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KMID : 0613820100200030416
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Journal of Life Science
2010 Volume.20 No. 3 p.416 ~ p.423
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Variation of Lactate Dehydrogenase Isozymes in Angelfish (Pterophyllum scalare) according to Acute Environmental Change
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An Chang-Su
Cho Sung-Kyu
Yum Jung-Joo
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Abstract
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In this study, the properties and gene expression of the lactate dehydrogenase (EC 1.1.1.27, LDH) isozyme were studied in angelfish (Pterophyllum scalare) - known for their adaptation to the low oxygen environment of the tropics ?. which were acclimated to acute temperature change (27±0.5→18±0.5℃) and dissolved oxygen (DO) change (6±1→18 ppm) for 2 hours. The properties of the LDH isozymes were confirmed in the native-polyacrylamide gel electrophoresis, Western blot analysis and enzyme activity measurement. Liver- and eye-specific Ldh-C gene were expressed in liver, eye and brain tissues. Through Western blot analysis, the LDH A₄ isozyme was shown to have a more cathodal mobility relative to the B₄ isozyme. In the liver tissue, the LDH A₄ isozyme increased with temperature drop while the B₄ isozyme decreased. The LDH A₄ and C₄ isozymes increased with DO increment, while the B₄ isozyme decreased. In the eye tissue, the LDH A₄ and B₄ isozymse increased with temperature drop while the C₄ isozyme decreased. The LDH A₄ and B₄ isozymes increased with DO increment, but the C₄ isozyme and isozymes including the subunit C decreased. In the heart tissue, LDH activity increased with DO increment, as well as the LDH B₄ isozyme. In the brain tissue, the LDH A₄ and B₄ isozymes increased with temperature drop. The LDH B₄ isozyme increased with DO increment. Accordingly, since the liver- and eye-specific Ldh-C are influenced by changes in DO and the LDH B₄ and C₄ isozymes are relatively controlled in the liver and eye tissues, the C₄ isozyme can be considered to have a lactate oxidase function.
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KEYWORD
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Angelfish (Pterophyllum scalare), lactate dehydrogenase, isozyme, temperature, DO
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