Cytochalasin B binding and actin content of endoplasmic reticulum subfractions isolated from L-929 cells
Heavy rough (HR) endoplasmic reticulum (ER) membranes and a dense fraction of light rough (LR) membranes (LR I) of L-929 cells bind 3H-cytochalasin B extremely poorly in comparison to smooth (S) membranes and a fraction of LR membranes of low density (LR II). The LR and S subfractions of ER are appa...
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| Veröffentlicht in: | Cell biology international reports 1987-08, Vol.11 (8), p.615-623 |
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| creator | Pryme, Ian F. Hesketh, John E. |
| description | Heavy rough (HR) endoplasmic reticulum (ER) membranes and a dense fraction of light rough (LR) membranes (LR I) of L-929 cells bind
3H-cytochalasin B extremely poorly in comparison to smooth (S) membranes and a fraction of LR membranes of low density (LR II). The LR and S subfractions of ER are apparently heterogeneous membrane populations with respect to cytochalasin B binding. The separation of proteins in HR and LR subfractions by electrophoresis followed by immunoblotting with monoclonal antibodies against actin showed that actin was not present in the former membranes while there were large amounts in the LR subfraction. It is concluded that membranes in the LR II fraction of ER are associated with actin-containing microfilaments of the cytoskeleton, but that HR membranes are not. |
| doi_str_mv | 10.1016/0309-1651(87)90142-1 |
| format | Article |
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3H-cytochalasin B extremely poorly in comparison to smooth (S) membranes and a fraction of LR membranes of low density (LR II). The LR and S subfractions of ER are apparently heterogeneous membrane populations with respect to cytochalasin B binding. The separation of proteins in HR and LR subfractions by electrophoresis followed by immunoblotting with monoclonal antibodies against actin showed that actin was not present in the former membranes while there were large amounts in the LR subfraction. It is concluded that membranes in the LR II fraction of ER are associated with actin-containing microfilaments of the cytoskeleton, but that HR membranes are not.</description><identifier>ISSN: 0309-1651</identifier><identifier>EISSN: 1878-240X</identifier><identifier>DOI: 10.1016/0309-1651(87)90142-1</identifier><identifier>PMID: 3621359</identifier><identifier>CODEN: CBRPDS</identifier><language>eng</language><publisher>London: Elsevier B.V</publisher><subject>Actins - metabolism ; Animals ; Antibodies, Monoclonal ; Biological and medical sciences ; Cell structures and functions ; Cytochalasin B - metabolism ; Cytoskeleton, cytoplasm. Intracellular movements ; Electrophoresis, Polyacrylamide Gel ; Endoplasmic Reticulum - physiology ; Fundamental and applied biological sciences. Psychology ; Intracellular Membranes - metabolism ; L Cells (Cell Line) ; Mice ; Molecular and cellular biology ; Subcellular Fractions - metabolism</subject><ispartof>Cell biology international reports, 1987-08, Vol.11 (8), p.615-623</ispartof><rights>1987</rights><rights>1988 INIST-CNRS</rights><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c386t-d91135503904a3aa5abaa3913eb45b3ff96d3888869b0bd6d5c095fd09e97983</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,776,780,27901,27902</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=7533911$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/3621359$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Pryme, Ian F.</creatorcontrib><creatorcontrib>Hesketh, John E.</creatorcontrib><title>Cytochalasin B binding and actin content of endoplasmic reticulum subfractions isolated from L-929 cells</title><title>Cell biology international reports</title><addtitle>Cell Biol Int Rep</addtitle><description>Heavy rough (HR) endoplasmic reticulum (ER) membranes and a dense fraction of light rough (LR) membranes (LR I) of L-929 cells bind
3H-cytochalasin B extremely poorly in comparison to smooth (S) membranes and a fraction of LR membranes of low density (LR II). The LR and S subfractions of ER are apparently heterogeneous membrane populations with respect to cytochalasin B binding. The separation of proteins in HR and LR subfractions by electrophoresis followed by immunoblotting with monoclonal antibodies against actin showed that actin was not present in the former membranes while there were large amounts in the LR subfraction. It is concluded that membranes in the LR II fraction of ER are associated with actin-containing microfilaments of the cytoskeleton, but that HR membranes are not.</description><subject>Actins - metabolism</subject><subject>Animals</subject><subject>Antibodies, Monoclonal</subject><subject>Biological and medical sciences</subject><subject>Cell structures and functions</subject><subject>Cytochalasin B - metabolism</subject><subject>Cytoskeleton, cytoplasm. Intracellular movements</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Endoplasmic Reticulum - physiology</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Intracellular Membranes - metabolism</subject><subject>L Cells (Cell Line)</subject><subject>Mice</subject><subject>Molecular and cellular biology</subject><subject>Subcellular Fractions - metabolism</subject><issn>0309-1651</issn><issn>1878-240X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1987</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kM9P2zAUgK1pCErHfzAkHxDaDmF2nDjxBYlVDJAqceHAzXLsl-EpsYvtIPW_x2mrHueL_fy-90MfQt8puaGE8l-EEVFQXtMfbfNTEFqVBf2CFrRt2qKsyOtXtDgiZ-g8xn8kx6wWp-iU8ZLm1wK9rbbJ6zc1qGgd_o0764x1f7FyBiud8p_2LoFL2PcYnPGbTI5W4wDJ6mmYRhynrg8z613ENvpBJTC4D37E60KUAmsYhvgNnfRqiHBxuJfo5c_9y-qxWD8_PK3u1oVmLU-FETQvVhMmSKWYUrXqlGKCMuiqumN9L7hhbT5cdKQz3NSaiLo3RIBoRMuW6HrfdhP8-wQxydHGeQHlwE9RNg3npMkzlqjagzr4GAP0chPsqMJWUiJnv3KWJ2d5sm3kzq-cyy4P_aduBHMsOgjN-atDXkWthizGaRuPWFMzJnbTb_cYZBUfFoKM2oLTYGwAnaTx9v97fAIsfpaf</recordid><startdate>19870801</startdate><enddate>19870801</enddate><creator>Pryme, Ian F.</creator><creator>Hesketh, John E.</creator><general>Elsevier B.V</general><general>Academic Press</general><scope>IQODW</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>19870801</creationdate><title>Cytochalasin B binding and actin content of endoplasmic reticulum subfractions isolated from L-929 cells</title><author>Pryme, Ian F. ; Hesketh, John E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c386t-d91135503904a3aa5abaa3913eb45b3ff96d3888869b0bd6d5c095fd09e97983</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1987</creationdate><topic>Actins - metabolism</topic><topic>Animals</topic><topic>Antibodies, Monoclonal</topic><topic>Biological and medical sciences</topic><topic>Cell structures and functions</topic><topic>Cytochalasin B - metabolism</topic><topic>Cytoskeleton, cytoplasm. Intracellular movements</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Endoplasmic Reticulum - physiology</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Intracellular Membranes - metabolism</topic><topic>L Cells (Cell Line)</topic><topic>Mice</topic><topic>Molecular and cellular biology</topic><topic>Subcellular Fractions - metabolism</topic><toplevel>online_resources</toplevel><creatorcontrib>Pryme, Ian F.</creatorcontrib><creatorcontrib>Hesketh, John E.</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>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Cell biology international reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pryme, Ian F.</au><au>Hesketh, John E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Cytochalasin B binding and actin content of endoplasmic reticulum subfractions isolated from L-929 cells</atitle><jtitle>Cell biology international reports</jtitle><addtitle>Cell Biol Int Rep</addtitle><date>1987-08-01</date><risdate>1987</risdate><volume>11</volume><issue>8</issue><spage>615</spage><epage>623</epage><pages>615-623</pages><issn>0309-1651</issn><eissn>1878-240X</eissn><coden>CBRPDS</coden><abstract>Heavy rough (HR) endoplasmic reticulum (ER) membranes and a dense fraction of light rough (LR) membranes (LR I) of L-929 cells bind
3H-cytochalasin B extremely poorly in comparison to smooth (S) membranes and a fraction of LR membranes of low density (LR II). The LR and S subfractions of ER are apparently heterogeneous membrane populations with respect to cytochalasin B binding. The separation of proteins in HR and LR subfractions by electrophoresis followed by immunoblotting with monoclonal antibodies against actin showed that actin was not present in the former membranes while there were large amounts in the LR subfraction. It is concluded that membranes in the LR II fraction of ER are associated with actin-containing microfilaments of the cytoskeleton, but that HR membranes are not.</abstract><cop>London</cop><cop>San Diego, CA</cop><cop>New York, NY</cop><pub>Elsevier B.V</pub><pmid>3621359</pmid><doi>10.1016/0309-1651(87)90142-1</doi><tpages>9</tpages></addata></record> |
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| ispartof | Cell biology international reports, 1987-08, Vol.11 (8), p.615-623 |
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| source | MEDLINE; Alma/SFX Local Collection |
| subjects | Actins - metabolism Animals Antibodies, Monoclonal Biological and medical sciences Cell structures and functions Cytochalasin B - metabolism Cytoskeleton, cytoplasm. Intracellular movements Electrophoresis, Polyacrylamide Gel Endoplasmic Reticulum - physiology Fundamental and applied biological sciences. Psychology Intracellular Membranes - metabolism L Cells (Cell Line) Mice Molecular and cellular biology Subcellular Fractions - metabolism |
| title | Cytochalasin B binding and actin content of endoplasmic reticulum subfractions isolated from L-929 cells |
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