Hosler 2023 Mitochondrion: Difference between revisions
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|title=Hosler J, Hoang N, Shirey Edwards K (2023) The cyclic lipopeptide micafungin induces rupture of isolated mitochondria by reprograming the mitochondrial inner membrane anion channel. https://doi.org/10.1016/j.mito.2023.05.004 | |title=Hosler J, Hoang N, Shirey Edwards K (2023) The cyclic lipopeptide micafungin induces rupture of isolated mitochondria by reprograming the mitochondrial inner membrane anion channel. https://doi.org/10.1016/j.mito.2023.05.004 | ||
|info=Mitochondrion [Epub ahead of print]. [https://www.ncbi.nlm.nih.gov/pubmed/37201620 PMID: 37201620 Open Access] | |info=Mitochondrion [Epub ahead of print]. [https://www.ncbi.nlm.nih.gov/pubmed/37201620 PMID: 37201620 Open Access] | ||
|authors=Hosler | |authors=Hosler Jonathan, Hoang Ngoc, Shirey Edwards Kristine | ||
|year=2023 | |year=2023 | ||
|journal=Mitochondrion | |journal=Mitochondrion | ||
|abstract=The antifungal activity of the drug micafungin, a cyclic lipopeptide that interacts with membrane proteins, may involve inhibition of fungal mitochondria. In humans, mitochondria are spared by the inability of micafungin to cross the cytoplasmic membrane. Using isolated mitochondria, we find that micafungin initiates the uptake of salts, causing rapid swelling and rupture of mitochondria with release of cytochrome c. The inner membrane anion channel (IMAC) is altered by micafungin to transfer both cations and anions. We propose that binding of anionic micafungin to IMAC attracts cations into the ion pore for the rapid transfer of ion pairs. | |abstract=The antifungal activity of the drug micafungin, a cyclic lipopeptide that interacts with membrane proteins, may involve inhibition of fungal mitochondria. In humans, mitochondria are spared by the inability of micafungin to cross the cytoplasmic membrane. Using isolated mitochondria, we find that micafungin initiates the uptake of salts, causing rapid swelling and rupture of mitochondria with release of cytochrome c. The inner membrane anion channel (IMAC) is altered by micafungin to transfer both cations and anions. We propose that binding of anionic micafungin to IMAC attracts cations into the ion pore for the rapid transfer of ion pairs. | ||
|keywords=Anion transport, Cyclic lipopeptides, Inner mitochondrial anion channel, Ion channel, Micafungin, Mitochondrial respiratory chain complex, Mitochondrial transport | |||
|editor=[[Plangger M]] | |editor=[[Plangger M]] | ||
}} | }} | ||
Revision as of 18:23, 22 May 2023
| Hosler J, Hoang N, Shirey Edwards K (2023) The cyclic lipopeptide micafungin induces rupture of isolated mitochondria by reprograming the mitochondrial inner membrane anion channel. https://doi.org/10.1016/j.mito.2023.05.004 |
» Mitochondrion [Epub ahead of print]. PMID: 37201620 Open Access
Hosler Jonathan, Hoang Ngoc, Shirey Edwards Kristine (2023) Mitochondrion
Abstract: The antifungal activity of the drug micafungin, a cyclic lipopeptide that interacts with membrane proteins, may involve inhibition of fungal mitochondria. In humans, mitochondria are spared by the inability of micafungin to cross the cytoplasmic membrane. Using isolated mitochondria, we find that micafungin initiates the uptake of salts, causing rapid swelling and rupture of mitochondria with release of cytochrome c. The inner membrane anion channel (IMAC) is altered by micafungin to transfer both cations and anions. We propose that binding of anionic micafungin to IMAC attracts cations into the ion pore for the rapid transfer of ion pairs. • Keywords: Anion transport, Cyclic lipopeptides, Inner mitochondrial anion channel, Ion channel, Micafungin, Mitochondrial respiratory chain complex, Mitochondrial transport • Bioblast editor: Plangger M
Labels: MiParea: Respiration
HRR: Oxygraph-2k
2023-05
