Anisodamine Causes the Changes of Structure and Function in the Transmembrane Domain of the Ca^<2+>-ATPase from Sarcoplasmic Reticulum

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概要

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•   The effects of anisodamine on the Ca2+-ATPsae of sarcoplasmic reticulum (SR) were investigated by using differential scanning calorimetry to measure the ability of anisodamine to denature the transmembrane domain and the cytoplasmic domain. Anisodamine significantly altered the thermotropic phase behaviors of the transmembrane domain of purified Ca2+-ATPase. Specifically, the melting temperature of the transmembrane domain moved toward lower temperatures with the concentrations of anisodamine increasing and the thermotropic phase peak was abolished at 10 mM, indicating that the stabilized structure of the transmembrane domain in the presence of Ca2+ could be destabilized by anisodamine. Decreases of the intrinsic fluorescence and increases of the extrinsic fluorescence of ANS, a fluorescent probe, showed the exposure of tryptophan and hydrophobic region, respectively, suggesting again that anisodamine caused a less compact conformation in the transmembrane domain. A marked inhibition of the Ca2+ uptake activity of SR Ca2+-ATPase was observed when the addition of anisodamine. The drug did not affect the cytoplasmic domain of the enzyme and only slightly decreased the ATPase activity of the enzyme at concentrations up to 10 mM. This was likely due to the destabilized protein transmembrane domain. To sum up, our results revealed that anisodamine interacted specifically with the transmembrane domain of SR Ca2+-ATPase and inhibited the Ca2+ uptake activity of the enzyme.

• 社団法人 日本農芸化学会の論文
• 2004-01-23

著者

• CHEN Jian-Wen

  National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica

• Chen Jian-wen

  National Laboratory Of Biomacromolecules Institute Of Biophysics Academia Sinica

• PANG Yu-Hong

  National Laboratory of Biomacromolecules, Institute of Biophysics, Academia Sinica

• Pang Yu-hong

  National Laboratory Of Biomacromolecules Institute Of Biophysics Academia Sinica

関連論文

• The Behaviors of Ca^-ATPase Embedded in Interdigitated Bilayer
• Effect of Cholesterol on the Formation of an Interdigitated Gel Phase in Lysophosphatidylcholine and Phosphatidylcholine Binary Mixtures^1
• More Ordered, Convex Ganglioside-Enriched Membrane Domains : The Effects of GM_1 on Sphingomyelin Bilayers Containing a Low Level of Cholesterol
• Anisodamine Causes the Changes of Structure and Function in the Transmembrane Domain of the Ca^-ATPase from Sarcoplasmic Reticulum
• Effect of Cholesterol on the Formation of an Interdigitated Gel Phase in Lysophosphatidylcholine and Phosphatidylcholine Binary Mixtures.

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