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Stabilizing and destabilizing effects on plasma membrane Ca2+-ATPase activity

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Abstract

We have examined the temperature-dependent effects of several organic compounds on the activity of the purified Ca2+-ATPase of erythrocytes. The monomeric enzyme was activated either by interaction with calmodulin or by oligomerization in the absence of calmodulin. Of the four homologous solute series studied including polyols, alkanols, aprotic solvents, and N-methyl derivatives of formamide and acetamide only polyols stabilized the enzyme over a broad range of concentration and temperature. Similarity of Ca2+-ATPase activity patterns at 25 and 37°C and in the presence of glycerol is in agreement with indirect, stabilizing interactions. Glycerol also protected the Ca2+-ATPase from thermal denaturation at 45°C. Within each homologous series, inhibitory effects increased with increasing solute concentration and with increasing structural similarity to detergents, indicating that direct destabilizing interactions are responsible for the observed inhibition. These were comparable to the destabilizing effect of urea. Oligomers were more resistant to all inhibitory solutes as compared to calmodulin-activated monomers suggesting that the nonpolar patches of the oligomerized enzyme are less accessible to solutes.

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Author notes

  1. Alicja Wawrzynow

    Present address: Institute of Chemistry, University of Gdansk, Gdansk, Poland

Authors and Affiliations

  1. Department of Anesthesiology/CCM, The Johns Hopkins University School of Medicine, 600 N. Wolfe St, Blalock 1404, 21287, Baltimore, Maryland, USA

    Danuta Kosk-Kosicka, Alicja Wawrzynow & Grazyna Roszczynska

Authors
  1. Danuta Kosk-Kosicka
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  2. Alicja Wawrzynow
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  3. Grazyna Roszczynska
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Kosk-Kosicka, D., Wawrzynow, A. & Roszczynska, G. Stabilizing and destabilizing effects on plasma membrane Ca2+-ATPase activity. Mol Cell Biochem 139, 1–9 (1994). https://doi.org/10.1007/BF00944197

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  • DOI: https://doi.org/10.1007/BF00944197

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