smooth muscle trachea Trachea - drug effects Trachea - metabolism Trachea - physiology |
| title | Phosphorylation of smooth muscle myosin heavy and light chains. Effects of phorbol dibutyrate and agonists |
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