Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis
Voltage-dependent anion channel （VDAC）I is the main channel of the mitochondrial outer membrane （MOM） and it has been proposed to be part of the permeability transition pore （PTP）, a putative multiprotein complex candidate agent of the mitochondrial permeability transition （MPT）. Working at the sing...
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| Veröffentlicht in: | Cell research 2009-12, Vol.19 (12), p.1363-1376 |
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| creator | Tomasello, Flora Messina, Angela Lartigue, Lydia Schembri, Laura Medina, Chantal Reina, Simona Thoraval, Didier Crouzet, Marc Ichas, François De Pinto, Vito De Giorgi, Francesca |
| description | Voltage-dependent anion channel （VDAC）I is the main channel of the mitochondrial outer membrane （MOM） and it has been proposed to be part of the permeability transition pore （PTP）, a putative multiprotein complex candidate agent of the mitochondrial permeability transition （MPT）. Working at the single live cell level, we found that overexpression of VDAC1 triggers MPT at the mitochondrial inner membrane （MIM）. Conversely, silencing VDAC1 ex- pression results in the inhibition of MPT caused by selenite-induced oxidative stress. This MOM-MIM crosstalk was modulated by Cyclosporin A and mitochondrial Cyclophilin D, but not by Bcl-2 and BcI-XL, indicative of PTP operation. VDAC1-dependent MPT engages a positive feedback loop involving reactive oxygen species and p38-MAPK, and secondarily triggers a canonical apoptotic response including Bax activation, cytochrome e release and caspase 3 activation. Our data thus support a model of the PTP complex involving VDAC1 at the MOM, and indicate that VDACl-dependent MPT is an upstream mechanism playing a causal role in oxidative stress-induced apoptosis. |
| doi_str_mv | 10.1038/cr.2009.98 |
| format | Article |
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Working at the single live cell level, we found that overexpression of VDAC1 triggers MPT at the mitochondrial inner membrane （MIM）. Conversely, silencing VDAC1 ex- pression results in the inhibition of MPT caused by selenite-induced oxidative stress. This MOM-MIM crosstalk was modulated by Cyclosporin A and mitochondrial Cyclophilin D, but not by Bcl-2 and BcI-XL, indicative of PTP operation. VDAC1-dependent MPT engages a positive feedback loop involving reactive oxygen species and p38-MAPK, and secondarily triggers a canonical apoptotic response including Bax activation, cytochrome e release and caspase 3 activation. Our data thus support a model of the PTP complex involving VDAC1 at the MOM, and indicate that VDACl-dependent MPT is an upstream mechanism playing a causal role in oxidative stress-induced apoptosis.</description><identifier>ISSN: 1001-0602</identifier><identifier>EISSN: 1748-7838</identifier><identifier>DOI: 10.1038/cr.2009.98</identifier><identifier>PMID: 19668262</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Animals ; Apoptosis Regulatory Proteins - metabolism ; Biomedical and Life Sciences ; caspase ; Cell Biology ; Cell Membrane Permeability - physiology ; Chlorocebus aethiops ; COS Cells ; Cyclophilins - pharmacology ; Cyclosporine - pharmacology ; Cytochrome ; Feedback, Physiological - physiology ; Gene Silencing - physiology ; HeLa Cells ; Humans ; Life Sciences ; Membrane Potential, Mitochondrial - physiology ; Membranes ; Mitochondrial Membranes - metabolism ; original-article ; Oxidative stress ; Oxidative Stress - drug effects ; Oxidative Stress - physiology ; p38蛋白激酶 ; Peptidyl-Prolyl Isomerase F ; Permeability ; Sodium Selenite - pharmacology ; Stress, Physiological - physiology ; Upstream ; Voltage-Dependent Anion Channel 1 - genetics ; Voltage-Dependent Anion Channel 1 - metabolism ; 微波等离子体炬 ; 线粒体膜 ; 细胞凋亡 ; 膜通透性 ; 蛋白质复合体</subject><ispartof>Cell research, 2009-12, Vol.19 (12), p.1363-1376</ispartof><rights>Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences 2009</rights><rights>Copyright Nature Publishing Group Dec 2009</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c479t-806eed391c22c4b14ff3feb0953a8ec2e0188a618d17447b0febe6b5c5b204203</citedby><cites>FETCH-LOGICAL-c479t-806eed391c22c4b14ff3feb0953a8ec2e0188a618d17447b0febe6b5c5b204203</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Uhttp://image.cqvip.com/vip1000/qk/85240X/85240X.jpg</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/cr.2009.98$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/cr.2009.98$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,776,780,27901,27902,41464,42533,51294</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/19668262$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Tomasello, Flora</creatorcontrib><creatorcontrib>Messina, Angela</creatorcontrib><creatorcontrib>Lartigue, Lydia</creatorcontrib><creatorcontrib>Schembri, Laura</creatorcontrib><creatorcontrib>Medina, Chantal</creatorcontrib><creatorcontrib>Reina, Simona</creatorcontrib><creatorcontrib>Thoraval, Didier</creatorcontrib><creatorcontrib>Crouzet, Marc</creatorcontrib><creatorcontrib>Ichas, François</creatorcontrib><creatorcontrib>De Pinto, Vito</creatorcontrib><creatorcontrib>De Giorgi, Francesca</creatorcontrib><title>Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis</title><title>Cell research</title><addtitle>Cell Res</addtitle><addtitle>Cell Research</addtitle><description>Voltage-dependent anion channel （VDAC）I is the main channel of the mitochondrial outer membrane （MOM） and it has been proposed to be part of the permeability transition pore （PTP）, a putative multiprotein complex candidate agent of the mitochondrial permeability transition （MPT）. Working at the single live cell level, we found that overexpression of VDAC1 triggers MPT at the mitochondrial inner membrane （MIM）. Conversely, silencing VDAC1 ex- pression results in the inhibition of MPT caused by selenite-induced oxidative stress. This MOM-MIM crosstalk was modulated by Cyclosporin A and mitochondrial Cyclophilin D, but not by Bcl-2 and BcI-XL, indicative of PTP operation. VDAC1-dependent MPT engages a positive feedback loop involving reactive oxygen species and p38-MAPK, and secondarily triggers a canonical apoptotic response including Bax activation, cytochrome e release and caspase 3 activation. Our data thus support a model of the PTP complex involving VDAC1 at the MOM, and indicate that VDACl-dependent MPT is an upstream mechanism playing a causal role in oxidative stress-induced apoptosis.</description><subject>Animals</subject><subject>Apoptosis Regulatory Proteins - metabolism</subject><subject>Biomedical and Life Sciences</subject><subject>caspase</subject><subject>Cell Biology</subject><subject>Cell Membrane Permeability - physiology</subject><subject>Chlorocebus aethiops</subject><subject>COS Cells</subject><subject>Cyclophilins - pharmacology</subject><subject>Cyclosporine - pharmacology</subject><subject>Cytochrome</subject><subject>Feedback, Physiological - physiology</subject><subject>Gene Silencing - physiology</subject><subject>HeLa Cells</subject><subject>Humans</subject><subject>Life Sciences</subject><subject>Membrane Potential, Mitochondrial - physiology</subject><subject>Membranes</subject><subject>Mitochondrial Membranes - metabolism</subject><subject>original-article</subject><subject>Oxidative stress</subject><subject>Oxidative Stress - drug effects</subject><subject>Oxidative Stress - physiology</subject><subject>p38蛋白激酶</subject><subject>Peptidyl-Prolyl Isomerase F</subject><subject>Permeability</subject><subject>Sodium Selenite - pharmacology</subject><subject>Stress, Physiological - physiology</subject><subject>Upstream</subject><subject>Voltage-Dependent Anion Channel 1 - genetics</subject><subject>Voltage-Dependent Anion Channel 1 - metabolism</subject><subject>微波等离子体炬</subject><subject>线粒体膜</subject><subject>细胞凋亡</subject><subject>膜通透性</subject><subject>蛋白质复合体</subject><issn>1001-0602</issn><issn>1748-7838</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2009</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNptkUtv1TAUhC0Eog_Y8AOQBQskUC5-xXGW1aU8pErdAFvLdk5al8RObWfRPT8cR_dKRYiVLfk7c8YzCL2iZEcJVx9d2jFC-l2vnqBT2gnVdIqrp_VOCG2IJOwEneV8RwhrRUufoxPaS6mYZKfo9_VaIOEZZptMAPzz08WeYhdDSXHKeIE0g7F-8uUBl0pkX3wMOI643AL2IWzDvkR3G8OQvJkepXzADqZpnSIe1uTDDc4lQc6ND8PqYMBmiUuJ2ecX6Nlopgwvj-c5-vH58vv-a3N1_eXb_uKqcaLrS6OIBBh4Tx1jTlgqxpGPYEnfcqPAMSBUKSOpGmoIorOkPoK0rWstI4IRfo7eHXSXFO9XyEXPPm8eq924Zt1xQWUnZFfJt_-Qd3FNoZrTlLCuFbLtN733B8qlmHOCUS_JzyY9VEhv1WiX9FaN7lWFXx8lVzvD8Igeu6jAhwOQly0tSH_v_I_cm-PumvzNfR3Q1rhfo59AcyZ4_bDkfwAt3KUk</recordid><startdate>20091201</startdate><enddate>20091201</enddate><creator>Tomasello, Flora</creator><creator>Messina, Angela</creator><creator>Lartigue, Lydia</creator><creator>Schembri, Laura</creator><creator>Medina, Chantal</creator><creator>Reina, Simona</creator><creator>Thoraval, Didier</creator><creator>Crouzet, Marc</creator><creator>Ichas, François</creator><creator>De Pinto, Vito</creator><creator>De Giorgi, Francesca</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>2RA</scope><scope>92L</scope><scope>CQIGP</scope><scope>W94</scope><scope>WU4</scope><scope>~WA</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>3V.</scope><scope>7QO</scope><scope>7QP</scope><scope>7QR</scope><scope>7T5</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X7</scope><scope>7XB</scope><scope>88E</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M7N</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>RC3</scope><scope>7X8</scope></search><sort><creationdate>20091201</creationdate><title>Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis</title><author>Tomasello, Flora ; Messina, Angela ; Lartigue, Lydia ; Schembri, Laura ; Medina, Chantal ; Reina, Simona ; Thoraval, Didier ; Crouzet, Marc ; Ichas, François ; De Pinto, Vito ; De Giorgi, Francesca</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c479t-806eed391c22c4b14ff3feb0953a8ec2e0188a618d17447b0febe6b5c5b204203</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2009</creationdate><topic>Animals</topic><topic>Apoptosis Regulatory Proteins - 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Academic</collection><jtitle>Cell research</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Tomasello, Flora</au><au>Messina, Angela</au><au>Lartigue, Lydia</au><au>Schembri, Laura</au><au>Medina, Chantal</au><au>Reina, Simona</au><au>Thoraval, Didier</au><au>Crouzet, Marc</au><au>Ichas, François</au><au>De Pinto, Vito</au><au>De Giorgi, Francesca</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis</atitle><jtitle>Cell research</jtitle><stitle>Cell Res</stitle><addtitle>Cell Research</addtitle><date>2009-12-01</date><risdate>2009</risdate><volume>19</volume><issue>12</issue><spage>1363</spage><epage>1376</epage><pages>1363-1376</pages><issn>1001-0602</issn><eissn>1748-7838</eissn><abstract>Voltage-dependent anion channel （VDAC）I is the main channel of the mitochondrial outer membrane （MOM） and it has been proposed to be part of the permeability transition pore （PTP）, a putative multiprotein complex candidate agent of the mitochondrial permeability transition （MPT）. Working at the single live cell level, we found that overexpression of VDAC1 triggers MPT at the mitochondrial inner membrane （MIM）. Conversely, silencing VDAC1 ex- pression results in the inhibition of MPT caused by selenite-induced oxidative stress. This MOM-MIM crosstalk was modulated by Cyclosporin A and mitochondrial Cyclophilin D, but not by Bcl-2 and BcI-XL, indicative of PTP operation. VDAC1-dependent MPT engages a positive feedback loop involving reactive oxygen species and p38-MAPK, and secondarily triggers a canonical apoptotic response including Bax activation, cytochrome e release and caspase 3 activation. Our data thus support a model of the PTP complex involving VDAC1 at the MOM, and indicate that VDACl-dependent MPT is an upstream mechanism playing a causal role in oxidative stress-induced apoptosis.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>19668262</pmid><doi>10.1038/cr.2009.98</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Cell research, 2009-12, Vol.19 (12), p.1363-1376 |
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| source | MEDLINE; Springer Nature - Complete Springer Journals; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals |
| subjects | Animals Apoptosis Regulatory Proteins - metabolism Biomedical and Life Sciences caspase Cell Biology Cell Membrane Permeability - physiology Chlorocebus aethiops COS Cells Cyclophilins - pharmacology Cyclosporine - pharmacology Cytochrome Feedback, Physiological - physiology Gene Silencing - physiology HeLa Cells Humans Life Sciences Membrane Potential, Mitochondrial - physiology Membranes Mitochondrial Membranes - metabolism original-article Oxidative stress Oxidative Stress - drug effects Oxidative Stress - physiology p38蛋白激酶 Peptidyl-Prolyl Isomerase F Permeability Sodium Selenite - pharmacology Stress, Physiological - physiology Upstream Voltage-Dependent Anion Channel 1 - genetics Voltage-Dependent Anion Channel 1 - metabolism 微波等离子体炬 线粒体膜 细胞凋亡 膜通透性 蛋白质复合体 |
| title | Outer membrane VDAC1 controls permeability transition of the inner mitochondrial membrane in cellulo during stress-induced apoptosis |
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