Complement proteins C5b-9 induce transbilayer migration of membrane phospholipids
Transbilayer migration of membrane phospholipid arising from membrane insertion of the terminal human complement proteins has been investigated. Asymmetric vesicles containing pyrene-labeled phosphatidylcholine (pyrenePC) concentrated in the inner monolayer were prepared by outer monolayer exchange...
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| Veröffentlicht in: | Biophysical journal 1989-11, Vol.56 (5), p.935-946 |
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| creator | Van der Meer, B.W. Fugate, R.D. Sims, P.J. |
| description | Transbilayer migration of membrane phospholipid arising from membrane insertion of the terminal human complement proteins has been investigated. Asymmetric vesicles containing pyrene-labeled phosphatidylcholine (pyrenePC) concentrated in the inner monolayer were prepared by outer monolayer exchange between pyrenePC-containing large unilamellar vesicles and excess (unlabeled) small unilamellar vesicles, using bovine liver phosphatidylcholine-specific exchange protein. After depletion of pyrenePC from the outer monolayer, the asymmetric large unilamellar vesicles were isolated by gel filtration and exposed to the purified C5b-9 proteins at 37 degrees C. Transbilayer exchange of phospholipid between inner and outer monolayers during C5b-9 assembly was monitored by changes in pyrene excimer and monomer fluorescence. Membrane deposition of the C5b67 complex (by incubation with C5b6 + C7) caused no change in pyrenePC fluorescence. Addition of C8 to the C5b67 vesicles resulted in a dose-dependent decrease in the excimer/monomer ratio. This change was observed both in the presence and absence of complement C9. No change in fluorescence was observed for control vesicles exposed to C8 (in the absence of membrane C5b67), or upon C5b-9 addition to vesicles containing pyrenePC symmetrically distributed between inner and outer monolayers. These data suggest that a transbilayer exchange of phospholipid between inner and outer monolayers is initiated upon C8 binding to C5b67. The fluorescence data were analyzed according to a "random walk" model for excimer formation developed for the case where pyrenePC is asymmetrically distributed between lipid bilayers. Based on this analysis, we estimate that a net transbilayer migration of approximately 1% of total membrane phospholipid is initiated upon C8 binding to C5b67. The potential significance of this transbilayer exchange of membrane phospholipid to the biological activity of the terminal complement proteins is considered. |
| doi_str_mv | 10.1016/S0006-3495(89)82739-0 |
| format | Article |
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Asymmetric vesicles containing pyrene-labeled phosphatidylcholine (pyrenePC) concentrated in the inner monolayer were prepared by outer monolayer exchange between pyrenePC-containing large unilamellar vesicles and excess (unlabeled) small unilamellar vesicles, using bovine liver phosphatidylcholine-specific exchange protein. After depletion of pyrenePC from the outer monolayer, the asymmetric large unilamellar vesicles were isolated by gel filtration and exposed to the purified C5b-9 proteins at 37 degrees C. Transbilayer exchange of phospholipid between inner and outer monolayers during C5b-9 assembly was monitored by changes in pyrene excimer and monomer fluorescence. Membrane deposition of the C5b67 complex (by incubation with C5b6 + C7) caused no change in pyrenePC fluorescence. Addition of C8 to the C5b67 vesicles resulted in a dose-dependent decrease in the excimer/monomer ratio. This change was observed both in the presence and absence of complement C9. No change in fluorescence was observed for control vesicles exposed to C8 (in the absence of membrane C5b67), or upon C5b-9 addition to vesicles containing pyrenePC symmetrically distributed between inner and outer monolayers. These data suggest that a transbilayer exchange of phospholipid between inner and outer monolayers is initiated upon C8 binding to C5b67. The fluorescence data were analyzed according to a "random walk" model for excimer formation developed for the case where pyrenePC is asymmetrically distributed between lipid bilayers. Based on this analysis, we estimate that a net transbilayer migration of approximately 1% of total membrane phospholipid is initiated upon C8 binding to C5b67. The potential significance of this transbilayer exchange of membrane phospholipid to the biological activity of the terminal complement proteins is considered.</description><identifier>ISSN: 0006-3495</identifier><identifier>EISSN: 1542-0086</identifier><identifier>DOI: 10.1016/S0006-3495(89)82739-0</identifier><identifier>PMID: 2605304</identifier><identifier>CODEN: BIOJAU</identifier><language>eng</language><publisher>Bethesda, MD: Elsevier Inc</publisher><subject>Androgen-Binding Protein ; Artificial membranes and reconstituted systems ; Biological and medical sciences ; Carrier Proteins - metabolism ; Complement Membrane Attack Complex - metabolism ; Complement System Proteins - isolation & purification ; Complement System Proteins - metabolism ; Fundamental and applied biological sciences. Psychology ; Humans ; Kinetics ; Lipid Bilayers ; Liposomes ; Mathematics ; Membrane physicochemistry ; Models, Theoretical ; Molecular biophysics ; Phosphatidylcholines - metabolism ; Phosphatidylethanolamine Binding Protein ; Phospholipid Transfer Proteins ; Spectrometry, Fluorescence</subject><ispartof>Biophysical journal, 1989-11, Vol.56 (5), p.935-946</ispartof><rights>1989 The Biophysical Society</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c523t-307a4e317440914e90dd5b31a661b21175170c842e70fa55d4efec9eb67333643</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC1280592/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006349589827390$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,881,3537,27901,27902,53766,53768,65306</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=19459835$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2605304$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Van der Meer, B.W.</creatorcontrib><creatorcontrib>Fugate, R.D.</creatorcontrib><creatorcontrib>Sims, P.J.</creatorcontrib><title>Complement proteins C5b-9 induce transbilayer migration of membrane phospholipids</title><title>Biophysical journal</title><addtitle>Biophys J</addtitle><description>Transbilayer migration of membrane phospholipid arising from membrane insertion of the terminal human complement proteins has been investigated. Asymmetric vesicles containing pyrene-labeled phosphatidylcholine (pyrenePC) concentrated in the inner monolayer were prepared by outer monolayer exchange between pyrenePC-containing large unilamellar vesicles and excess (unlabeled) small unilamellar vesicles, using bovine liver phosphatidylcholine-specific exchange protein. After depletion of pyrenePC from the outer monolayer, the asymmetric large unilamellar vesicles were isolated by gel filtration and exposed to the purified C5b-9 proteins at 37 degrees C. Transbilayer exchange of phospholipid between inner and outer monolayers during C5b-9 assembly was monitored by changes in pyrene excimer and monomer fluorescence. Membrane deposition of the C5b67 complex (by incubation with C5b6 + C7) caused no change in pyrenePC fluorescence. Addition of C8 to the C5b67 vesicles resulted in a dose-dependent decrease in the excimer/monomer ratio. This change was observed both in the presence and absence of complement C9. No change in fluorescence was observed for control vesicles exposed to C8 (in the absence of membrane C5b67), or upon C5b-9 addition to vesicles containing pyrenePC symmetrically distributed between inner and outer monolayers. These data suggest that a transbilayer exchange of phospholipid between inner and outer monolayers is initiated upon C8 binding to C5b67. The fluorescence data were analyzed according to a "random walk" model for excimer formation developed for the case where pyrenePC is asymmetrically distributed between lipid bilayers. Based on this analysis, we estimate that a net transbilayer migration of approximately 1% of total membrane phospholipid is initiated upon C8 binding to C5b67. The potential significance of this transbilayer exchange of membrane phospholipid to the biological activity of the terminal complement proteins is considered.</description><subject>Androgen-Binding Protein</subject><subject>Artificial membranes and reconstituted systems</subject><subject>Biological and medical sciences</subject><subject>Carrier Proteins - metabolism</subject><subject>Complement Membrane Attack Complex - metabolism</subject><subject>Complement System Proteins - isolation & purification</subject><subject>Complement System Proteins - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Humans</subject><subject>Kinetics</subject><subject>Lipid Bilayers</subject><subject>Liposomes</subject><subject>Mathematics</subject><subject>Membrane physicochemistry</subject><subject>Models, Theoretical</subject><subject>Molecular biophysics</subject><subject>Phosphatidylcholines - metabolism</subject><subject>Phosphatidylethanolamine Binding Protein</subject><subject>Phospholipid Transfer Proteins</subject><subject>Spectrometry, Fluorescence</subject><issn>0006-3495</issn><issn>1542-0086</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1989</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFUU1v1DAQtRCoLIWfUCkXEBwCM_5KfAGhFV9SJYSAs-U4k9YoiYOdrdR_j7e7WuDUw2gO782befMYu0B4jYD6zXcA0LWQRr1szauWN8LU8IBtUEleA7T6IducKI_Zk5x_ASBXgGfsjGtQAuSGfdvGaRlponmtlhRXCnOutqqrTRXmfuepWpObcxdGd0upmsJVcmuIcxWHaqKpKyBVy3XMpcawhD4_ZY8GN2Z6duzn7OfHDz-2n-vLr5--bN9f1l5xsdYCGidJYCMlGJRkoO9VJ9BpjR1HbBQ24FvJqYHBKdVLGsgb6nQjhNBSnLO3B91l103U--IgudEuKUwu3drogv0fmcO1vYo3FnkLyvAi8OIokOLvHeXVTiF7GsdiKe6ybYxEqcHcS0SllJFqr6gORJ9izomG0zUIdh-avQvN7hOxrbF3oVkocxf_WjlNHVMq-PMj7rJ341Ce7kP-K16Wm1aownt34FH5-02gZLMPNHvqQyK_2j6Gey75A2nLtCY</recordid><startdate>19891101</startdate><enddate>19891101</enddate><creator>Van der Meer, B.W.</creator><creator>Fugate, R.D.</creator><creator>Sims, P.J.</creator><general>Elsevier Inc</general><general>Biophysical Society</general><scope>6I.</scope><scope>AAFTH</scope><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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>19891101</creationdate><title>Complement proteins C5b-9 induce transbilayer migration of membrane phospholipids</title><author>Van der Meer, B.W. ; Fugate, R.D. ; Sims, P.J.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c523t-307a4e317440914e90dd5b31a661b21175170c842e70fa55d4efec9eb67333643</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1989</creationdate><topic>Androgen-Binding Protein</topic><topic>Artificial membranes and reconstituted systems</topic><topic>Biological and medical sciences</topic><topic>Carrier Proteins - metabolism</topic><topic>Complement Membrane Attack Complex - metabolism</topic><topic>Complement System Proteins - isolation & purification</topic><topic>Complement System Proteins - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Humans</topic><topic>Kinetics</topic><topic>Lipid Bilayers</topic><topic>Liposomes</topic><topic>Mathematics</topic><topic>Membrane physicochemistry</topic><topic>Models, Theoretical</topic><topic>Molecular biophysics</topic><topic>Phosphatidylcholines - metabolism</topic><topic>Phosphatidylethanolamine Binding Protein</topic><topic>Phospholipid Transfer Proteins</topic><topic>Spectrometry, Fluorescence</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Van der Meer, B.W.</creatorcontrib><creatorcontrib>Fugate, R.D.</creatorcontrib><creatorcontrib>Sims, P.J.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><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>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Biophysical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Van der Meer, B.W.</au><au>Fugate, R.D.</au><au>Sims, P.J.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Complement proteins C5b-9 induce transbilayer migration of membrane phospholipids</atitle><jtitle>Biophysical journal</jtitle><addtitle>Biophys J</addtitle><date>1989-11-01</date><risdate>1989</risdate><volume>56</volume><issue>5</issue><spage>935</spage><epage>946</epage><pages>935-946</pages><issn>0006-3495</issn><eissn>1542-0086</eissn><coden>BIOJAU</coden><abstract>Transbilayer migration of membrane phospholipid arising from membrane insertion of the terminal human complement proteins has been investigated. Asymmetric vesicles containing pyrene-labeled phosphatidylcholine (pyrenePC) concentrated in the inner monolayer were prepared by outer monolayer exchange between pyrenePC-containing large unilamellar vesicles and excess (unlabeled) small unilamellar vesicles, using bovine liver phosphatidylcholine-specific exchange protein. After depletion of pyrenePC from the outer monolayer, the asymmetric large unilamellar vesicles were isolated by gel filtration and exposed to the purified C5b-9 proteins at 37 degrees C. Transbilayer exchange of phospholipid between inner and outer monolayers during C5b-9 assembly was monitored by changes in pyrene excimer and monomer fluorescence. Membrane deposition of the C5b67 complex (by incubation with C5b6 + C7) caused no change in pyrenePC fluorescence. Addition of C8 to the C5b67 vesicles resulted in a dose-dependent decrease in the excimer/monomer ratio. This change was observed both in the presence and absence of complement C9. No change in fluorescence was observed for control vesicles exposed to C8 (in the absence of membrane C5b67), or upon C5b-9 addition to vesicles containing pyrenePC symmetrically distributed between inner and outer monolayers. These data suggest that a transbilayer exchange of phospholipid between inner and outer monolayers is initiated upon C8 binding to C5b67. The fluorescence data were analyzed according to a "random walk" model for excimer formation developed for the case where pyrenePC is asymmetrically distributed between lipid bilayers. Based on this analysis, we estimate that a net transbilayer migration of approximately 1% of total membrane phospholipid is initiated upon C8 binding to C5b67. The potential significance of this transbilayer exchange of membrane phospholipid to the biological activity of the terminal complement proteins is considered.</abstract><cop>Bethesda, MD</cop><pub>Elsevier Inc</pub><pmid>2605304</pmid><doi>10.1016/S0006-3495(89)82739-0</doi><tpages>12</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Biophysical journal, 1989-11, Vol.56 (5), p.935-946 |
| issn | 0006-3495 1542-0086 |
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| source | MEDLINE; Cell Press Free Archives; Elsevier ScienceDirect Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Androgen-Binding Protein Artificial membranes and reconstituted systems Biological and medical sciences Carrier Proteins - metabolism Complement Membrane Attack Complex - metabolism Complement System Proteins - isolation & purification Complement System Proteins - metabolism Fundamental and applied biological sciences. Psychology Humans Kinetics Lipid Bilayers Liposomes Mathematics Membrane physicochemistry Models, Theoretical Molecular biophysics Phosphatidylcholines - metabolism Phosphatidylethanolamine Binding Protein Phospholipid Transfer Proteins Spectrometry, Fluorescence |
| title | Complement proteins C5b-9 induce transbilayer migration of membrane phospholipids |
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