Osmotic regulation of the mitochondrial permeability transition pore investigated by light scattering, fluorescence and electron microscopy techniques

Artyom Y. Baev, Pia A. Elustondo, Alexander Negoda, Evgeny Pavlov

Research output: Contribution to journalArticle

Abstract

Mitochondrial permeability transition (PT) is a phenomenon of an increase of the inner membrane permeability in response to an excessive matrix calcium accumulation. PTP is caused by the opening of the large weakly selective channel. Molecular composition and regulation of permeability transition pore (PTP) are not well understood. Here we used isolated mitochondria to investigate dependence of PTP activation on the osmotic pressure. We found that in low osmotic strength solution calcium-induced PTP is significantly inhibited. We propose that this effect is linked to the changes in the curvature of the mitochondrial inner membrane. This interpretation is consistent with the idea about the importance of ATP synthase dimerization in modulation of the PTP activity.

Original languageEnglish (US)
JournalAnalytical Biochemistry
DOIs
StateAccepted/In press - 2017

Fingerprint

Fluorescence microscopy
Fluorescence Microscopy
Light scattering
Electron microscopy
Permeability
Electron Microscopy
Calcium
Membranes
Light
Mitochondria
Dimerization
Adenosine Triphosphate
Chemical activation
Modulation
Chemical analysis
Osmotic Pressure
Mitochondrial Membranes
mitochondrial permeability transition pore

Keywords

  • ATP-synthase
  • C-subunit
  • Calcium
  • Mitochondrial permeability transition pore
  • Osmotic pressure
  • Swelling

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

@article{4923faafbbd8481f9441d528d5c88c74,
title = "Osmotic regulation of the mitochondrial permeability transition pore investigated by light scattering, fluorescence and electron microscopy techniques",
abstract = "Mitochondrial permeability transition (PT) is a phenomenon of an increase of the inner membrane permeability in response to an excessive matrix calcium accumulation. PTP is caused by the opening of the large weakly selective channel. Molecular composition and regulation of permeability transition pore (PTP) are not well understood. Here we used isolated mitochondria to investigate dependence of PTP activation on the osmotic pressure. We found that in low osmotic strength solution calcium-induced PTP is significantly inhibited. We propose that this effect is linked to the changes in the curvature of the mitochondrial inner membrane. This interpretation is consistent with the idea about the importance of ATP synthase dimerization in modulation of the PTP activity.",
keywords = "ATP-synthase, C-subunit, Calcium, Mitochondrial permeability transition pore, Osmotic pressure, Swelling",
author = "Baev, {Artyom Y.} and Elustondo, {Pia A.} and Alexander Negoda and Evgeny Pavlov",
year = "2017",
doi = "10.1016/j.ab.2017.07.006",
language = "English (US)",
journal = "Analytical Biochemistry",
issn = "0003-2697",
publisher = "Academic Press Inc.",

}

TY - JOUR

T1 - Osmotic regulation of the mitochondrial permeability transition pore investigated by light scattering, fluorescence and electron microscopy techniques

AU - Baev, Artyom Y.

AU - Elustondo, Pia A.

AU - Negoda, Alexander

AU - Pavlov, Evgeny

PY - 2017

Y1 - 2017

N2 - Mitochondrial permeability transition (PT) is a phenomenon of an increase of the inner membrane permeability in response to an excessive matrix calcium accumulation. PTP is caused by the opening of the large weakly selective channel. Molecular composition and regulation of permeability transition pore (PTP) are not well understood. Here we used isolated mitochondria to investigate dependence of PTP activation on the osmotic pressure. We found that in low osmotic strength solution calcium-induced PTP is significantly inhibited. We propose that this effect is linked to the changes in the curvature of the mitochondrial inner membrane. This interpretation is consistent with the idea about the importance of ATP synthase dimerization in modulation of the PTP activity.

AB - Mitochondrial permeability transition (PT) is a phenomenon of an increase of the inner membrane permeability in response to an excessive matrix calcium accumulation. PTP is caused by the opening of the large weakly selective channel. Molecular composition and regulation of permeability transition pore (PTP) are not well understood. Here we used isolated mitochondria to investigate dependence of PTP activation on the osmotic pressure. We found that in low osmotic strength solution calcium-induced PTP is significantly inhibited. We propose that this effect is linked to the changes in the curvature of the mitochondrial inner membrane. This interpretation is consistent with the idea about the importance of ATP synthase dimerization in modulation of the PTP activity.

KW - ATP-synthase

KW - C-subunit

KW - Calcium

KW - Mitochondrial permeability transition pore

KW - Osmotic pressure

KW - Swelling

UR - http://www.scopus.com/inward/record.url?scp=85024479300&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=85024479300&partnerID=8YFLogxK

U2 - 10.1016/j.ab.2017.07.006

DO - 10.1016/j.ab.2017.07.006

M3 - Article

C2 - 28693989

AN - SCOPUS:85024479300

JO - Analytical Biochemistry

JF - Analytical Biochemistry

SN - 0003-2697

ER -