Metabolic adaptations to environmental changes in Caenorhabditis elegans

被引:14
|
作者
Paul, RJ
Gohla, J
Föll, R
Schneckenburger, H
机构
[1] Univ Munster, Inst Zoophysiol, D-48143 Munster, Germany
[2] Fachhsch Aalen, Inst Angew Forsch, D-73428 Aalen, Germany
关键词
adaptation; anoxia; Caenorhabditis elegans; enzyme activity; metabolic depression; NADH fluorescence; redox state; temperature adaptation;
D O I
10.1016/S0305-0491(00)00284-4
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Metabolic adaptations to environmental changes were studied in Caenorhabditis elegans. To assess adjustments in enzyme function, maximum activities of key enzymes of main metabolic pathways were determined. After a 12 h incubation at varying temperatures (10, 20 degreesC) and oxygen supplies (normoxia or anoxia), the activities of the following enzymes were determined at two measuring temperatures in tissue extracts: lactate dehydrogenase (LDH; anaerobic glycolysis), 3-hydroxyacyl-CoA-dehydrogenase (HCDH; fatty acid oxidation), isocitrate dehydrogenases (NAD-IDH, NADP-IDH; tricarboxylic acid cycle) and isocitrate lyase (ICL; glyoxylate cycle). Incubation at 20 degreesC induced a strong increase in maximum LDH activity. Anoxic incubation caused maximum HCDH and NADP-IDH activities and, at 10 degreesC incubation, LDH activity to increase. Maximum NAD-IDH and ICL activities were not influenced by any type of incubation. In order to study the time course of metabolic adaptations to varying oxygen supplies, relative quantities of free and protein-bound NADH were determined in living C. elegans using time-resolved fluorescence spectroscopy. During several hours of anoxia, free and protein-bound NADH showed different time courses. One main result was that just at the moment when the protein-bound NADH had reached a constant level, and the free NADH started to increase rapidly, the worms fell into a rigor state. The data on enzyme activity and NADH fluorescence can be interpreted on the basis of a two-stage model of anaerobiosis. (C) 2000 Elsevier Science Inc. All rights reserved.
引用
收藏
页码:469 / 479
页数:11
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