Ca2+-independent myosin II phosphorylation and contraction in chicken embryo fibroblasts
Non-muscle contraction is widely believed to be mediated through Ca 2+ -stimulated myosin II regulatory light chain (LC20) phosphorylation, similar to the contractile regulation of smooth muscle. However, this hypothesis lacks conclusive experimental support. By modulating chicken embryo fibroblast...
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| Veröffentlicht in: | The Journal of physiology 1999-02, Vol.515 (1), p.87-92 |
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| creator | Michael S Kolodney Matthew S Thimgan Henry M Honda George Tsai Hal F Yee, Jr |
| description | Non-muscle contraction is widely believed to be mediated through Ca 2+ -stimulated myosin II regulatory light chain (LC20) phosphorylation, similar to the contractile regulation of smooth muscle.
However, this hypothesis lacks conclusive experimental support.
By modulating chicken embryo fibroblast cytosolic Ca 2+ concentration ([Ca 2+ ] i ), we investigated the putative role of [Ca 2+ ] i in fetal bovine serum (FBS)-stimulated LC20 phosphorylation and force development in these cells.
Eliminating the FBS-stimulated rise in [Ca 2+ ] i with the Ca 2+ chelator BAPTA only partially inhibited FBS-stimulated LC20 phosphorylation and did not significantly alter the magnitude
of FBS-stimulated isometric contraction.
Ionomycin (1 μ m ) produced a larger but shorter lasting rise in [Ca 2+ ] i relative to FBS. However, ionomycin only stimulated a small and transient increase in LC20 phosphorylation and did not cause
contraction.
We conclude that fibroblasts differ from smooth muscle in that LC20 phosphorylation and contraction are predominantly regulated
independently of [Ca 2+ ] i . |
| doi_str_mv | 10.1111/j.1469-7793.1999.087ad.x |
| format | Article |
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However, this hypothesis lacks conclusive experimental support.
By modulating chicken embryo fibroblast cytosolic Ca 2+ concentration ([Ca 2+ ] i ), we investigated the putative role of [Ca 2+ ] i in fetal bovine serum (FBS)-stimulated LC20 phosphorylation and force development in these cells.
Eliminating the FBS-stimulated rise in [Ca 2+ ] i with the Ca 2+ chelator BAPTA only partially inhibited FBS-stimulated LC20 phosphorylation and did not significantly alter the magnitude
of FBS-stimulated isometric contraction.
Ionomycin (1 μ m ) produced a larger but shorter lasting rise in [Ca 2+ ] i relative to FBS. However, ionomycin only stimulated a small and transient increase in LC20 phosphorylation and did not cause
contraction.
We conclude that fibroblasts differ from smooth muscle in that LC20 phosphorylation and contraction are predominantly regulated
independently of [Ca 2+ ] i .</description><identifier>ISSN: 0022-3751</identifier><identifier>EISSN: 1469-7793</identifier><identifier>DOI: 10.1111/j.1469-7793.1999.087ad.x</identifier><identifier>PMID: 9925880</identifier><language>eng</language><publisher>Oxford, UK: The Physiological Society</publisher><subject>Animals ; Calcium - physiology ; Chelating Agents - pharmacology ; Chick Embryo ; Cytosol - metabolism ; Cytosol - physiology ; Egtazic Acid - analogs & derivatives ; Egtazic Acid - pharmacology ; Fibroblasts ; Ionomycin - pharmacology ; Ionophores - pharmacology ; Isometric Contraction - drug effects ; Isometric Contraction - physiology ; Myosin Light Chains - metabolism ; Myosin Light Chains - physiology ; Myosins - metabolism ; Phosphorylation ; Rapid Report</subject><ispartof>The Journal of physiology, 1999-02, Vol.515 (1), p.87-92</ispartof><rights>1999 The Journal of Physiology © 1999 The Physiological Society</rights><rights>The Physiological Society 1999 1999</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2269119/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2269119/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,727,780,784,885,1417,1433,27924,27925,45574,45575,46409,46833,53791,53793</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/9925880$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Michael S Kolodney</creatorcontrib><creatorcontrib>Matthew S Thimgan</creatorcontrib><creatorcontrib>Henry M Honda</creatorcontrib><creatorcontrib>George Tsai</creatorcontrib><creatorcontrib>Hal F Yee, Jr</creatorcontrib><title>Ca2+-independent myosin II phosphorylation and contraction in chicken embryo fibroblasts</title><title>The Journal of physiology</title><addtitle>J Physiol</addtitle><description>Non-muscle contraction is widely believed to be mediated through Ca 2+ -stimulated myosin II regulatory light chain (LC20) phosphorylation, similar to the contractile regulation of smooth muscle.
However, this hypothesis lacks conclusive experimental support.
By modulating chicken embryo fibroblast cytosolic Ca 2+ concentration ([Ca 2+ ] i ), we investigated the putative role of [Ca 2+ ] i in fetal bovine serum (FBS)-stimulated LC20 phosphorylation and force development in these cells.
Eliminating the FBS-stimulated rise in [Ca 2+ ] i with the Ca 2+ chelator BAPTA only partially inhibited FBS-stimulated LC20 phosphorylation and did not significantly alter the magnitude
of FBS-stimulated isometric contraction.
Ionomycin (1 μ m ) produced a larger but shorter lasting rise in [Ca 2+ ] i relative to FBS. However, ionomycin only stimulated a small and transient increase in LC20 phosphorylation and did not cause
contraction.
We conclude that fibroblasts differ from smooth muscle in that LC20 phosphorylation and contraction are predominantly regulated
independently of [Ca 2+ ] i .</description><subject>Animals</subject><subject>Calcium - physiology</subject><subject>Chelating Agents - pharmacology</subject><subject>Chick Embryo</subject><subject>Cytosol - metabolism</subject><subject>Cytosol - physiology</subject><subject>Egtazic Acid - analogs & derivatives</subject><subject>Egtazic Acid - pharmacology</subject><subject>Fibroblasts</subject><subject>Ionomycin - pharmacology</subject><subject>Ionophores - pharmacology</subject><subject>Isometric Contraction - drug effects</subject><subject>Isometric Contraction - physiology</subject><subject>Myosin Light Chains - metabolism</subject><subject>Myosin Light Chains - physiology</subject><subject>Myosins - metabolism</subject><subject>Phosphorylation</subject><subject>Rapid Report</subject><issn>0022-3751</issn><issn>1469-7793</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1999</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVUV2L1DAUDaKs4-pPEPrki7Qm6STpRRBk8GNkQR9W8O2Stsk2Y5vUpuNu_73p7jBqILlczuHcc3MIyRgtWDpvDgXbSsiVgrJgAFDQSum2uHtENmfgMdlQynleKsGekmcxHihlJQW4IBcAXFQV3ZAfO81f5863ZjTp8XM2LCE6n-332diFmO609Hp2wWfat1kT_Dzp5r5PrKZzzU_jMzPU0xIy6-op1L2Oc3xOnljdR_PiVC_J948frnef86uvn_a791d5V8JW5VZIy42WRlspW6uk4JYKACMsVDVYkLISUiTfsra64WlZQVUrqJQWtlSWl-Tdg-54rAfTNmb11-M4uUFPCwbt8H_Euw5vwm_kXAJjkARenQSm8Oto4oyDi43pe-1NOEaUINSWVmUivvx30nnE6S8T_vYBv3W9Wc4wo7hGhgdck8E1GVwjw_vI8A6vv3yr1F8bnbvpbt1kcOyW6EIMjTPzgoIJZJiIfwCHH5oZ</recordid><startdate>19990215</startdate><enddate>19990215</enddate><creator>Michael S Kolodney</creator><creator>Matthew S Thimgan</creator><creator>Henry M Honda</creator><creator>George Tsai</creator><creator>Hal F Yee, Jr</creator><general>The Physiological Society</general><general>Blackwell Science Ltd</general><general>Blackwell Science Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19990215</creationdate><title>Ca2+-independent myosin II phosphorylation and contraction in chicken embryo fibroblasts</title><author>Michael S Kolodney ; Matthew S Thimgan ; Henry M Honda ; George Tsai ; Hal F Yee, Jr</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-h3947-f56f2ea6eaf66df7652f0599e5f98b9f96685651306bfac2199507d5066f94063</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1999</creationdate><topic>Animals</topic><topic>Calcium - physiology</topic><topic>Chelating Agents - pharmacology</topic><topic>Chick Embryo</topic><topic>Cytosol - metabolism</topic><topic>Cytosol - physiology</topic><topic>Egtazic Acid - analogs & derivatives</topic><topic>Egtazic Acid - pharmacology</topic><topic>Fibroblasts</topic><topic>Ionomycin - pharmacology</topic><topic>Ionophores - pharmacology</topic><topic>Isometric Contraction - drug effects</topic><topic>Isometric Contraction - physiology</topic><topic>Myosin Light Chains - metabolism</topic><topic>Myosin Light Chains - physiology</topic><topic>Myosins - metabolism</topic><topic>Phosphorylation</topic><topic>Rapid Report</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Michael S Kolodney</creatorcontrib><creatorcontrib>Matthew S Thimgan</creatorcontrib><creatorcontrib>Henry M Honda</creatorcontrib><creatorcontrib>George Tsai</creatorcontrib><creatorcontrib>Hal F Yee, Jr</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Michael S Kolodney</au><au>Matthew S Thimgan</au><au>Henry M Honda</au><au>George Tsai</au><au>Hal F Yee, Jr</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ca2+-independent myosin II phosphorylation and contraction in chicken embryo fibroblasts</atitle><jtitle>The Journal of physiology</jtitle><addtitle>J Physiol</addtitle><date>1999-02-15</date><risdate>1999</risdate><volume>515</volume><issue>1</issue><spage>87</spage><epage>92</epage><pages>87-92</pages><issn>0022-3751</issn><eissn>1469-7793</eissn><abstract>Non-muscle contraction is widely believed to be mediated through Ca 2+ -stimulated myosin II regulatory light chain (LC20) phosphorylation, similar to the contractile regulation of smooth muscle.
However, this hypothesis lacks conclusive experimental support.
By modulating chicken embryo fibroblast cytosolic Ca 2+ concentration ([Ca 2+ ] i ), we investigated the putative role of [Ca 2+ ] i in fetal bovine serum (FBS)-stimulated LC20 phosphorylation and force development in these cells.
Eliminating the FBS-stimulated rise in [Ca 2+ ] i with the Ca 2+ chelator BAPTA only partially inhibited FBS-stimulated LC20 phosphorylation and did not significantly alter the magnitude
of FBS-stimulated isometric contraction.
Ionomycin (1 μ m ) produced a larger but shorter lasting rise in [Ca 2+ ] i relative to FBS. However, ionomycin only stimulated a small and transient increase in LC20 phosphorylation and did not cause
contraction.
We conclude that fibroblasts differ from smooth muscle in that LC20 phosphorylation and contraction are predominantly regulated
independently of [Ca 2+ ] i .</abstract><cop>Oxford, UK</cop><pub>The Physiological Society</pub><pmid>9925880</pmid><doi>10.1111/j.1469-7793.1999.087ad.x</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| source | MEDLINE; Wiley Online Library Free Content; Access via Wiley Online Library; IngentaConnect Free/Open Access Journals; EZB-FREE-00999 freely available EZB journals; PubMed Central |
| subjects | Animals Calcium - physiology Chelating Agents - pharmacology Chick Embryo Cytosol - metabolism Cytosol - physiology Egtazic Acid - analogs & derivatives Egtazic Acid - pharmacology Fibroblasts Ionomycin - pharmacology Ionophores - pharmacology Isometric Contraction - drug effects Isometric Contraction - physiology Myosin Light Chains - metabolism Myosin Light Chains - physiology Myosins - metabolism Phosphorylation Rapid Report |
| title | Ca2+-independent myosin II phosphorylation and contraction in chicken embryo fibroblasts |
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