Chicken gizzard: relation between calcium-activated phosphorylation and contraction

Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca$^{2+}$-and Sr$^{2+}$-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca$^{2+}$- and Sr$^{2+}$-activated ten...

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Veröffentlicht in:	Science (American Association for the Advancement of Science) 1979-05, Vol.204 (4392), p.503-506
Hauptverfasser:	Hoar, P E, Kerrick, W G, Cassidy, P S
Format:	Artikel
Sprache:	eng
Schlagworte:	Anatomy Animals Calcium - pharmacology Chickens Creatine Gels Gizzard Gizzard, Avian - physiology In Vitro Techniques Molecular Weight Muscle Contraction - drug effects Muscle, Smooth - physiology Myosins - metabolism Nucleotides Phosphatases Phosphates Phosphorylation Poultry Poultry (Animals) Protein Kinases - metabolism Skeletal muscle Smooth muscle
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container_title	Science (American Association for the Advancement of Science)
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creator	Hoar, P E Kerrick, W G Cassidy, P S
description	Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca$^{2+}$-and Sr$^{2+}$-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca$^{2+}$- and Sr$^{2+}$-activated tensions. Adenosine 5′-O (3′-thiotriphosphate) only in the presence of Ca$^{2+}$ induced irreversible Ca$^{2+}$-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of $^{32}$P from [γ-$^{32}$P]adenosine triphosphate into the myosin light chains.
doi_str_mv	10.1126/science.432654
format	Article
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Phosphorylation closely corresponded with the Ca$^{2+}$- and Sr$^{2+}$-activated tensions. Adenosine 5′-O (3′-thiotriphosphate) only in the presence of Ca$^{2+}$ induced irreversible Ca$^{2+}$-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of $^{32}$P from [γ-$^{32}$P]adenosine triphosphate into the myosin light chains.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.432654</identifier><identifier>PMID: 432654</identifier><language>eng</language><publisher>United States: American Association for the Advancement of Science</publisher><subject>Anatomy ; Animals ; Calcium - pharmacology ; Chickens ; Creatine ; Gels ; Gizzard ; Gizzard, Avian - physiology ; In Vitro Techniques ; Molecular Weight ; Muscle Contraction - drug effects ; Muscle, Smooth - physiology ; Myosins - metabolism ; Nucleotides ; Phosphatases ; Phosphates ; Phosphorylation ; Poultry ; Poultry (Animals) ; Protein Kinases - metabolism ; Skeletal muscle ; Smooth muscle</subject><ispartof>Science (American Association for the Advancement of Science), 1979-05, Vol.204 (4392), p.503-506</ispartof><rights>Copyright 1979 American Association for the Advancement of Science</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c399t-5223f5790d61c7133cf15818c9320be1548d4a0d5e2b38bd310fcefa25bf3b253</citedby><cites>FETCH-LOGICAL-c399t-5223f5790d61c7133cf15818c9320be1548d4a0d5e2b38bd310fcefa25bf3b253</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/1748809$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/1748809$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,776,780,799,2871,2872,27901,27902,57992,58225</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/432654$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hoar, P E</creatorcontrib><creatorcontrib>Kerrick, W G</creatorcontrib><creatorcontrib>Cassidy, P S</creatorcontrib><title>Chicken gizzard: relation between calcium-activated phosphorylation and contraction</title><title>Science (American Association for the Advancement of Science)</title><addtitle>Science</addtitle><description>Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca$^{2+}$-and Sr$^{2+}$-dependent changes in phosphorylation. 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Adenosine 5′-O (3′-thiotriphosphate) only in the presence of Ca$^{2+}$ induced irreversible Ca$^{2+}$-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of $^{32}$P from [γ-$^{32}$P]adenosine triphosphate into the myosin light chains.</description><subject>Anatomy</subject><subject>Animals</subject><subject>Calcium - pharmacology</subject><subject>Chickens</subject><subject>Creatine</subject><subject>Gels</subject><subject>Gizzard</subject><subject>Gizzard, Avian - physiology</subject><subject>In Vitro Techniques</subject><subject>Molecular Weight</subject><subject>Muscle Contraction - drug effects</subject><subject>Muscle, Smooth - physiology</subject><subject>Myosins - metabolism</subject><subject>Nucleotides</subject><subject>Phosphatases</subject><subject>Phosphates</subject><subject>Phosphorylation</subject><subject>Poultry</subject><subject>Poultry (Animals)</subject><subject>Protein Kinases - metabolism</subject><subject>Skeletal muscle</subject><subject>Smooth muscle</subject><issn>0036-8075</issn><issn>1095-9203</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1979</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpdkDtP5DAUhS3Ea3i0VCuUaptVhms7Tuzt0GhhkZAogNpynJvBkIkH27M8fj0ZMlokCsvF992jo0PICYUppaw8i9Zhb3FacFaKYotMKCiRKwZ8m0wAeJlLqMQ-OYjxEWBgiu-R3dGekNvZg7NP2Gdz9_5uQvM7C9iZ5Hyf1ZhecCDWdNatFrmxyf0zCZts-eDj8MLbxjR9k1nfp7BWfH9EdlrTRTze_Ifk_uLP3exvfn1zeTU7v84tVyrlgjHeikpBU1JbUc5tS4Wk0irOoEYqCtkUBhqBrOaybjiF1mJrmKhbXjPBD8nPMXcZ_PMKY9ILFy12nenRr6KuClFwkGwQf43i3HSoXb_uiq_J-q7DOeqh1OxGn1NWMfYZOx1tG3yMAVu9DG5hwpumoNeT683kehxxOPix6bGqF9j817_jx5h8-AqrCilBDfh0xK3x2syDi_r-lioJIEBWtOQfanyQeA</recordid><startdate>19790504</startdate><enddate>19790504</enddate><creator>Hoar, P E</creator><creator>Kerrick, W G</creator><creator>Cassidy, P S</creator><general>American Association for the Advancement of Science</general><scope>FBQ</scope><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>19790504</creationdate><title>Chicken gizzard: relation between calcium-activated phosphorylation and contraction</title><author>Hoar, P E ; Kerrick, W G ; Cassidy, P S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c399t-5223f5790d61c7133cf15818c9320be1548d4a0d5e2b38bd310fcefa25bf3b253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1979</creationdate><topic>Anatomy</topic><topic>Animals</topic><topic>Calcium - pharmacology</topic><topic>Chickens</topic><topic>Creatine</topic><topic>Gels</topic><topic>Gizzard</topic><topic>Gizzard, Avian - physiology</topic><topic>In Vitro Techniques</topic><topic>Molecular Weight</topic><topic>Muscle Contraction - drug effects</topic><topic>Muscle, Smooth - physiology</topic><topic>Myosins - metabolism</topic><topic>Nucleotides</topic><topic>Phosphatases</topic><topic>Phosphates</topic><topic>Phosphorylation</topic><topic>Poultry</topic><topic>Poultry (Animals)</topic><topic>Protein Kinases - metabolism</topic><topic>Skeletal muscle</topic><topic>Smooth muscle</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hoar, P E</creatorcontrib><creatorcontrib>Kerrick, W G</creatorcontrib><creatorcontrib>Cassidy, P S</creatorcontrib><collection>AGRIS</collection><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>Science (American Association for the Advancement of Science)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hoar, P E</au><au>Kerrick, W G</au><au>Cassidy, P S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Chicken gizzard: relation between calcium-activated phosphorylation and contraction</atitle><jtitle>Science (American Association for the Advancement of Science)</jtitle><addtitle>Science</addtitle><date>1979-05-04</date><risdate>1979</risdate><volume>204</volume><issue>4392</issue><spage>503</spage><epage>506</epage><pages>503-506</pages><issn>0036-8075</issn><eissn>1095-9203</eissn><abstract>Of the proteins in mechanically disrupted chicken gizzard fibers (no functional sarcolemma) only the 20,000-dalton light chains of myosin underwent large Ca$^{2+}$-and Sr$^{2+}$-dependent changes in phosphorylation. Phosphorylation closely corresponded with the Ca$^{2+}$- and Sr$^{2+}$-activated tensions. Adenosine 5′-O (3′-thiotriphosphate) only in the presence of Ca$^{2+}$ induced irreversible Ca$^{2+}$-insensitive activation of tension and thiophosphorylation of the 20,000-dalton light chains, and blocked incorporation of $^{32}$P from [γ-$^{32}$P]adenosine triphosphate into the myosin light chains.</abstract><cop>United States</cop><pub>American Association for the Advancement of Science</pub><pmid>432654</pmid><doi>10.1126/science.432654</doi><tpages>4</tpages></addata></record>
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source	American Association for the Advancement of Science; Jstor Complete Legacy; MEDLINE
subjects	Anatomy Animals Calcium - pharmacology Chickens Creatine Gels Gizzard Gizzard, Avian - physiology In Vitro Techniques Molecular Weight Muscle Contraction - drug effects Muscle, Smooth - physiology Myosins - metabolism Nucleotides Phosphatases Phosphates Phosphorylation Poultry Poultry (Animals) Protein Kinases - metabolism Skeletal muscle Smooth muscle
title	Chicken gizzard: relation between calcium-activated phosphorylation and contraction
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