Effect of hyperthermia on electron transport in ehrlich ascites tumor mitochondria

A. Floridi, A. Nista, M. G. Paggi, L. Pellegrini, A. Bagnato, M. Fanciulli, A. Caputo

Research output: Contribution to journalArticle

Abstract

The effect of hyperthermia (1 hr, 41°C) on the functional properties of Ehrlich ascites tumor mitochondria was investigated. Mitochondria isolated from Ehrlich ascites tumor after exposure of whole cells to 41°C for 1 hr still phosphorylate and maintain a normal acceptor control ratio (ACR). The temperature decreases state 4 and ADP- and FCCP-stimulated respiration on various substrates entering at three energy-conserving sites of the respiratory chain. The inhibition of oxygen consumption by NAD- and FAD-linked substrates was 40% for state 4 and 70% for ADP- or FCCP-stimulated respiration. State 4 and FCCP-stimulated respiration of mitochondria on TMPD + ascorbate was affected 38% and 45%, respectively. ATPase activity was unaffected by hyperthermia, indicating that under these experimental conditions, the inhibition of ADP-stimulated respiration does not depend on an effect on either Fo F4-ATPase or adenine translocase, the activity of which is required for ATP entry prior to ATPase activity. Because of the inability to detect a specific site of action of temperature, it is conceivable that hyperthermia might inhibit substrate oxidation by altering some components of the inner mitochondrial membrane, which regulates the kinetic properties of the membrane-associated enzymes.

Original languageEnglish
Pages (from-to)279-293
Number of pages15
JournalExperimental and Molecular Pathology
Volume46
Issue number3
DOIs
Publication statusPublished - 1987

Fingerprint

Carbonyl Cyanide p-Trifluoromethoxyphenylhydrazone
Ehrlich Tumor Carcinoma
Mitochondria
Electron Transport
Adenosine Diphosphate
Adenosine Triphosphatases
Tumors
Respiration
Fever
Substrates
Membranes
Flavin-Adenine Dinucleotide
Adenine
NAD
Temperature
Mitochondrial Membranes
Adenosine Triphosphate
Oxygen Consumption
Oxygen
Oxidation

ASJC Scopus subject areas

  • Clinical Biochemistry
  • Molecular Biology
  • Pathology and Forensic Medicine

Cite this

Effect of hyperthermia on electron transport in ehrlich ascites tumor mitochondria. / Floridi, A.; Nista, A.; Paggi, M. G.; Pellegrini, L.; Bagnato, A.; Fanciulli, M.; Caputo, A.

In: Experimental and Molecular Pathology, Vol. 46, No. 3, 1987, p. 279-293.

Research output: Contribution to journalArticle

@article{d86de2bba20b433599893db5f2191629,
title = "Effect of hyperthermia on electron transport in ehrlich ascites tumor mitochondria",
abstract = "The effect of hyperthermia (1 hr, 41°C) on the functional properties of Ehrlich ascites tumor mitochondria was investigated. Mitochondria isolated from Ehrlich ascites tumor after exposure of whole cells to 41°C for 1 hr still phosphorylate and maintain a normal acceptor control ratio (ACR). The temperature decreases state 4 and ADP- and FCCP-stimulated respiration on various substrates entering at three energy-conserving sites of the respiratory chain. The inhibition of oxygen consumption by NAD- and FAD-linked substrates was 40{\%} for state 4 and 70{\%} for ADP- or FCCP-stimulated respiration. State 4 and FCCP-stimulated respiration of mitochondria on TMPD + ascorbate was affected 38{\%} and 45{\%}, respectively. ATPase activity was unaffected by hyperthermia, indicating that under these experimental conditions, the inhibition of ADP-stimulated respiration does not depend on an effect on either Fo F4-ATPase or adenine translocase, the activity of which is required for ATP entry prior to ATPase activity. Because of the inability to detect a specific site of action of temperature, it is conceivable that hyperthermia might inhibit substrate oxidation by altering some components of the inner mitochondrial membrane, which regulates the kinetic properties of the membrane-associated enzymes.",
author = "A. Floridi and A. Nista and Paggi, {M. G.} and L. Pellegrini and A. Bagnato and M. Fanciulli and A. Caputo",
year = "1987",
doi = "10.1016/0014-4800(87)90050-5",
language = "English",
volume = "46",
pages = "279--293",
journal = "Experimental and Molecular Pathology",
issn = "0014-4800",
publisher = "Academic Press Inc.",
number = "3",

}

TY - JOUR

T1 - Effect of hyperthermia on electron transport in ehrlich ascites tumor mitochondria

AU - Floridi, A.

AU - Nista, A.

AU - Paggi, M. G.

AU - Pellegrini, L.

AU - Bagnato, A.

AU - Fanciulli, M.

AU - Caputo, A.

PY - 1987

Y1 - 1987

N2 - The effect of hyperthermia (1 hr, 41°C) on the functional properties of Ehrlich ascites tumor mitochondria was investigated. Mitochondria isolated from Ehrlich ascites tumor after exposure of whole cells to 41°C for 1 hr still phosphorylate and maintain a normal acceptor control ratio (ACR). The temperature decreases state 4 and ADP- and FCCP-stimulated respiration on various substrates entering at three energy-conserving sites of the respiratory chain. The inhibition of oxygen consumption by NAD- and FAD-linked substrates was 40% for state 4 and 70% for ADP- or FCCP-stimulated respiration. State 4 and FCCP-stimulated respiration of mitochondria on TMPD + ascorbate was affected 38% and 45%, respectively. ATPase activity was unaffected by hyperthermia, indicating that under these experimental conditions, the inhibition of ADP-stimulated respiration does not depend on an effect on either Fo F4-ATPase or adenine translocase, the activity of which is required for ATP entry prior to ATPase activity. Because of the inability to detect a specific site of action of temperature, it is conceivable that hyperthermia might inhibit substrate oxidation by altering some components of the inner mitochondrial membrane, which regulates the kinetic properties of the membrane-associated enzymes.

AB - The effect of hyperthermia (1 hr, 41°C) on the functional properties of Ehrlich ascites tumor mitochondria was investigated. Mitochondria isolated from Ehrlich ascites tumor after exposure of whole cells to 41°C for 1 hr still phosphorylate and maintain a normal acceptor control ratio (ACR). The temperature decreases state 4 and ADP- and FCCP-stimulated respiration on various substrates entering at three energy-conserving sites of the respiratory chain. The inhibition of oxygen consumption by NAD- and FAD-linked substrates was 40% for state 4 and 70% for ADP- or FCCP-stimulated respiration. State 4 and FCCP-stimulated respiration of mitochondria on TMPD + ascorbate was affected 38% and 45%, respectively. ATPase activity was unaffected by hyperthermia, indicating that under these experimental conditions, the inhibition of ADP-stimulated respiration does not depend on an effect on either Fo F4-ATPase or adenine translocase, the activity of which is required for ATP entry prior to ATPase activity. Because of the inability to detect a specific site of action of temperature, it is conceivable that hyperthermia might inhibit substrate oxidation by altering some components of the inner mitochondrial membrane, which regulates the kinetic properties of the membrane-associated enzymes.

UR - http://www.scopus.com/inward/record.url?scp=0023256281&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023256281&partnerID=8YFLogxK

U2 - 10.1016/0014-4800(87)90050-5

DO - 10.1016/0014-4800(87)90050-5

M3 - Article

C2 - 2954847

AN - SCOPUS:0023256281

VL - 46

SP - 279

EP - 293

JO - Experimental and Molecular Pathology

JF - Experimental and Molecular Pathology

SN - 0014-4800

IS - 3

ER -