Matches in SemOpenAlex for { <https://semopenalex.org/work/W2320051510> ?p ?o ?g. }
Showing items 1 to 99 of
99
with 100 items per page.
- W2320051510 abstract "Low permeability of the mitochondrial inner membrane is critical for maintaining the mitochondrial electrochemical potential - the driving force for ATP production. Acute stress conditions, lead to the increase in the mitochondrial inner membrane permeability due to the opening of the permeability transition pore (PTP). PTP allows free movement of ions and small molecules leading to mitochondrial depolarization, ATP depletion and cell death. Recent studies suggest that C-subunit of the mitochondrial ATP synthase plays a central role in PTP. Previous work in our laboratory showed that mitochondria contain non-protein complex composed of polyhydroxybutyrate, inorganic polyphosphate and calcium that forms an ion channel with properties resembling PTP. Here we explore the possibility of interactions between these non-protein components and C-subunit during the induction of PTP.To induce PTP,isolated energized mitochondria were treated with calcium. Control mitochondria were treated with calcium either in the presence of ruthenium red, inhibitor of calcium uptake or Cyclosporin A, inhibitor of PTP. This was followed by a water-free chloroform extraction of channel forming fraction of PTP. Components of the extract were analyzed using immunoblot analysis. We found significantly increased amount of C-subunit associated with channel forming fraction extracted from mitochondria with activated PTP. In contrast, C-subunit was not detectable in the extract when Ruthenium Red was present and significantly decreased in the presence of Cyclosporin A or in the absence of calcium.These results show that C-subunit is likely an interacting partner of the pore-forming complex of polyphosphate, calcium and polyhydroxybutyrate. We hypothesize that fully functional PTP requires calcium-induced formation of the pore made of both the complexed polymers and the c-subunit of ATP synthase" @default.
- W2320051510 created "2016-06-24" @default.
- W2320051510 creator A5008049187 @default.
- W2320051510 creator A5055612936 @default.
- W2320051510 creator A5068047345 @default.
- W2320051510 creator A5081258581 @default.
- W2320051510 date "2015-01-01" @default.
- W2320051510 modified "2023-09-26" @default.
- W2320051510 title "Activation of the Mitochondrial Permeability Transition Pore Leads to the Increase in Amount of C-Subunit of ATP Synthase Associated with Channel-Forming Complex of Polyhydroxybutyrate and Inorganic Polyphosphate" @default.
- W2320051510 doi "https://doi.org/10.1016/j.bpj.2014.11.3309" @default.
- W2320051510 hasPublicationYear "2015" @default.
- W2320051510 type Work @default.
- W2320051510 sameAs 2320051510 @default.
- W2320051510 citedByCount "0" @default.
- W2320051510 crossrefType "journal-article" @default.
- W2320051510 hasAuthorship W2320051510A5008049187 @default.
- W2320051510 hasAuthorship W2320051510A5055612936 @default.
- W2320051510 hasAuthorship W2320051510A5068047345 @default.
- W2320051510 hasAuthorship W2320051510A5081258581 @default.
- W2320051510 hasBestOaLocation W23200515101 @default.
- W2320051510 hasConcept C104292427 @default.
- W2320051510 hasConcept C104317684 @default.
- W2320051510 hasConcept C112243037 @default.
- W2320051510 hasConcept C12554922 @default.
- W2320051510 hasConcept C13591479 @default.
- W2320051510 hasConcept C178790620 @default.
- W2320051510 hasConcept C181199279 @default.
- W2320051510 hasConcept C181911157 @default.
- W2320051510 hasConcept C185592680 @default.
- W2320051510 hasConcept C190283241 @default.
- W2320051510 hasConcept C2777132085 @default.
- W2320051510 hasConcept C2778038992 @default.
- W2320051510 hasConcept C2779657890 @default.
- W2320051510 hasConcept C2780849362 @default.
- W2320051510 hasConcept C28859421 @default.
- W2320051510 hasConcept C31573885 @default.
- W2320051510 hasConcept C35341161 @default.
- W2320051510 hasConcept C4141045 @default.
- W2320051510 hasConcept C519063684 @default.
- W2320051510 hasConcept C523546767 @default.
- W2320051510 hasConcept C54355233 @default.
- W2320051510 hasConcept C55493867 @default.
- W2320051510 hasConcept C75385678 @default.
- W2320051510 hasConcept C86803240 @default.
- W2320051510 hasConcept C95444343 @default.
- W2320051510 hasConcept C98539663 @default.
- W2320051510 hasConceptScore W2320051510C104292427 @default.
- W2320051510 hasConceptScore W2320051510C104317684 @default.
- W2320051510 hasConceptScore W2320051510C112243037 @default.
- W2320051510 hasConceptScore W2320051510C12554922 @default.
- W2320051510 hasConceptScore W2320051510C13591479 @default.
- W2320051510 hasConceptScore W2320051510C178790620 @default.
- W2320051510 hasConceptScore W2320051510C181199279 @default.
- W2320051510 hasConceptScore W2320051510C181911157 @default.
- W2320051510 hasConceptScore W2320051510C185592680 @default.
- W2320051510 hasConceptScore W2320051510C190283241 @default.
- W2320051510 hasConceptScore W2320051510C2777132085 @default.
- W2320051510 hasConceptScore W2320051510C2778038992 @default.
- W2320051510 hasConceptScore W2320051510C2779657890 @default.
- W2320051510 hasConceptScore W2320051510C2780849362 @default.
- W2320051510 hasConceptScore W2320051510C28859421 @default.
- W2320051510 hasConceptScore W2320051510C31573885 @default.
- W2320051510 hasConceptScore W2320051510C35341161 @default.
- W2320051510 hasConceptScore W2320051510C4141045 @default.
- W2320051510 hasConceptScore W2320051510C519063684 @default.
- W2320051510 hasConceptScore W2320051510C523546767 @default.
- W2320051510 hasConceptScore W2320051510C54355233 @default.
- W2320051510 hasConceptScore W2320051510C55493867 @default.
- W2320051510 hasConceptScore W2320051510C75385678 @default.
- W2320051510 hasConceptScore W2320051510C86803240 @default.
- W2320051510 hasConceptScore W2320051510C95444343 @default.
- W2320051510 hasConceptScore W2320051510C98539663 @default.
- W2320051510 hasLocation W23200515101 @default.
- W2320051510 hasOpenAccess W2320051510 @default.
- W2320051510 hasPrimaryLocation W23200515101 @default.
- W2320051510 hasRelatedWork W1745469069 @default.
- W2320051510 hasRelatedWork W1964952409 @default.
- W2320051510 hasRelatedWork W2012135330 @default.
- W2320051510 hasRelatedWork W2017230178 @default.
- W2320051510 hasRelatedWork W2021185445 @default.
- W2320051510 hasRelatedWork W2021752587 @default.
- W2320051510 hasRelatedWork W2044715720 @default.
- W2320051510 hasRelatedWork W2052737683 @default.
- W2320051510 hasRelatedWork W2062043492 @default.
- W2320051510 hasRelatedWork W2074330066 @default.
- W2320051510 hasRelatedWork W2090616503 @default.
- W2320051510 hasRelatedWork W2152748697 @default.
- W2320051510 hasRelatedWork W2281010423 @default.
- W2320051510 hasRelatedWork W2356287247 @default.
- W2320051510 hasRelatedWork W2395326345 @default.
- W2320051510 hasRelatedWork W2465548909 @default.
- W2320051510 hasRelatedWork W2908117805 @default.
- W2320051510 hasRelatedWork W2912127486 @default.
- W2320051510 hasRelatedWork W3004029150 @default.
- W2320051510 hasRelatedWork W3119356782 @default.
- W2320051510 isParatext "false" @default.
- W2320051510 isRetracted "false" @default.
- W2320051510 magId "2320051510" @default.
- W2320051510 workType "article" @default.