cGMP-mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery
Nitrovasodilators such as nitroglycerine, via production of nitric oxide and an increase in [cGMP], can induce arterial smooth muscle relaxation without proportional reduction in myosin light chain (MLC) phosphorylation or myoplasmic [Ca 2+ ]. These findings suggest that regulatory systems, other th...
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| creator | Rembold, Christopher M. Foster, D. Brian Strauss, John D. Wingard, Christopher J. Eyk, Jennifer E. |
| description | Nitrovasodilators such as nitroglycerine, via production of nitric oxide and an increase in [cGMP], can induce arterial smooth
muscle relaxation without proportional reduction in myosin light chain (MLC) phosphorylation or myoplasmic [Ca 2+ ]. These findings suggest that regulatory systems, other than MLC phosphorylation and Ca 2+ , partially mediate nitroglycerine-induced relaxation.
In swine carotid artery, we found that a membrane-permeant cGMP analogue induced relaxation without MLC dephosphorylation,
suggesting that cGMP mediated the relaxation.
Nitroglycerine-induced relaxation was associated with a reduction in O 2 consumption, suggesting that the interaction between phosphorylated myosin and the thin filament was inhibited.
Nitroglycerine-induced relaxation was associated with a 10-fold increase in the phosphorylation of a protein on Ser 16 . We identified this protein as heat shock protein 20 (HSP20), a member of a family of proteins known to bind to thin filaments.
When homogenates of nitroglycerine-relaxed tissues were centrifuged at 6000 g , phosphorylated HSP20 preferentially sedimented in the pellet, suggesting that phosphorylation of HSP20 may increase its
affinity for the thin filament.
We noted that a domain of HSP20 is partially homologous to the âminimum inhibitory sequenceâ of skeletal troponin I. The peptide
HSP20 110-121 , which contains this domain, bound to actin-containing filaments only in the presence of tropomyosin, a characteristic of
troponin I. High concentrations of HSP20 110-121 abolished Ca 2+ -activated force in skinned swine carotid artery. HSP20 110-121 also partially decreased actin-activated myosin S1 ATPase activity.
These data suggest that cGMP-mediated phosphorylation of HSP20 on Ser 16 may have a role in smooth muscle relaxation without MLC dephosphorylation. HSP20 contains an actin-binding sequence at amino
acid residues 110â121 that inhibited force production in skinned carotid artery. We hypothesize that phosphorylation of HSP20
regulates force independent of MLC phosphorylation via binding of HSP20 to thin filaments and inhibition of cross-bridge cycling. |
| doi_str_mv | 10.1111/j.1469-7793.2000.00865.x |
| format | Article |
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muscle relaxation without proportional reduction in myosin light chain (MLC) phosphorylation or myoplasmic [Ca 2+ ]. These findings suggest that regulatory systems, other than MLC phosphorylation and Ca 2+ , partially mediate nitroglycerine-induced relaxation.
In swine carotid artery, we found that a membrane-permeant cGMP analogue induced relaxation without MLC dephosphorylation,
suggesting that cGMP mediated the relaxation.
Nitroglycerine-induced relaxation was associated with a reduction in O 2 consumption, suggesting that the interaction between phosphorylated myosin and the thin filament was inhibited.
Nitroglycerine-induced relaxation was associated with a 10-fold increase in the phosphorylation of a protein on Ser 16 . We identified this protein as heat shock protein 20 (HSP20), a member of a family of proteins known to bind to thin filaments.
When homogenates of nitroglycerine-relaxed tissues were centrifuged at 6000 g , phosphorylated HSP20 preferentially sedimented in the pellet, suggesting that phosphorylation of HSP20 may increase its
affinity for the thin filament.
We noted that a domain of HSP20 is partially homologous to the âminimum inhibitory sequenceâ of skeletal troponin I. The peptide
HSP20 110-121 , which contains this domain, bound to actin-containing filaments only in the presence of tropomyosin, a characteristic of
troponin I. High concentrations of HSP20 110-121 abolished Ca 2+ -activated force in skinned swine carotid artery. HSP20 110-121 also partially decreased actin-activated myosin S1 ATPase activity.
These data suggest that cGMP-mediated phosphorylation of HSP20 on Ser 16 may have a role in smooth muscle relaxation without MLC dephosphorylation. HSP20 contains an actin-binding sequence at amino
acid residues 110â121 that inhibited force production in skinned carotid artery. We hypothesize that phosphorylation of HSP20
regulates force independent of MLC phosphorylation via binding of HSP20 to thin filaments and inhibition of cross-bridge cycling.</description><identifier>ISSN: 0022-3751</identifier><identifier>EISSN: 1469-7793</identifier><identifier>DOI: 10.1111/j.1469-7793.2000.00865.x</identifier><identifier>PMID: 10790164</identifier><language>eng</language><publisher>Oxford, UK: The Physiological Society</publisher><subject>Actins - isolation & purification ; Actins - metabolism ; Actomyosin - chemistry ; Actomyosin - metabolism ; Animals ; Carotid Arteries - chemistry ; Carotid Arteries - metabolism ; Centrifugation ; Crystallins - chemistry ; Crystallins - metabolism ; Cyclic GMP - metabolism ; Heat-Shock Proteins - chemistry ; Heat-Shock Proteins - isolation & purification ; Heat-Shock Proteins - metabolism ; Histamine - pharmacology ; HSP20 Heat-Shock Proteins ; In Vitro Techniques ; Molecular Sequence Data ; Muscle, Smooth, Vascular - metabolism ; Myosin Light Chains - metabolism ; Nitroglycerin - pharmacology ; Original ; Oxygen Consumption - drug effects ; Phosphoproteins - chemistry ; Phosphoproteins - isolation & purification ; Phosphoproteins - metabolism ; Phosphorylation ; Sequence Homology, Amino Acid ; Swine ; Troponin I - chemistry ; Troponin I - metabolism ; Vasodilation - drug effects ; Vasodilation - physiology ; Vasodilator Agents - pharmacology</subject><ispartof>The Journal of physiology, 2000-05, Vol.524 (3), p.865-878</ispartof><rights>2000 The Journal of Physiology © 2000 The Physiological Society</rights><rights>The Physiological Society 2000 2000</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c5675-ac3ee8ee1794573f0182e89f0ef8149743be4ea1307104d7b442e66775b7010c3</citedby><cites>FETCH-LOGICAL-c5675-ac3ee8ee1794573f0182e89f0ef8149743be4ea1307104d7b442e66775b7010c3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2269896/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC2269896/$$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/10790164$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Rembold, Christopher M.</creatorcontrib><creatorcontrib>Foster, D. Brian</creatorcontrib><creatorcontrib>Strauss, John D.</creatorcontrib><creatorcontrib>Wingard, Christopher J.</creatorcontrib><creatorcontrib>Eyk, Jennifer E.</creatorcontrib><title>cGMP-mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery</title><title>The Journal of physiology</title><addtitle>J Physiol</addtitle><description>Nitrovasodilators such as nitroglycerine, via production of nitric oxide and an increase in [cGMP], can induce arterial smooth
muscle relaxation without proportional reduction in myosin light chain (MLC) phosphorylation or myoplasmic [Ca 2+ ]. These findings suggest that regulatory systems, other than MLC phosphorylation and Ca 2+ , partially mediate nitroglycerine-induced relaxation.
In swine carotid artery, we found that a membrane-permeant cGMP analogue induced relaxation without MLC dephosphorylation,
suggesting that cGMP mediated the relaxation.
Nitroglycerine-induced relaxation was associated with a reduction in O 2 consumption, suggesting that the interaction between phosphorylated myosin and the thin filament was inhibited.
Nitroglycerine-induced relaxation was associated with a 10-fold increase in the phosphorylation of a protein on Ser 16 . We identified this protein as heat shock protein 20 (HSP20), a member of a family of proteins known to bind to thin filaments.
When homogenates of nitroglycerine-relaxed tissues were centrifuged at 6000 g , phosphorylated HSP20 preferentially sedimented in the pellet, suggesting that phosphorylation of HSP20 may increase its
affinity for the thin filament.
We noted that a domain of HSP20 is partially homologous to the âminimum inhibitory sequenceâ of skeletal troponin I. The peptide
HSP20 110-121 , which contains this domain, bound to actin-containing filaments only in the presence of tropomyosin, a characteristic of
troponin I. High concentrations of HSP20 110-121 abolished Ca 2+ -activated force in skinned swine carotid artery. HSP20 110-121 also partially decreased actin-activated myosin S1 ATPase activity.
These data suggest that cGMP-mediated phosphorylation of HSP20 on Ser 16 may have a role in smooth muscle relaxation without MLC dephosphorylation. HSP20 contains an actin-binding sequence at amino
acid residues 110â121 that inhibited force production in skinned carotid artery. We hypothesize that phosphorylation of HSP20
regulates force independent of MLC phosphorylation via binding of HSP20 to thin filaments and inhibition of cross-bridge cycling.</description><subject>Actins - isolation & purification</subject><subject>Actins - metabolism</subject><subject>Actomyosin - chemistry</subject><subject>Actomyosin - metabolism</subject><subject>Animals</subject><subject>Carotid Arteries - chemistry</subject><subject>Carotid Arteries - metabolism</subject><subject>Centrifugation</subject><subject>Crystallins - chemistry</subject><subject>Crystallins - metabolism</subject><subject>Cyclic GMP - metabolism</subject><subject>Heat-Shock Proteins - chemistry</subject><subject>Heat-Shock Proteins - isolation & purification</subject><subject>Heat-Shock Proteins - metabolism</subject><subject>Histamine - pharmacology</subject><subject>HSP20 Heat-Shock Proteins</subject><subject>In Vitro Techniques</subject><subject>Molecular Sequence Data</subject><subject>Muscle, Smooth, Vascular - metabolism</subject><subject>Myosin Light Chains - metabolism</subject><subject>Nitroglycerin - pharmacology</subject><subject>Original</subject><subject>Oxygen Consumption - drug effects</subject><subject>Phosphoproteins - chemistry</subject><subject>Phosphoproteins - isolation & purification</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Sequence Homology, Amino Acid</subject><subject>Swine</subject><subject>Troponin I - chemistry</subject><subject>Troponin I - metabolism</subject><subject>Vasodilation - drug effects</subject><subject>Vasodilation - physiology</subject><subject>Vasodilator Agents - pharmacology</subject><issn>0022-3751</issn><issn>1469-7793</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqNUV9v1SAUJ0bjrtOvYHjSp1ZoaSmJMTGLbpoZ9zCfCZeeDq5tuQLdvf0yftZRuyzTJ0kIJ5zfnwM_hDAlOU3r3S6nrBYZ56LMC0JITkhTV_nxCdo8NJ6iDSFFkZW8oifoRQg7QmhJhHiOTijhgtCabdBvff7tKhugtSpCi_fGhbT93Kto3Yhdhw2oiINx-ifeexfBjrggeFAz1moKgMPgXDR4mILuAXvo1XHlHmw0bop4mF1IpN7emIi1Ualu4V-jdBkOdoQkmkxsi5WP4OeX6Fmn-gCv7s9T9OPzp-uzi-zy-_mXs4-Xma5qXmVKlwANAOWCVbzsCG0KaERHoGsoE5yVW2Cg0vM5JazlW8YKqGvOqy0nlOjyFH1YdffTNn2GhjF61cu9t4Pys3TKyr87ozXyxt3KoqhFI-ok8OZewLtfE4QoBxs09L0awU1BJl_OWFMmYLMCtXcheOgeTCiRS7hyJ5cM5ZKhXMKVf8KVx0R9_XjIR8Q1zQR4vwIOtof5v4Xl9derVCT625VuUlQH60HuzRysC05biLOsCiZLuSDvAGCjxdU</recordid><startdate>20000501</startdate><enddate>20000501</enddate><creator>Rembold, Christopher M.</creator><creator>Foster, D. Brian</creator><creator>Strauss, John D.</creator><creator>Wingard, Christopher J.</creator><creator>Eyk, Jennifer E.</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>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20000501</creationdate><title>cGMP-mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery</title><author>Rembold, Christopher M. ; Foster, D. Brian ; Strauss, John D. ; Wingard, Christopher J. ; Eyk, Jennifer E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c5675-ac3ee8ee1794573f0182e89f0ef8149743be4ea1307104d7b442e66775b7010c3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Actins - isolation & purification</topic><topic>Actins - metabolism</topic><topic>Actomyosin - chemistry</topic><topic>Actomyosin - metabolism</topic><topic>Animals</topic><topic>Carotid Arteries - chemistry</topic><topic>Carotid Arteries - metabolism</topic><topic>Centrifugation</topic><topic>Crystallins - chemistry</topic><topic>Crystallins - metabolism</topic><topic>Cyclic GMP - metabolism</topic><topic>Heat-Shock Proteins - chemistry</topic><topic>Heat-Shock Proteins - isolation & purification</topic><topic>Heat-Shock Proteins - metabolism</topic><topic>Histamine - pharmacology</topic><topic>HSP20 Heat-Shock Proteins</topic><topic>In Vitro Techniques</topic><topic>Molecular Sequence Data</topic><topic>Muscle, Smooth, Vascular - metabolism</topic><topic>Myosin Light Chains - metabolism</topic><topic>Nitroglycerin - pharmacology</topic><topic>Original</topic><topic>Oxygen Consumption - drug effects</topic><topic>Phosphoproteins - chemistry</topic><topic>Phosphoproteins - isolation & purification</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Sequence Homology, Amino Acid</topic><topic>Swine</topic><topic>Troponin I - chemistry</topic><topic>Troponin I - metabolism</topic><topic>Vasodilation - drug effects</topic><topic>Vasodilation - physiology</topic><topic>Vasodilator Agents - pharmacology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Rembold, Christopher M.</creatorcontrib><creatorcontrib>Foster, D. Brian</creatorcontrib><creatorcontrib>Strauss, John D.</creatorcontrib><creatorcontrib>Wingard, Christopher J.</creatorcontrib><creatorcontrib>Eyk, Jennifer E.</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><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>Rembold, Christopher M.</au><au>Foster, D. Brian</au><au>Strauss, John D.</au><au>Wingard, Christopher J.</au><au>Eyk, Jennifer E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>cGMP-mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery</atitle><jtitle>The Journal of physiology</jtitle><addtitle>J Physiol</addtitle><date>2000-05-01</date><risdate>2000</risdate><volume>524</volume><issue>3</issue><spage>865</spage><epage>878</epage><pages>865-878</pages><issn>0022-3751</issn><eissn>1469-7793</eissn><abstract>Nitrovasodilators such as nitroglycerine, via production of nitric oxide and an increase in [cGMP], can induce arterial smooth
muscle relaxation without proportional reduction in myosin light chain (MLC) phosphorylation or myoplasmic [Ca 2+ ]. These findings suggest that regulatory systems, other than MLC phosphorylation and Ca 2+ , partially mediate nitroglycerine-induced relaxation.
In swine carotid artery, we found that a membrane-permeant cGMP analogue induced relaxation without MLC dephosphorylation,
suggesting that cGMP mediated the relaxation.
Nitroglycerine-induced relaxation was associated with a reduction in O 2 consumption, suggesting that the interaction between phosphorylated myosin and the thin filament was inhibited.
Nitroglycerine-induced relaxation was associated with a 10-fold increase in the phosphorylation of a protein on Ser 16 . We identified this protein as heat shock protein 20 (HSP20), a member of a family of proteins known to bind to thin filaments.
When homogenates of nitroglycerine-relaxed tissues were centrifuged at 6000 g , phosphorylated HSP20 preferentially sedimented in the pellet, suggesting that phosphorylation of HSP20 may increase its
affinity for the thin filament.
We noted that a domain of HSP20 is partially homologous to the âminimum inhibitory sequenceâ of skeletal troponin I. The peptide
HSP20 110-121 , which contains this domain, bound to actin-containing filaments only in the presence of tropomyosin, a characteristic of
troponin I. High concentrations of HSP20 110-121 abolished Ca 2+ -activated force in skinned swine carotid artery. HSP20 110-121 also partially decreased actin-activated myosin S1 ATPase activity.
These data suggest that cGMP-mediated phosphorylation of HSP20 on Ser 16 may have a role in smooth muscle relaxation without MLC dephosphorylation. HSP20 contains an actin-binding sequence at amino
acid residues 110â121 that inhibited force production in skinned carotid artery. We hypothesize that phosphorylation of HSP20
regulates force independent of MLC phosphorylation via binding of HSP20 to thin filaments and inhibition of cross-bridge cycling.</abstract><cop>Oxford, UK</cop><pub>The Physiological Society</pub><pmid>10790164</pmid><doi>10.1111/j.1469-7793.2000.00865.x</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of physiology, 2000-05, Vol.524 (3), p.865-878 |
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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 | Actins - isolation & purification Actins - metabolism Actomyosin - chemistry Actomyosin - metabolism Animals Carotid Arteries - chemistry Carotid Arteries - metabolism Centrifugation Crystallins - chemistry Crystallins - metabolism Cyclic GMP - metabolism Heat-Shock Proteins - chemistry Heat-Shock Proteins - isolation & purification Heat-Shock Proteins - metabolism Histamine - pharmacology HSP20 Heat-Shock Proteins In Vitro Techniques Molecular Sequence Data Muscle, Smooth, Vascular - metabolism Myosin Light Chains - metabolism Nitroglycerin - pharmacology Original Oxygen Consumption - drug effects Phosphoproteins - chemistry Phosphoproteins - isolation & purification Phosphoproteins - metabolism Phosphorylation Sequence Homology, Amino Acid Swine Troponin I - chemistry Troponin I - metabolism Vasodilation - drug effects Vasodilation - physiology Vasodilator Agents - pharmacology |
| title | cGMP-mediated phosphorylation of heat shock protein 20 may cause smooth muscle relaxation without myosin light chain dephosphorylation in swine carotid artery |
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