Elevation by ethanol and its metabolites of liver adenosine monophosphate

Kai O. Lindros, Raija-Liisa Kivikataja, Antti Suokas

Research output: Contribution to journalArticleScientificpeer-review

4 Citations (Scopus)

Abstract

Acute ethanol administration significantly increased the concentration of adenosine monophosphate (5′-AMP) in the intact freeze-clamped rat liver regardless of the ethanol dose administered. The increase was abolished by the alcohol dehydrogenase inhibitor 4-methylpyrazole, but was also seen after direct infusion of acetaldehyde into the portal vein. Administration of acetate to give hepatic levels similar to those seen during ethanol oxidation failed, however, to cause an increase in AMP. After ethanol administration there was a highly significant positive correlation between individual AMP levels and 3-OH-butyrate/acetoacetate ratios. The results suggest that the increase in liver AMP reflects activation of ethanol-derived acetate by acetothiokinase in the mitochondrial matrix. Ethanol, but not acetate inhibits the citric acid cycle, as reflected by the shift in the mitochondrial redox state. This could inhibit production of GTP needed for AMP phosphorylation by GTP-AMP phosphotransferase, thus explaining the accumulation
Original languageEnglish
Pages (from-to)63-67
JournalAlcohol
Volume3
Issue number1
DOIs
Publication statusPublished - 1986
MoE publication typeA1 Journal article-refereed

Fingerprint

Adenosine Monophosphate
Metabolites
Liver
activation
Ethanol
alcohol
cause
Acetates
nucleoside triphosphate-adenylate kinase
Acetate-CoA Ligase
Phosphorylation
Citric Acid Cycle
Acetaldehyde
Butyrates
Alcohol Dehydrogenase
Portal Vein
Guanosine Triphosphate
Oxidation-Reduction
Rats
Chemical activation

Cite this

Lindros, Kai O. ; Kivikataja, Raija-Liisa ; Suokas, Antti. / Elevation by ethanol and its metabolites of liver adenosine monophosphate. In: Alcohol. 1986 ; Vol. 3, No. 1. pp. 63-67.
@article{d331567939524b8ba62cba2ac304c262,
title = "Elevation by ethanol and its metabolites of liver adenosine monophosphate",
abstract = "Acute ethanol administration significantly increased the concentration of adenosine monophosphate (5′-AMP) in the intact freeze-clamped rat liver regardless of the ethanol dose administered. The increase was abolished by the alcohol dehydrogenase inhibitor 4-methylpyrazole, but was also seen after direct infusion of acetaldehyde into the portal vein. Administration of acetate to give hepatic levels similar to those seen during ethanol oxidation failed, however, to cause an increase in AMP. After ethanol administration there was a highly significant positive correlation between individual AMP levels and 3-OH-butyrate/acetoacetate ratios. The results suggest that the increase in liver AMP reflects activation of ethanol-derived acetate by acetothiokinase in the mitochondrial matrix. Ethanol, but not acetate inhibits the citric acid cycle, as reflected by the shift in the mitochondrial redox state. This could inhibit production of GTP needed for AMP phosphorylation by GTP-AMP phosphotransferase, thus explaining the accumulation",
author = "Lindros, {Kai O.} and Raija-Liisa Kivikataja and Antti Suokas",
year = "1986",
doi = "10.1016/0741-8329(86)90072-8",
language = "English",
volume = "3",
pages = "63--67",
journal = "Alcohol",
issn = "0741-8329",
publisher = "Elsevier",
number = "1",

}

Elevation by ethanol and its metabolites of liver adenosine monophosphate. / Lindros, Kai O.; Kivikataja, Raija-Liisa; Suokas, Antti.

In: Alcohol, Vol. 3, No. 1, 1986, p. 63-67.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Elevation by ethanol and its metabolites of liver adenosine monophosphate

AU - Lindros, Kai O.

AU - Kivikataja, Raija-Liisa

AU - Suokas, Antti

PY - 1986

Y1 - 1986

N2 - Acute ethanol administration significantly increased the concentration of adenosine monophosphate (5′-AMP) in the intact freeze-clamped rat liver regardless of the ethanol dose administered. The increase was abolished by the alcohol dehydrogenase inhibitor 4-methylpyrazole, but was also seen after direct infusion of acetaldehyde into the portal vein. Administration of acetate to give hepatic levels similar to those seen during ethanol oxidation failed, however, to cause an increase in AMP. After ethanol administration there was a highly significant positive correlation between individual AMP levels and 3-OH-butyrate/acetoacetate ratios. The results suggest that the increase in liver AMP reflects activation of ethanol-derived acetate by acetothiokinase in the mitochondrial matrix. Ethanol, but not acetate inhibits the citric acid cycle, as reflected by the shift in the mitochondrial redox state. This could inhibit production of GTP needed for AMP phosphorylation by GTP-AMP phosphotransferase, thus explaining the accumulation

AB - Acute ethanol administration significantly increased the concentration of adenosine monophosphate (5′-AMP) in the intact freeze-clamped rat liver regardless of the ethanol dose administered. The increase was abolished by the alcohol dehydrogenase inhibitor 4-methylpyrazole, but was also seen after direct infusion of acetaldehyde into the portal vein. Administration of acetate to give hepatic levels similar to those seen during ethanol oxidation failed, however, to cause an increase in AMP. After ethanol administration there was a highly significant positive correlation between individual AMP levels and 3-OH-butyrate/acetoacetate ratios. The results suggest that the increase in liver AMP reflects activation of ethanol-derived acetate by acetothiokinase in the mitochondrial matrix. Ethanol, but not acetate inhibits the citric acid cycle, as reflected by the shift in the mitochondrial redox state. This could inhibit production of GTP needed for AMP phosphorylation by GTP-AMP phosphotransferase, thus explaining the accumulation

U2 - 10.1016/0741-8329(86)90072-8

DO - 10.1016/0741-8329(86)90072-8

M3 - Article

VL - 3

SP - 63

EP - 67

JO - Alcohol

JF - Alcohol

SN - 0741-8329

IS - 1

ER -