The Effects of Lanthanoid on the Structure-Function of Lactate Dehydrogenase from Mice Heart
2009
Li, Na | Duan, Yanmei | Zhou, Min | Liu, Chao | Hong, Fashui
The activity of lactate dehydrogenase (LDH, EC1.1.1.27) is often changed upon inflammatory responses in animals. Lanthanoid (Ln) was shown to provoke various inflammatory responses both in rats and mice; however, the molecular mechanism by which Ln³⁺ exert its toxicity has not been completely understood, especially that we know little about the mechanism of the interaction between Ln with 4f electron shell and alternation valence and LDH. In this report, we investigated the mechanisms of LaCl₃, CeCl₃, and NdCl₃ on LDH activity in vivo and in vitro. Our results showed that La³⁺, Ce³⁺, and Nd³⁺ could significantly activate LDH in vivo and in vitro; the order of activation was Ce³⁺ > Nd³⁺ > La³⁺ > control. The affinity of LDH for Ce³⁺ was higher than Nd³⁺ and La³⁺; the saturated binding sites for Ce³⁺ on the LDH protein were 1.2 and for La³⁺ and Nd³⁺ 1.55. Ln³⁺ caused the reduction of exposure degree of cysteine or tryptophan/tyrosine of LDH, the increase of space resistance, and the enhancement of α-helix in secondary structure of LDH, which was greatest in Ce³⁺ treatment, medium in Nd³⁺ treatment, and least in La³⁺ treatment. It implied that the changes of structure-function on LDH caused by Ln³⁺ were closely related to the characteristics of 4f electron shell and alternation valence in Ln.
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