Nigericin modifies the mechanism of the uncoupling action of bile acids in rat liver mitochondria by converting ΔpH into Δψ.
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| Title: | Nigericin modifies the mechanism of the uncoupling action of bile acids in rat liver mitochondria by converting ΔpH into Δψ. |
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| Authors: | Pavlova, Evgeniya K.1 (AUTHOR), Samartsev, Victor N.1 (AUTHOR), Dubinin, Mikhail V.1 (AUTHOR) dubinin1989@gmail.com |
| Source: | Journal of Bioenergetics & Biomembranes. Feb2025, Vol. 57 Issue 1, p39-48. 10p. |
| Subjects: | Liver mitochondria, Cholic acid, Chenodeoxycholic acid, Biochemical substrates, Secretion |
| Abstract: | Cholestasis caused by impaired bile secretion in the liver is associated with the accumulation of primary bile acids (BA): cholic acid (CA) and chenodeoxycholic acid (CDCA) in the cells of this organ. The paper studies the uncoupling effect of the CA and CDCA on the succinate-fueled rat liver mitochondria under conditions of ΔpH to Δψ conversion by nigericin. It has been established that without nigericin, the dependence of the resting-state (state 4) respiration rate on the concentrations of these BA is nonlinear and is described by a parabolic equation. Under these conditions, the specific inhibitor of the ADP/ATP-antiporter – carboxyatractylate and the substrate of the aspartate/glutamate-antiporter – glutamate do not affect the state 4 respiration of mitochondria stimulated by these BA. It is suggested that without nigericin, the protonophore action of BA is due to the formation of a dimeric complex of their anion with the acid. In the presence of nigericin, the dependence of state 4 respiration rate on BA concentration is linear. Under these conditions, carboxyatractylate inhibits BA-stimulated respiration. Unlike the CDCA, the uncoupling action of CA is also suppressed by the substrates of the aspartate/glutamate-antiporter. The obtained results are considered as evidence that in the presence of nigericin, uncoupling action of CDCA is carried out primarily with the participation of ADP/ATP-antiporter. Both ADP/ATP-antiporter and aspartate/glutamate-antiporter are involved in the uncoupling action of CA. It is concluded that nigericin modifies the mechanism of the uncoupling action of BA in liver mitochondria by converting ΔpH to Δψ. [ABSTRACT FROM AUTHOR] |
| Copyright of Journal of Bioenergetics & Biomembranes is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.) | |
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| Header | DbId: egs DbLabel: Engineering Source An: 183076779 AccessLevel: 6 PubType: Academic Journal PubTypeId: academicJournal PreciseRelevancyScore: 0 |
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| Items | – Name: Title Label: Title Group: Ti Data: Nigericin modifies the mechanism of the uncoupling action of bile acids in rat liver mitochondria by converting ΔpH into Δψ. – Name: Author Label: Authors Group: Au Data: <searchLink fieldCode="AR" term="%22Pavlova%2C+Evgeniya+K%2E%22">Pavlova, Evgeniya K.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Samartsev%2C+Victor+N%2E%22">Samartsev, Victor N.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<br /><searchLink fieldCode="AR" term="%22Dubinin%2C+Mikhail+V%2E%22">Dubinin, Mikhail V.</searchLink><relatesTo>1</relatesTo> (AUTHOR)<i> dubinin1989@gmail.com</i> – Name: TitleSource Label: Source Group: Src Data: <searchLink fieldCode="JN" term="%22Journal+of+Bioenergetics+%26+Biomembranes%22">Journal of Bioenergetics & Biomembranes</searchLink>. Feb2025, Vol. 57 Issue 1, p39-48. 10p. – Name: Subject Label: Subjects Group: Su Data: <searchLink fieldCode="DE" term="%22Liver+mitochondria%22">Liver mitochondria</searchLink><br /><searchLink fieldCode="DE" term="%22Cholic+acid%22">Cholic acid</searchLink><br /><searchLink fieldCode="DE" term="%22Chenodeoxycholic+acid%22">Chenodeoxycholic acid</searchLink><br /><searchLink fieldCode="DE" term="%22Biochemical+substrates%22">Biochemical substrates</searchLink><br /><searchLink fieldCode="DE" term="%22Secretion%22">Secretion</searchLink> – Name: Abstract Label: Abstract Group: Ab Data: Cholestasis caused by impaired bile secretion in the liver is associated with the accumulation of primary bile acids (BA): cholic acid (CA) and chenodeoxycholic acid (CDCA) in the cells of this organ. The paper studies the uncoupling effect of the CA and CDCA on the succinate-fueled rat liver mitochondria under conditions of ΔpH to Δψ conversion by nigericin. It has been established that without nigericin, the dependence of the resting-state (state 4) respiration rate on the concentrations of these BA is nonlinear and is described by a parabolic equation. Under these conditions, the specific inhibitor of the ADP/ATP-antiporter – carboxyatractylate and the substrate of the aspartate/glutamate-antiporter – glutamate do not affect the state 4 respiration of mitochondria stimulated by these BA. It is suggested that without nigericin, the protonophore action of BA is due to the formation of a dimeric complex of their anion with the acid. In the presence of nigericin, the dependence of state 4 respiration rate on BA concentration is linear. Under these conditions, carboxyatractylate inhibits BA-stimulated respiration. Unlike the CDCA, the uncoupling action of CA is also suppressed by the substrates of the aspartate/glutamate-antiporter. The obtained results are considered as evidence that in the presence of nigericin, uncoupling action of CDCA is carried out primarily with the participation of ADP/ATP-antiporter. Both ADP/ATP-antiporter and aspartate/glutamate-antiporter are involved in the uncoupling action of CA. It is concluded that nigericin modifies the mechanism of the uncoupling action of BA in liver mitochondria by converting ΔpH to Δψ. [ABSTRACT FROM AUTHOR] – Name: AbstractSuppliedCopyright Label: Group: Ab Data: <i>Copyright of Journal of Bioenergetics & Biomembranes is the property of Springer Nature and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.) |
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| RecordInfo | BibRecord: BibEntity: Identifiers: – Type: doi Value: 10.1007/s10863-024-10048-5 Languages: – Code: eng Text: English PhysicalDescription: Pagination: PageCount: 10 StartPage: 39 Subjects: – SubjectFull: Liver mitochondria Type: general – SubjectFull: Cholic acid Type: general – SubjectFull: Chenodeoxycholic acid Type: general – SubjectFull: Biochemical substrates Type: general – SubjectFull: Secretion Type: general Titles: – TitleFull: Nigericin modifies the mechanism of the uncoupling action of bile acids in rat liver mitochondria by converting ΔpH into Δψ. Type: main BibRelationships: HasContributorRelationships: – PersonEntity: Name: NameFull: Pavlova, Evgeniya K. – PersonEntity: Name: NameFull: Samartsev, Victor N. – PersonEntity: Name: NameFull: Dubinin, Mikhail V. IsPartOfRelationships: – BibEntity: Dates: – D: 01 M: 02 Text: Feb2025 Type: published Y: 2025 Identifiers: – Type: issn-print Value: 0145479X Numbering: – Type: volume Value: 57 – Type: issue Value: 1 Titles: – TitleFull: Journal of Bioenergetics & Biomembranes Type: main |
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