Release of compartment-specific enzymes from neonatal rat heart cell cultures during anoxia and reoxygenation

The effects of anoxia and substrate deprivation on the extent of the release of several intracellular marker enzymes and DNA were studied using monolayer cultures of neonatal rat heart cells. After varying periods of anoxia, in a number of experiments followed by 1 h of reoxygenation and substrate r...

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Bibliographic Details
Published in:Cardiovascular research 1984-02, Vol.18 (2), p.99-106
Main Authors: ALTONA, J C, VAN DER LAARSE, A, VAN TRESLONG, C H F BLOYS
Format: Article
Language:English
Subjects:
5'-Nucleotidase
Acetylglucosaminidase - metabolism
Animals
anoxia
Aspartate Aminotransferases - metabolism
Biological and medical sciences
Cathepsin D
Cathepsins - metabolism
Cells, Cultured
DNA - metabolism
enzyme release
Fundamental and applied biological sciences. Psychology
Glucuronidase - metabolism
Heart
heart cell cultures
Hydroxybutyrate Dehydrogenase - metabolism
Isoenzymes
L-Lactate Dehydrogenase - metabolism
Leucyl Aminopeptidase - metabolism
Monoamine Oxidase - metabolism
Myocardium - enzymology
Myocardium - metabolism
Nucleotidases - metabolism
Oxygen
Rats
reoxygenation
Succinate Cytochrome c Oxidoreductase - metabolism
Time Factors
Vertebrates: cardiovascular system
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Summary:The effects of anoxia and substrate deprivation on the extent of the release of several intracellular marker enzymes and DNA were studied using monolayer cultures of neonatal rat heart cells. After varying periods of anoxia, in a number of experiments followed by 1 h of reoxygenation and substrate repletion, the cells were analysed for cytoplasmic, lysosomal, and mitochondrial enzymes, and for nuclear DNA. Cellular enzyme activity and DNA content at any time during incubation were compared with the remaining activity of α-hydroxybutyrate dehydrogenase (HBDH), a cytoplasmic enzyme. The study demonstrates that the ultimate extent of enzyme depletion induced by anoxia with or without reoxygenation, is high (>80%) for cytoplasmic enzymes, is intermediate for sarcolemmal and lysosomal enzymes, and enzyme associated with the mitochondrial outer membrane (about 50%) and small (
ISSN:0008-6363
1755-3245
DOI:10.1093/cvr/18.2.99