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dc.contributor.authorKluck, Ruth M
dc.contributor.authorEsposti, Mauro Dogli
dc.contributor.authorPerkins, Guy
dc.contributor.authorRenken, Christian
dc.contributor.authorKuwana, Tomomi
dc.contributor.authorBossy-Wetzel, Ella
dc.contributor.authorGoldberg, Martin W
dc.contributor.authorAllen, Terence D
dc.contributor.authorBarber, Michael J
dc.contributor.authorGreen, Douglas R
dc.contributor.authorNewmeyer, Donald D
dc.date.accessioned2010-02-08T11:04:31Z
dc.date.available2010-02-08T11:04:31Z
dc.date.issued1999-11-15
dc.identifier.citationThe pro-apoptotic proteins, Bid and Bax, cause a limited permeabilization of the mitochondrial outer membrane that is enhanced by cytosol. 1999, 147 (4):809-22 J. Cell Biol.en
dc.identifier.issn0021-9525
dc.identifier.pmid10562282
dc.identifier.urihttp://hdl.handle.net/10541/91339
dc.description.abstractDuring apoptosis, an important pathway leading to caspase activation involves the release of cytochrome c from the intermembrane space of mitochondria. Using a cell-free system based on Xenopus egg extracts, we examined changes in the outer mitochondrial membrane accompanying cytochrome c efflux. The pro-apoptotic proteins, Bid and Bax, as well as factors present in Xenopus egg cytosol, each induced cytochrome c release when incubated with isolated mitochondria. These factors caused a permeabilization of the outer membrane that allowed the corelease of multiple intermembrane space proteins: cytochrome c, adenylate kinase and sulfite oxidase. The efflux process is thus nonspecific. None of the cytochrome c-releasing factors caused detectable mitochondrial swelling, arguing that matrix swelling is not required for outer membrane permeability in this system. Bid and Bax caused complete release of cytochrome c but only a limited permeabilization of the outer membrane, as measured by the accessibility of inner membrane-associated respiratory complexes III and IV to exogenously added cytochrome c. However, outer membrane permeability was strikingly increased by a macromolecular cytosolic factor, termed PEF (permeability enhancing factor). We hypothesize that PEF activity could help determine whether cells can recover from mitochondrial cytochrome c release.
dc.language.isoenen
dc.subject.meshAdenylate Kinase
dc.subject.meshAlamethicin
dc.subject.meshAnimals
dc.subject.meshApoptosis
dc.subject.meshBH3 Interacting Domain Death Agonist Protein
dc.subject.meshCarrier Proteins
dc.subject.meshCell-Free System
dc.subject.meshCytochrome c Group
dc.subject.meshCytosol
dc.subject.meshElectron Transport Complex III
dc.subject.meshElectron Transport Complex IV
dc.subject.meshIntracellular Membranes
dc.subject.meshKinetics
dc.subject.meshMale
dc.subject.meshMicroscopy, Electron
dc.subject.meshMicroscopy, Electron, Scanning
dc.subject.meshMitochondria, Liver
dc.subject.meshOocytes
dc.subject.meshPeptide Hydrolases
dc.subject.meshPermeability
dc.subject.meshProto-Oncogene Proteins
dc.subject.meshProto-Oncogene Proteins c-bcl-2
dc.subject.meshRats
dc.subject.meshRats, Sprague-Dawley
dc.subject.meshRecombinant Proteins
dc.subject.meshXenopus laevis
dc.subject.meshbcl-2-Associated X Protein
dc.titleThe pro-apoptotic proteins, Bid and Bax, cause a limited permeabilization of the mitochondrial outer membrane that is enhanced by cytosol.en
dc.typeArticleen
dc.contributor.departmentDivision of Cellular Immunology, La Jolla Institute for Allergy and Immunology, San Diego, California 92121, USA.en
dc.identifier.journalJournal of Cell Biologyen
html.description.abstractDuring apoptosis, an important pathway leading to caspase activation involves the release of cytochrome c from the intermembrane space of mitochondria. Using a cell-free system based on Xenopus egg extracts, we examined changes in the outer mitochondrial membrane accompanying cytochrome c efflux. The pro-apoptotic proteins, Bid and Bax, as well as factors present in Xenopus egg cytosol, each induced cytochrome c release when incubated with isolated mitochondria. These factors caused a permeabilization of the outer membrane that allowed the corelease of multiple intermembrane space proteins: cytochrome c, adenylate kinase and sulfite oxidase. The efflux process is thus nonspecific. None of the cytochrome c-releasing factors caused detectable mitochondrial swelling, arguing that matrix swelling is not required for outer membrane permeability in this system. Bid and Bax caused complete release of cytochrome c but only a limited permeabilization of the outer membrane, as measured by the accessibility of inner membrane-associated respiratory complexes III and IV to exogenously added cytochrome c. However, outer membrane permeability was strikingly increased by a macromolecular cytosolic factor, termed PEF (permeability enhancing factor). We hypothesize that PEF activity could help determine whether cells can recover from mitochondrial cytochrome c release.


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