The subcellular distribution and properties of aldehyde dehydrogenase of hepatoma AH-130.

Abstract

Aldehyde dehydrogenase subcellular distribution and activity were studied in the Yoshida hepatoma AH-130 and rat liver. NAD+- and NADP+-dependent dehydrogenase activities were lower in all hepatoma subfractions (except the cytosol) than in liver subfractions. In the presence of 0.025 mM substrate 78-80% of the liver NAD+- or NADP+-dependent aldehyde dehydrogenase was found in the mitochondria. With 10 mM substrate the enzyme activity was primarily in the mitochondria and microsomes. In the hepatoma a sharp increase of the soluble aldehyde dehydrogenase (either NAD+- or NADP+ dependent) was observed at all substrate concentrations. The Km of the different isoenzymes (either identified by their localization or coenzyme dependency) were of the same order for liver and hepatoma. However, a high Km enzyme was present in liver mitochondria outer membranes but not in hepatoma. Hepatoma acetaldehyde dehydrogenase was inhibited, as was the liver enzyme, by diethyldithiocarbamate. The return of activity was slower for the hepatoma and neonatal liver than for the adult liver enzyme.

• Authors: R A Canuto, R Garcea, M Biocca, R Pascale, L Pirisi, F Feo
• Journal: European journal of cancer & clinical oncology (Eur J Cancer Clin Oncol) Vol. 19 Issue 3 Pg. 389-400 (Mar 1983) ISSN: 0277-5379 [Print] England
• PMID: 6305666 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Isoenzymes
• Ditiocarb
• Aldehyde Oxidoreductases
• Acetaldehyde

Topics

• Acetaldehyde (metabolism)
• Aldehyde Oxidoreductases (antagonists & inhibitors, metabolism)
• Animals
• Ditiocarb (pharmacology)
• Isoenzymes (metabolism)
• Liver (enzymology)
• Liver Neoplasms, Experimental (enzymology)
• Male
• Microsomes, Liver (enzymology)
• Mitochondria, Liver (enzymology)
• Rats
• Rats, Inbred Strains
• Subcellular Fractions (enzymology)