We have compared effects of dimethylsulfoxide (Me2SO) and two polyols on the Ca2+-ATPase purified from human erythrocytes. As studied under steady-state conditions over a broad solute concentration range and temperature, Me2SO, glycerol, and xylitol do not inhibit the Ca2+-ATPase activity; this is in contrast to numerous other organic solutes that we have investigated. Under specific experimental conditions, Me2SO (but not glycerol) substantially increases Ca2+-ATPase activity, suggesting a possible facilitation of enzyme oligomerization. The activation is more pronounced at low Ca2+ concentrations. In contrast to glycerol, Me2SO shows no protective effect on enzyme structure as assessed by determining residual Ca2+-ATPase activity after exposing the enzyme to thermal denaturation at 45°C. Under these conditions several other organic solutes strongly enhance the denaturating effect of temperature. Because of the temperature dependence of its effect on the Ca2+-ATPase activity we believe that Me2SO activates the Ca2+-ATPase by indirect water-mediated interactions.
This is a preview of subscription content, log in to check access.
Buy single article
Instant access to the full article PDF.
Price includes VAT for USA
Subscribe to journal
Immediate online access to all issues from 2019. Subscription will auto renew annually.
This is the net price. Taxes to be calculated in checkout.
Wang KK, Villalobo A, Roufogalis BD: The plasma membrane calcium pump: a mutliregulated transporter. Trends Cell Biol 2: 46–52, 1992
Kosk-Kosicka D, Inesi G: Cooperative calcium binding and calmodulin regulation in the calcium-dependent adenosine triphosphatase purified from the erythrocyte membrane. FEBS Lett 189: 67–71, 1985
Kosk-Kosicka D, Scaillet S, Inesi G: The partial reactions in the catalyic cycle of the calcium dependent adenosinetriphosphatase purified from erythrocyte membranes. J Biol Chem 261: 3333–3338, 1986
Kosk-Kosicka D, Bzdega T: Activation of the erythrocyte Ca2+-ATPase by either self-association or interaction with calmodulin. J Biol Chem 263: 18184–18189, 1988
Kosk-Kosicka D, Bzdega T, Wawrzynow A: Fluorescence energy transfer studies of purified erythrocyte Ca2+-ATPase. J Biol Chem 264: 19495–19499, 1989
Kosk-Kosicka D, Bzdega T: Effects of calmodulin on erythrocyte Ca2+-ATPase activation and oligomerization. Biochemistry 29: 3772–3777, 1990
Kosk-Kosicka D, Bzdega T, Johnson JD: Fluorescence studies on calmodulin binding to erythrocyte Ca2+-ATPase in different oligomerization states. Biochemistry 29: 1875–1879, 1990
Kosk-Kosicka D: Comparison of the red cell Ca2+-ATPase in ghost membranes and after purification. Mol Cell Biochem 99: 75–81, 1990
Kosk-Kosicka D, Bzdega T: Regulation of the erythrocyte Ca2+-ATPase by mutant calmodulins with positively charged amino acid substitutions. Biochemistry 30: 66–70, 1991
Bzdega T, Kosk-Kosicka D: Regulation of the erythrocyte Ca2+-ATPase by mutated calmodulins with Glu Ala substitutions in the Ca2+ binding domains. J Biol Chem 267: 4394–4397, 1992
Kosk-Kosicka D, Bzdega T, Wawrzynow A, Watterson DM, Lukas T: Site-specific amino acid alterations in Ca2+-binding domains in calmodulin impair activation of RBC Ca2+-ATPase. Biophys J 62: 77–78, 1992
Persechini A, Jarret H, Kosk-Kosicka D, Krinks M, Lee H: Activation of enzymes by calmodulins containing intramolecular cross-links. Biochim Biophys Acta 1163: 309–314, 1993
Kosk-Kosicka D, Wawrzynow A, Roszczynska G: Different solute sensitivity for the RBC plasma membrane Ca2+-ATPase activation in the calmodulin-dependent and calmodulin-independent pathways. Ann NY Acad Sci 671: 424–427, 1992
Kosk-Kosicka D, Wawrzynow A, Roszczynska G: Stabilizing and destabilizing effects on plasma membrane Ca2+-ATPase activity. Mol Cell Biochem 139: 1–9, 1994
deMeis L, Martins O, Alves E: Role of water, hydrogen ion, and temperature on the synthesis of adenosine triphosphate by the sarcoplasmic reticulum adenosine triphosphatase in the absence of a calcium ion gradient. Biochemistry 19: 4252–4261, 1980.
deMeis L, Inesi G: Intrinsic regulation of substrate fluxes and energy conservation in Ca2+-ATPase. FEBS Lett 185: 135–138, 1985
The R, Hasselbach W: Stimulatory and inhibitory effects of dimethyl sulfoxide and ethylene glycol on ATPase activity and calcium transport of sarcoplasmic reticulum. Eur J Biochem 74: 611–621, 1977
Benaim G, deMeis L: Activation of the purified erythrocyte plasma membrane Ca2+-ATPase by organic solvents. FEBS Lett 244: 484–486, 1989
Benaim G, deMeis L: Similarities between the effects of dimethyl sulfoxide and calmodulin on the red blood cell Ca2+-ATPase. Biochim Biophys Acta 1026: 87–92, 1990
Romero PJ: Inhibition of the human erythrocyte calcium pump by dimethyl sulfoxide. Cell Calcium 13: 659–667, 1992
Collins KD, Washabaugh MW: The Hofmeister effect and the behaviour of water at interfaces. Quart Rev Biophys 18: 323–422, 1985
Combes D, Graber M, Ye WN: Stabilizing effect of polyhydric alcohols: influence of the enzyme. Ann NY Acad Sci 613: 559–563, 1990
About this article
Cite this article
Kosk-Kosicka, D., Roszczyńska, G. Neutral organic solute effects on the activity of the plasma membrane Ca2+-ATPase. Mol Cell Biochem 140, 195–199 (1994). https://doi.org/10.1007/BF00926758
- purified enzyme
- Ca2+-ATPase activity