Effects of equisetin on rat liver mitochondria

Evidence for inhibition of substrate anion carriers of the inner membrane

Tamás König, András Kapus, B. Sarkadi

Research output: Contribution to journalArticle

21 Citations (Scopus)

Abstract

The effect of equisetin, an antibiotic produced by Fusarium equiseti, has been studied on mitochondrial functions (respiration, ATPase, ion transport). Equisetin inhibits the DNP-stimulated ATPase activity of rat liver mitochondria and mitoplasts in a concentration-dependent manner; 50% inhibition is caused by about 8 nmol equisetin/mg protein. The antibiotic is without effect either on the ATPase activity of submitochondrial particles or on the purified F1-ATPase. It inhibits both the ADP- or DNP-activated oxygen uptake by mitochondria in the presence of glutamate + malate or succinate as substrates, but only the ADP-stimulated respiration is inhibited if the electron donors are TMPD + ascorbate. It does not affect the NADH or succinate oxidation of submitochondrial particles. Equisetin inhibits in a concentration-dependent manner the active Ca2+-uptake of mitochondria energized both by ATP or succinate without affecting the Ca2+-uniporter itself. The antibiotic inhibits the ATP-uptake by mitochondria (50% inhibition at about 8 nmol equisetin/mg protein) and the Pi and dicarboxylate carrier. It does not lower the membrane potential at least up to 200 nmol/mg protein concentration. The data presented in this paper indicate that equisetin specifically inhibits the substrate anion carriers of the mitochondrial inner membrane.

Original languageEnglish
Pages (from-to)537-545
Number of pages9
JournalJournal of Bioenergetics and Biomembranes
Volume25
Issue number5
DOIs
Publication statusPublished - Oct 1993

Fingerprint

Liver Mitochondrion
Anions
Membranes
Succinic Acid
Submitochondrial Particles
Adenosine Triphosphatases
Mitochondria
Anti-Bacterial Agents
Adenosine Diphosphate
Dicarboxylic Acid Transporters
Respiration
Adenosine Triphosphate
Proteins
Proton-Translocating ATPases
Ion Transport
Fusarium
Mitochondrial Membranes
NAD
Membrane Potentials
equisetin

Keywords

  • ATPase
  • equisetin
  • rat liver mitochondria
  • Respiratory chain
  • substrate anion carriers

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

Effects of equisetin on rat liver mitochondria : Evidence for inhibition of substrate anion carriers of the inner membrane. / König, Tamás; Kapus, András; Sarkadi, B.

In: Journal of Bioenergetics and Biomembranes, Vol. 25, No. 5, 10.1993, p. 537-545.

Research output: Contribution to journalArticle

@article{263526dcee324b608a73becef66529f1,
title = "Effects of equisetin on rat liver mitochondria: Evidence for inhibition of substrate anion carriers of the inner membrane",
abstract = "The effect of equisetin, an antibiotic produced by Fusarium equiseti, has been studied on mitochondrial functions (respiration, ATPase, ion transport). Equisetin inhibits the DNP-stimulated ATPase activity of rat liver mitochondria and mitoplasts in a concentration-dependent manner; 50{\%} inhibition is caused by about 8 nmol equisetin/mg protein. The antibiotic is without effect either on the ATPase activity of submitochondrial particles or on the purified F1-ATPase. It inhibits both the ADP- or DNP-activated oxygen uptake by mitochondria in the presence of glutamate + malate or succinate as substrates, but only the ADP-stimulated respiration is inhibited if the electron donors are TMPD + ascorbate. It does not affect the NADH or succinate oxidation of submitochondrial particles. Equisetin inhibits in a concentration-dependent manner the active Ca2+-uptake of mitochondria energized both by ATP or succinate without affecting the Ca2+-uniporter itself. The antibiotic inhibits the ATP-uptake by mitochondria (50{\%} inhibition at about 8 nmol equisetin/mg protein) and the Pi and dicarboxylate carrier. It does not lower the membrane potential at least up to 200 nmol/mg protein concentration. The data presented in this paper indicate that equisetin specifically inhibits the substrate anion carriers of the mitochondrial inner membrane.",
keywords = "ATPase, equisetin, rat liver mitochondria, Respiratory chain, substrate anion carriers",
author = "Tam{\'a}s K{\"o}nig and Andr{\'a}s Kapus and B. Sarkadi",
year = "1993",
month = "10",
doi = "10.1007/BF01108410",
language = "English",
volume = "25",
pages = "537--545",
journal = "Journal of Bioenergetics and Biomembranes",
issn = "0145-479X",
publisher = "Springer New York",
number = "5",

}

TY - JOUR

T1 - Effects of equisetin on rat liver mitochondria

T2 - Evidence for inhibition of substrate anion carriers of the inner membrane

AU - König, Tamás

AU - Kapus, András

AU - Sarkadi, B.

PY - 1993/10

Y1 - 1993/10

N2 - The effect of equisetin, an antibiotic produced by Fusarium equiseti, has been studied on mitochondrial functions (respiration, ATPase, ion transport). Equisetin inhibits the DNP-stimulated ATPase activity of rat liver mitochondria and mitoplasts in a concentration-dependent manner; 50% inhibition is caused by about 8 nmol equisetin/mg protein. The antibiotic is without effect either on the ATPase activity of submitochondrial particles or on the purified F1-ATPase. It inhibits both the ADP- or DNP-activated oxygen uptake by mitochondria in the presence of glutamate + malate or succinate as substrates, but only the ADP-stimulated respiration is inhibited if the electron donors are TMPD + ascorbate. It does not affect the NADH or succinate oxidation of submitochondrial particles. Equisetin inhibits in a concentration-dependent manner the active Ca2+-uptake of mitochondria energized both by ATP or succinate without affecting the Ca2+-uniporter itself. The antibiotic inhibits the ATP-uptake by mitochondria (50% inhibition at about 8 nmol equisetin/mg protein) and the Pi and dicarboxylate carrier. It does not lower the membrane potential at least up to 200 nmol/mg protein concentration. The data presented in this paper indicate that equisetin specifically inhibits the substrate anion carriers of the mitochondrial inner membrane.

AB - The effect of equisetin, an antibiotic produced by Fusarium equiseti, has been studied on mitochondrial functions (respiration, ATPase, ion transport). Equisetin inhibits the DNP-stimulated ATPase activity of rat liver mitochondria and mitoplasts in a concentration-dependent manner; 50% inhibition is caused by about 8 nmol equisetin/mg protein. The antibiotic is without effect either on the ATPase activity of submitochondrial particles or on the purified F1-ATPase. It inhibits both the ADP- or DNP-activated oxygen uptake by mitochondria in the presence of glutamate + malate or succinate as substrates, but only the ADP-stimulated respiration is inhibited if the electron donors are TMPD + ascorbate. It does not affect the NADH or succinate oxidation of submitochondrial particles. Equisetin inhibits in a concentration-dependent manner the active Ca2+-uptake of mitochondria energized both by ATP or succinate without affecting the Ca2+-uniporter itself. The antibiotic inhibits the ATP-uptake by mitochondria (50% inhibition at about 8 nmol equisetin/mg protein) and the Pi and dicarboxylate carrier. It does not lower the membrane potential at least up to 200 nmol/mg protein concentration. The data presented in this paper indicate that equisetin specifically inhibits the substrate anion carriers of the mitochondrial inner membrane.

KW - ATPase

KW - equisetin

KW - rat liver mitochondria

KW - Respiratory chain

KW - substrate anion carriers

UR - http://www.scopus.com/inward/record.url?scp=0027136099&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0027136099&partnerID=8YFLogxK

U2 - 10.1007/BF01108410

DO - 10.1007/BF01108410

M3 - Article

VL - 25

SP - 537

EP - 545

JO - Journal of Bioenergetics and Biomembranes

JF - Journal of Bioenergetics and Biomembranes

SN - 0145-479X

IS - 5

ER -