We are analyzing https://link.springer.com/article/10.1007/s10495-007-0718-8.

Title:
Cardiolipin: Setting the beat of apoptosis | Apoptosis
Description:
Cardiolipin (CL) is a mitochondria-specific phospholipid which is known to be intimately linked with the mitochondrial bioenergetic machinery. Accumulating evidence now suggests that this unique lipid also has active roles in several of the mitochondria-dependant steps of apoptosis. CL is closely associated with cytochrome c at the outer leaflet of the mitochondrial inner membrane. This interaction makes the process of cytochrome c release from mitochondria more complex than previously assumed, requiring more than pore formation in the mitochondrial outer membrane. While CL peroxidation could be crucial for enabling cytochrome c dissociation from the mitochondrial inner membrane, cytochrome c itself catalyzes CL peroxidation. Moreover, peroxy-CL directly activates the release of cytochrome c and other apoptogenic factors from the mitochondria. CL is also directly involved in mitochondrial outer membrane permeabilization by enabling docking and activation of pro-apoptotic Bcl-2 proteins. It appears therefore that CL has multiple roles in apoptosis and that CL metabolism contributes to the complexity of the apoptotic process.
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Keywords {🔍}

pubmed, google, scholar, cas, article, cardiolipin, mitochondrial, cytochrome, cell, apoptosis, biol, mitochondria, chem, lipid, death, biophys, release, membrane, biochim, acta, role, differ, bid, outer, activity, schlame, biochem, heart, membranes, gonzalvez, phospholipid, peroxidation, proapoptotic, bcl, barth, rat, tbid, privacy, cookies, content, research, gottlieb, interaction, syndrome, res, greenberg, synthase, molecular, electron, publish,

Topics {✒️}

pro-apoptotic bcl-2 proteins x-linked dilated cardiomyopathy chinese hamster ovary accelerates stimuli-elicited apoptosis attenuates stress-induced apoptosis nitric-oxide-induced apoptosis palmitate-induced cardiomyocyte apoptosis pgp synthase-defective mutant death receptor-mediated apoptosis peroxy-cl directly activates bcl-2 family proteins eyal gottlieb related subjects carnitine acylcarnitine translocase �pro-apoptotic genies” tbid/bax synergistic effects article gonzalvez privacy choices/manage cookies cpp32-deficient mice freeze-fracture techniques form supramolecular openings bcl-2 protein family mitochondrial contact sites mitochondrial cristae reorganization cardiolipin-lacking yeast mitochondria x-linked gene human cardiolipin synthase mitochondria-specific phospholipid mitochondrial phosphate carrier lipid-protein interactions bcl-2 interacting protein resonance energy transfer mitochondrial bioenergetic machinery age-dependent decline rat heart subjected hypoglycaemia-induced apoptosis mitochondrial respiratory chain ligand-induced activation bovine heart mitochondria ph-dependent association mitochondrial outer membrane outer mitochondrial membrane mitochondrial cardiolipin trigger european economic area critical control points polymorphic phase behaviour substrate-transporting properties cho-k1 cells programmed neuronal death posttranslational n-myristoylation

Questions {❓}

Does Oxidation of Mitochondrial Cardiolipin Trigger a Chain of Antiapoptotic Reactions?
Is cardiolipin present in the mitochondrial outer membrane?

Schema {🗺️}

WebPage:
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         headline:Cardiolipin: Setting the beat of apoptosis
         description:Cardiolipin (CL) is a mitochondria-specific phospholipid which is known to be intimately linked with the mitochondrial bioenergetic machinery. Accumulating evidence now suggests that this unique lipid also has active roles in several of the mitochondria-dependant steps of apoptosis. CL is closely associated with cytochrome c at the outer leaflet of the mitochondrial inner membrane. This interaction makes the process of cytochrome c release from mitochondria more complex than previously assumed, requiring more than pore formation in the mitochondrial outer membrane. While CL peroxidation could be crucial for enabling cytochrome c dissociation from the mitochondrial inner membrane, cytochrome c itself catalyzes CL peroxidation. Moreover, peroxy-CL directly activates the release of cytochrome c and other apoptogenic factors from the mitochondria. CL is also directly involved in mitochondrial outer membrane permeabilization by enabling docking and activation of pro-apoptotic Bcl-2 proteins. It appears therefore that CL has multiple roles in apoptosis and that CL metabolism contributes to the complexity of the apoptotic process.
         datePublished:2007-02-06T00:00:00Z
         dateModified:2007-02-06T00:00:00Z
         pageStart:877
         pageEnd:885
         sameAs:https://doi.org/10.1007/s10495-007-0718-8
         keywords:
            Mitochondria
            Apoptosis
            Cardiolipin
            Cancer Research
            Cell Biology
            Oncology
            Biochemistry
            general
            Virology
         image:
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            issn:
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         author:
               name:François Gonzalvez
               affiliation:
                     name:The Beatson Institute for Cancer Research
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                        name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
                        type:PostalAddress
                     type:Organization
               type:Person
               name:Eyal Gottlieb
               affiliation:
                     name:The Beatson Institute for Cancer Research
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                        name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
                        type:PostalAddress
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ScholarlyArticle:
      headline:Cardiolipin: Setting the beat of apoptosis
      description:Cardiolipin (CL) is a mitochondria-specific phospholipid which is known to be intimately linked with the mitochondrial bioenergetic machinery. Accumulating evidence now suggests that this unique lipid also has active roles in several of the mitochondria-dependant steps of apoptosis. CL is closely associated with cytochrome c at the outer leaflet of the mitochondrial inner membrane. This interaction makes the process of cytochrome c release from mitochondria more complex than previously assumed, requiring more than pore formation in the mitochondrial outer membrane. While CL peroxidation could be crucial for enabling cytochrome c dissociation from the mitochondrial inner membrane, cytochrome c itself catalyzes CL peroxidation. Moreover, peroxy-CL directly activates the release of cytochrome c and other apoptogenic factors from the mitochondria. CL is also directly involved in mitochondrial outer membrane permeabilization by enabling docking and activation of pro-apoptotic Bcl-2 proteins. It appears therefore that CL has multiple roles in apoptosis and that CL metabolism contributes to the complexity of the apoptotic process.
      datePublished:2007-02-06T00:00:00Z
      dateModified:2007-02-06T00:00:00Z
      pageStart:877
      pageEnd:885
      sameAs:https://doi.org/10.1007/s10495-007-0718-8
      keywords:
         Mitochondria
         Apoptosis
         Cardiolipin
         Cancer Research
         Cell Biology
         Oncology
         Biochemistry
         general
         Virology
      image:
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         name:Apoptosis
         issn:
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            1360-8185
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         name:Kluwer Academic Publishers
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            url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
            type:ImageObject
         type:Organization
      author:
            name:François Gonzalvez
            affiliation:
                  name:The Beatson Institute for Cancer Research
                  address:
                     name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
                     type:PostalAddress
                  type:Organization
            type:Person
            name:Eyal Gottlieb
            affiliation:
                  name:The Beatson Institute for Cancer Research
                  address:
                     name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
                     type:PostalAddress
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      name:Apoptosis
      issn:
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         1360-8185
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Organization:
      name:Kluwer Academic Publishers
      logo:
         url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
         type:ImageObject
      name:The Beatson Institute for Cancer Research
      address:
         name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
         type:PostalAddress
      name:The Beatson Institute for Cancer Research
      address:
         name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
         type:PostalAddress
ImageObject:
      url:https://www.springernature.com/app-sn/public/images/logo-springernature.png
Person:
      name:François Gonzalvez
      affiliation:
            name:The Beatson Institute for Cancer Research
            address:
               name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
               type:PostalAddress
            type:Organization
      name:Eyal Gottlieb
      affiliation:
            name:The Beatson Institute for Cancer Research
            address:
               name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
               type:PostalAddress
            type:Organization
      email:[email protected]
PostalAddress:
      name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom
      name:Cancer Research UK, The Beatson Institute for Cancer Research, Glasgow, United Kingdom

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