Hypoxia induced metabolism dysfunction of rat astrocytes in primary cell cultures.
In order to study the astroglial contribution to hypoxic injury on brain tissue metabolism, modifications of glutamine synthetase (GS) lactate dehydrogenase (LDH) enolase and malate dehydrogenase activity produced by reduced oxygen supply have been determined in primary cultures of astrocytes prepared from newborn rat cerebral cortex. Enzymatic activities were measured immediately after the hypoxic treatment (9 h) and during post injury recovery. GS level is significantly decreased in response to low oxygen pressure and increased above control value during the post hypoxic recovery period. The magnitude of GS reduction by hypoxia depends on the age of the cells in culture. Lactate dehydrogenase and enolase levels were significantly enhanced during the two periods considered. No modification of the MDH level was observed. The synthesis of LDH isoenzymes containing mainly M subunits is specifically induced by hypoxia. Our results suggest that astroglial cells may represent a particularly sensitive target toward hypoxia injury in brain tissue. Low oxygen pressure available may modify some fundamental metabolical functions of these cells such as glutamate turnover and lactic acid accumulation.
Centre de Neurochimie, CNRS 5, Strasbourg, France.
G
G
Tholey
J C
JC
Copin
M
M
Ledig
D000818:Animals; D000831:Animals, Newborn; D001253:Astrocytes / Q000201:enzymology*; D015687:Cell Hypoxia; D002478:Cells, Cultured; D002540:Cerebral Cortex / Q000201:enzymology*; D005974:Glutamate-Ammonia Ligase / Q000378:metabolism*; D007527:Isoenzymes; D007700:Kinetics; D007770:L-Lactate Dehydrogenase / Q000378:metabolism*; D008291:Malate Dehydrogenase / Q000378:metabolism*; D010751:Phosphopyruvate Hydratase / Q000378:metabolism*; D051381:Rats
D007527:Isoenzymes; D007770:L-Lactate Dehydrogenase; D008291:Malate Dehydrogenase; D010751:Phosphopyruvate Hydratase; D005974:Glutamate-Ammonia Ligase