Changes in enzyme pattern of ehrlich ascites tumor cells following serial cultivation in media with increased (hypertonic) NaCl content |
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Authors: | DO Schachtschabel J Yooktatat C Hirschhäuser |
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Institution: | Institut für Physiologische Chemie der Phillips-Universität, D-3550 Marburg, Lahnberge G.F.R. |
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Abstract: | Adaptation of Ehrlich ascites tumor cells to serial cultivation in media with progressively elevated (hypertonic) NaCl content (“high NaCl”-tolerant cells) has resulted in progressive increases of the cellular activities of NAD-dependent glycerol-3-phosohate dehydrogenase (EC 1.1.1.8), NAD-dependent malate dehydrogenase (EC 1.1.1.37), glutamate—oxalacetate transaminase (EC 2.6.1.1.), NAD(P)-dependent glutamate dehydrogenase (EC 1.4.1.3), NADP-dependent malate dehydrogenase (EC 1.1.1.40, “malic enzyme”) and NADP-dependent isocitrate dehydrogenase (EC 1.1.1.42). The activities of glutamate—pyruvate transaminase (EC 2.6.1.2.) and of glycolytic enzymes as phosphofructokinase (EC 2.7.1.11), glyceradehydephosphate dehydrogenase (EC 1.2.1.12) and lactate dehydrogenase (EC 1.1.1.27) were only slightly and not in progressive manner (in response to the progressive increase of the environmental NaCl concentration) affected. These changes are discussed with respect to a metabolic pattern of these “high NaCl”-tolerant cells which is compatible with increased energy requirements, especially for active cation transport. It is suggested that these increased cellular enzyme activitees reflect an increased transfer of reducing equivalents across mitochondrial membranes (via the “glycerophosphate cycle and the malate—aspartate shuttle”) and possibly a stimulated lipid metabolism. These alterations in the level of enzyme activities must be regarded as an adaptive cellular response to the “high NaCl” enviromment, since readaptation to growth in regular isotonic media resulted in a reversion to the enzyme pattern characteristic of the parent cells. |
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Keywords: | Requests for reprints should be sent to Professor Dr D Schachtschabel Institut fur Physiologische Chemie D-3550 Marburg/Lahn Lahnberge |
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