The tightly bound divalent cation regulates actin polymerization
The polymerization characteristics of Ca ++-actin and Mg ++-actin were studied by measuring initial rates of polymerization upon addition of phalloidin-stabilized nuclei and neutral salt. Under conditions where the effects of divalent cation exchange were minimized, CaCl 2 and MgCl 2 were found to b...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1983-10, Vol.116 (2), p.478-485 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Selden, Lynn A. Estes, James E. Gershman, Lewis C. |
| description | The polymerization characteristics of Ca
++-actin and Mg
++-actin were studied by measuring initial rates of polymerization upon addition of phalloidin-stabilized nuclei and neutral salt. Under conditions where the effects of divalent cation exchange were minimized, CaCl
2 and MgCl
2 were found to be equally effective in polymerizing actin. Mg
++-actin was found to nucleate and polymerize more readily than Ca
++-actin, having a forward rate constant about twice that of Ca
++-actin under a variety of polymerizing conditions. The critical concentration for Ca
++-actin is approximately 20 times that for Mg
++-actin under equivalent conditions. These data imply that the polymer of Mg
++-actin must be more stable than that of Ca
++-actin, having a depolymerization rate constant about 10 fold lower. Since Mg
++ is probably the tightly-bound cation
in vivo
, whereas Ca
++-actin has been more widely studied
in vitro
, it would appear that actin in its physiological state is probably more polymerizable and more stable in the polymer form than previously considered. |
| doi_str_mv | 10.1016/0006-291X(83)90548-X |
| format | Article |
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++-actin and Mg
++-actin were studied by measuring initial rates of polymerization upon addition of phalloidin-stabilized nuclei and neutral salt. Under conditions where the effects of divalent cation exchange were minimized, CaCl
2 and MgCl
2 were found to be equally effective in polymerizing actin. Mg
++-actin was found to nucleate and polymerize more readily than Ca
++-actin, having a forward rate constant about twice that of Ca
++-actin under a variety of polymerizing conditions. The critical concentration for Ca
++-actin is approximately 20 times that for Mg
++-actin under equivalent conditions. These data imply that the polymer of Mg
++-actin must be more stable than that of Ca
++-actin, having a depolymerization rate constant about 10 fold lower. Since Mg
++ is probably the tightly-bound cation
in vivo
, whereas Ca
++-actin has been more widely studied
in vitro
, it would appear that actin in its physiological state is probably more polymerizable and more stable in the polymer form than previously considered.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/0006-291X(83)90548-X</identifier><identifier>PMID: 6651822</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>actin ; Actins - metabolism ; calcium ; Calcium - metabolism ; Calcium Chloride - metabolism ; magnesium ; Magnesium - metabolism ; Magnesium Chloride ; Polymers - metabolism ; Time Factors</subject><ispartof>Biochemical and biophysical research communications, 1983-10, Vol.116 (2), p.478-485</ispartof><rights>1983</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c454t-3800bdcd17e06c2ba941728280a0d9a0ee60346a8b6b3befc17021e8912cab533</citedby><cites>FETCH-LOGICAL-c454t-3800bdcd17e06c2ba941728280a0d9a0ee60346a8b6b3befc17021e8912cab533</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/0006291X8390548X$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/6651822$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Selden, Lynn A.</creatorcontrib><creatorcontrib>Estes, James E.</creatorcontrib><creatorcontrib>Gershman, Lewis C.</creatorcontrib><title>The tightly bound divalent cation regulates actin polymerization</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The polymerization characteristics of Ca
++-actin and Mg
++-actin were studied by measuring initial rates of polymerization upon addition of phalloidin-stabilized nuclei and neutral salt. Under conditions where the effects of divalent cation exchange were minimized, CaCl
2 and MgCl
2 were found to be equally effective in polymerizing actin. Mg
++-actin was found to nucleate and polymerize more readily than Ca
++-actin, having a forward rate constant about twice that of Ca
++-actin under a variety of polymerizing conditions. The critical concentration for Ca
++-actin is approximately 20 times that for Mg
++-actin under equivalent conditions. These data imply that the polymer of Mg
++-actin must be more stable than that of Ca
++-actin, having a depolymerization rate constant about 10 fold lower. Since Mg
++ is probably the tightly-bound cation
in vivo
, whereas Ca
++-actin has been more widely studied
in vitro
, it would appear that actin in its physiological state is probably more polymerizable and more stable in the polymer form than previously considered.</description><subject>actin</subject><subject>Actins - metabolism</subject><subject>calcium</subject><subject>Calcium - metabolism</subject><subject>Calcium Chloride - metabolism</subject><subject>magnesium</subject><subject>Magnesium - metabolism</subject><subject>Magnesium Chloride</subject><subject>Polymers - metabolism</subject><subject>Time Factors</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1983</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtLxDAUhYMoOo7-A4WuRBfVe9NMmm5EEV8w4EZhdiFN72ik045JKoy_3s6DWerqLs53zoWPsROESwSUVwAgU17g5FxlFwWMhEonO2yAUEDKEcQuG2yRA3YYwicAopDFPtuXcoSK8wG7ef2gJLr3j1gvkrLtmiqp3LepqYmJNdG1TeLpvatNpJAYG12TzNt6MSPvflbxEdubmjrQ8eYO2dvD_evdUzp-eXy-ux2nVoxETDMFUFa2wpxAWl6aQmDOFVdgoCoMEEnIhDSqlGVW0tRiDhxJFcitKUdZNmRn6925b786ClHPXLBU16ahtgtagQIuc_4viFme96-wB8UatL4NwdNUz72bGb_QCHppWC_16aU-rTK9Mqwnfe10s9-VM6q2pY3SPr9e59Tb-HbkdbCOGkuV82Sjrlr394Nf1TGK3g</recordid><startdate>19831031</startdate><enddate>19831031</enddate><creator>Selden, Lynn A.</creator><creator>Estes, James E.</creator><creator>Gershman, Lewis C.</creator><general>Elsevier 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>7QL</scope><scope>C1K</scope><scope>7X8</scope></search><sort><creationdate>19831031</creationdate><title>The tightly bound divalent cation regulates actin polymerization</title><author>Selden, Lynn A. ; Estes, James E. ; Gershman, Lewis C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c454t-3800bdcd17e06c2ba941728280a0d9a0ee60346a8b6b3befc17021e8912cab533</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1983</creationdate><topic>actin</topic><topic>Actins - metabolism</topic><topic>calcium</topic><topic>Calcium - metabolism</topic><topic>Calcium Chloride - metabolism</topic><topic>magnesium</topic><topic>Magnesium - metabolism</topic><topic>Magnesium Chloride</topic><topic>Polymers - metabolism</topic><topic>Time Factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Selden, Lynn A.</creatorcontrib><creatorcontrib>Estes, James E.</creatorcontrib><creatorcontrib>Gershman, Lewis C.</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environmental Sciences and Pollution Management</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Selden, Lynn A.</au><au>Estes, James E.</au><au>Gershman, Lewis C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The tightly bound divalent cation regulates actin polymerization</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1983-10-31</date><risdate>1983</risdate><volume>116</volume><issue>2</issue><spage>478</spage><epage>485</epage><pages>478-485</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>The polymerization characteristics of Ca
++-actin and Mg
++-actin were studied by measuring initial rates of polymerization upon addition of phalloidin-stabilized nuclei and neutral salt. Under conditions where the effects of divalent cation exchange were minimized, CaCl
2 and MgCl
2 were found to be equally effective in polymerizing actin. Mg
++-actin was found to nucleate and polymerize more readily than Ca
++-actin, having a forward rate constant about twice that of Ca
++-actin under a variety of polymerizing conditions. The critical concentration for Ca
++-actin is approximately 20 times that for Mg
++-actin under equivalent conditions. These data imply that the polymer of Mg
++-actin must be more stable than that of Ca
++-actin, having a depolymerization rate constant about 10 fold lower. Since Mg
++ is probably the tightly-bound cation
in vivo
, whereas Ca
++-actin has been more widely studied
in vitro
, it would appear that actin in its physiological state is probably more polymerizable and more stable in the polymer form than previously considered.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>6651822</pmid><doi>10.1016/0006-291X(83)90548-X</doi><tpages>8</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0006-291X |
| ispartof | Biochemical and biophysical research communications, 1983-10, Vol.116 (2), p.478-485 |
| issn | 0006-291X 1090-2104 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_80802672 |
| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | actin Actins - metabolism calcium Calcium - metabolism Calcium Chloride - metabolism magnesium Magnesium - metabolism Magnesium Chloride Polymers - metabolism Time Factors |
| title | The tightly bound divalent cation regulates actin polymerization |
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