Connexins and the vacuolar proteolipid-like 16-kDa protein are not directly associated with each other but may be components of similar or the same gap junctional complexes
Gap junction preparations made from mouse liver plasma membranes by alkali extraction contain variable proportions of connexins (Cx32 and Cx26) and the 16-kDa protein which is closely related or may be identical to the 16-kDa proteolipid (subunit c) of the vacuolar H +-ATPase and the mediatophore co...
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| Veröffentlicht in: | Experimental cell research 1992-11, Vol.203 (1), p.280-284 |
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| creator | Finbow, Malcolm E. Meagher, Liam |
| description | Gap junction preparations made from mouse liver plasma membranes by alkali extraction contain variable proportions of connexins (Cx32 and Cx26) and the 16-kDa protein which is closely related or may be identical to the 16-kDa proteolipid (subunit c) of the vacuolar H
+-ATPase and the mediatophore complex. The absence of a stoichiometric relationship suggests that connexins and the 16-kDa protein are not subunits of the same channel complex, but analysis of alkali preparations by isopycnic centrifugation shows both types of protein are in membrane structures of the same buoyant density. Electron microscopic analysis of alkali preparations shows a homogeneous population of gap junctions of uniform morphology and width, suggesting the proteins are in the same or similar structures. The structures containing connexins and the 16-kDa protein can be separated by treatment of the plasma membranes with Triton X-100. After such treatment, the connexins remain associated with dense cellular or extracellular material and the gap junctional structures, after further extraction with
N-lauroyl sarcosine and urea, contain only the 16-kDa protein. These detergent-extracted gap junctions are thinner (14.1 nm) than those in alkali preparations (18.4 nm). |
| doi_str_mv | 10.1016/0014-4827(92)90066-H |
| format | Article |
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+-ATPase and the mediatophore complex. The absence of a stoichiometric relationship suggests that connexins and the 16-kDa protein are not subunits of the same channel complex, but analysis of alkali preparations by isopycnic centrifugation shows both types of protein are in membrane structures of the same buoyant density. Electron microscopic analysis of alkali preparations shows a homogeneous population of gap junctions of uniform morphology and width, suggesting the proteins are in the same or similar structures. The structures containing connexins and the 16-kDa protein can be separated by treatment of the plasma membranes with Triton X-100. After such treatment, the connexins remain associated with dense cellular or extracellular material and the gap junctional structures, after further extraction with
N-lauroyl sarcosine and urea, contain only the 16-kDa protein. These detergent-extracted gap junctions are thinner (14.1 nm) than those in alkali preparations (18.4 nm).</description><identifier>ISSN: 0014-4827</identifier><identifier>EISSN: 1090-2422</identifier><identifier>DOI: 10.1016/0014-4827(92)90066-H</identifier><identifier>PMID: 1330657</identifier><identifier>CODEN: ECREAL</identifier><language>eng</language><publisher>Orlando, FL: Elsevier Inc</publisher><subject>Animals ; Biological and medical sciences ; Cell Fractionation - methods ; Cell interactions, adhesion ; Cell Membrane - ultrastructure ; Connexins ; Detergents ; Electrophoresis, Gel, Two-Dimensional ; Electrophoresis, Polyacrylamide Gel ; Fundamental and applied biological sciences. Psychology ; Intercellular Junctions - chemistry ; Intercellular Junctions - ultrastructure ; Liver - chemistry ; Liver - ultrastructure ; Macromolecular Substances ; Membrane Proteins - analysis ; Membrane Proteins - isolation & purification ; Mice ; Microscopy, Electron ; Molecular and cellular biology ; Molecular Weight ; Octoxynol ; Peptide Mapping ; Polyethylene Glycols ; Proteolipids - analysis ; Proton-Translocating ATPases - analysis ; Vacuoles - chemistry ; Vacuoles - ultrastructure</subject><ispartof>Experimental cell research, 1992-11, Vol.203 (1), p.280-284</ispartof><rights>1992</rights><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c437t-8e5627cf841baea6fdd9324bb32533f89e28047ed88d2fca081b6f8cab377e453</citedby><cites>FETCH-LOGICAL-c437t-8e5627cf841baea6fdd9324bb32533f89e28047ed88d2fca081b6f8cab377e453</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0014-4827(92)90066-H$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4452132$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1330657$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Finbow, Malcolm E.</creatorcontrib><creatorcontrib>Meagher, Liam</creatorcontrib><title>Connexins and the vacuolar proteolipid-like 16-kDa protein are not directly associated with each other but may be components of similar or the same gap junctional complexes</title><title>Experimental cell research</title><addtitle>Exp Cell Res</addtitle><description>Gap junction preparations made from mouse liver plasma membranes by alkali extraction contain variable proportions of connexins (Cx32 and Cx26) and the 16-kDa protein which is closely related or may be identical to the 16-kDa proteolipid (subunit c) of the vacuolar H
+-ATPase and the mediatophore complex. The absence of a stoichiometric relationship suggests that connexins and the 16-kDa protein are not subunits of the same channel complex, but analysis of alkali preparations by isopycnic centrifugation shows both types of protein are in membrane structures of the same buoyant density. Electron microscopic analysis of alkali preparations shows a homogeneous population of gap junctions of uniform morphology and width, suggesting the proteins are in the same or similar structures. The structures containing connexins and the 16-kDa protein can be separated by treatment of the plasma membranes with Triton X-100. After such treatment, the connexins remain associated with dense cellular or extracellular material and the gap junctional structures, after further extraction with
N-lauroyl sarcosine and urea, contain only the 16-kDa protein. These detergent-extracted gap junctions are thinner (14.1 nm) than those in alkali preparations (18.4 nm).</description><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Fractionation - methods</subject><subject>Cell interactions, adhesion</subject><subject>Cell Membrane - ultrastructure</subject><subject>Connexins</subject><subject>Detergents</subject><subject>Electrophoresis, Gel, Two-Dimensional</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Intercellular Junctions - chemistry</subject><subject>Intercellular Junctions - ultrastructure</subject><subject>Liver - chemistry</subject><subject>Liver - ultrastructure</subject><subject>Macromolecular Substances</subject><subject>Membrane Proteins - analysis</subject><subject>Membrane Proteins - isolation & purification</subject><subject>Mice</subject><subject>Microscopy, Electron</subject><subject>Molecular and cellular biology</subject><subject>Molecular Weight</subject><subject>Octoxynol</subject><subject>Peptide Mapping</subject><subject>Polyethylene Glycols</subject><subject>Proteolipids - analysis</subject><subject>Proton-Translocating ATPases - analysis</subject><subject>Vacuoles - chemistry</subject><subject>Vacuoles - ultrastructure</subject><issn>0014-4827</issn><issn>1090-2422</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp9kcuO1DAQRS0EGpqBPwDJC4RgEfAribNBQs2jkUZiA2ur4lRozyR2sJ1h-p_4SNKd1rBjZcl1bpVdh5DnnL3ljFfvGOOqUFrUrxvxpmGsqordA7LhrGGFUEI8JJt75DF5ktI1Y0xrXl2QCy4lq8p6Q_5sg_d453yi4Dua90hvwc5hgEinGDKGwU2uKwZ3g5RXxc1HWO-dpxCR-pBp5yLaPBwopBSsg4wd_e3yniLYPQ1Lz0jbOdMRDrRFasM4BY8-Jxp6mtzojsNCPA1PMCL9CRO9nr3NLngYToEB7zA9JY96GBI-O5-X5MfnT9-3u-Lq25ev2w9XhVWyzoXGshK17bXiLSBUfdc1Uqi2laKUstcNCs1UjZ3WnegtMM3bqtcWWlnXqEp5SV6tfZef_poxZTO6ZHEYwGOYk6mX7dVaVguoVtDGkFLE3kzRjRAPhjNzlGSOBszRgGmEOUkyuyX24tx_bkfs_oVWK0v95bkOycLQR_DWpXtMqVJwKRbs_Yrhsotbh9Ek69BbXIWYLrj_v-MvMvOxKw</recordid><startdate>19921101</startdate><enddate>19921101</enddate><creator>Finbow, Malcolm E.</creator><creator>Meagher, Liam</creator><general>Elsevier Inc</general><general>Elsevier</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>19921101</creationdate><title>Connexins and the vacuolar proteolipid-like 16-kDa protein are not directly associated with each other but may be components of similar or the same gap junctional complexes</title><author>Finbow, Malcolm E. ; Meagher, Liam</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c437t-8e5627cf841baea6fdd9324bb32533f89e28047ed88d2fca081b6f8cab377e453</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Fractionation - methods</topic><topic>Cell interactions, adhesion</topic><topic>Cell Membrane - ultrastructure</topic><topic>Connexins</topic><topic>Detergents</topic><topic>Electrophoresis, Gel, Two-Dimensional</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Intercellular Junctions - chemistry</topic><topic>Intercellular Junctions - ultrastructure</topic><topic>Liver - chemistry</topic><topic>Liver - ultrastructure</topic><topic>Macromolecular Substances</topic><topic>Membrane Proteins - analysis</topic><topic>Membrane Proteins - isolation & purification</topic><topic>Mice</topic><topic>Microscopy, Electron</topic><topic>Molecular and cellular biology</topic><topic>Molecular Weight</topic><topic>Octoxynol</topic><topic>Peptide Mapping</topic><topic>Polyethylene Glycols</topic><topic>Proteolipids - analysis</topic><topic>Proton-Translocating ATPases - analysis</topic><topic>Vacuoles - chemistry</topic><topic>Vacuoles - ultrastructure</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Finbow, Malcolm E.</creatorcontrib><creatorcontrib>Meagher, Liam</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>Experimental cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Finbow, Malcolm E.</au><au>Meagher, Liam</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Connexins and the vacuolar proteolipid-like 16-kDa protein are not directly associated with each other but may be components of similar or the same gap junctional complexes</atitle><jtitle>Experimental cell research</jtitle><addtitle>Exp Cell Res</addtitle><date>1992-11-01</date><risdate>1992</risdate><volume>203</volume><issue>1</issue><spage>280</spage><epage>284</epage><pages>280-284</pages><issn>0014-4827</issn><eissn>1090-2422</eissn><coden>ECREAL</coden><abstract>Gap junction preparations made from mouse liver plasma membranes by alkali extraction contain variable proportions of connexins (Cx32 and Cx26) and the 16-kDa protein which is closely related or may be identical to the 16-kDa proteolipid (subunit c) of the vacuolar H
+-ATPase and the mediatophore complex. The absence of a stoichiometric relationship suggests that connexins and the 16-kDa protein are not subunits of the same channel complex, but analysis of alkali preparations by isopycnic centrifugation shows both types of protein are in membrane structures of the same buoyant density. Electron microscopic analysis of alkali preparations shows a homogeneous population of gap junctions of uniform morphology and width, suggesting the proteins are in the same or similar structures. The structures containing connexins and the 16-kDa protein can be separated by treatment of the plasma membranes with Triton X-100. After such treatment, the connexins remain associated with dense cellular or extracellular material and the gap junctional structures, after further extraction with
N-lauroyl sarcosine and urea, contain only the 16-kDa protein. These detergent-extracted gap junctions are thinner (14.1 nm) than those in alkali preparations (18.4 nm).</abstract><cop>Orlando, FL</cop><pub>Elsevier Inc</pub><pmid>1330657</pmid><doi>10.1016/0014-4827(92)90066-H</doi><tpages>5</tpages></addata></record> |
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| subjects | Animals Biological and medical sciences Cell Fractionation - methods Cell interactions, adhesion Cell Membrane - ultrastructure Connexins Detergents Electrophoresis, Gel, Two-Dimensional Electrophoresis, Polyacrylamide Gel Fundamental and applied biological sciences. Psychology Intercellular Junctions - chemistry Intercellular Junctions - ultrastructure Liver - chemistry Liver - ultrastructure Macromolecular Substances Membrane Proteins - analysis Membrane Proteins - isolation & purification Mice Microscopy, Electron Molecular and cellular biology Molecular Weight Octoxynol Peptide Mapping Polyethylene Glycols Proteolipids - analysis Proton-Translocating ATPases - analysis Vacuoles - chemistry Vacuoles - ultrastructure |
| title | Connexins and the vacuolar proteolipid-like 16-kDa protein are not directly associated with each other but may be components of similar or the same gap junctional complexes |
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