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Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase

The occurrence of Hofmeister (specific ion) effects in various membrane-related physiological processes is well documented. For example the effect of anions on the transport activity of the ion pump Na(+), K(+)-ATPase has been investigated. Here we report on specific anion effects on the ATP-depende...

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Autores principales: Tadini-Buoninsegni, Francesco, Moncelli, Maria Rosa, Peruzzi, Niccolò, Ninham, Barry W., Dei, Luigi, Nostro, Pierandrea Lo
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4593048/
https://www.ncbi.nlm.nih.gov/pubmed/26435197
http://dx.doi.org/10.1038/srep14282
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author Tadini-Buoninsegni, Francesco
Moncelli, Maria Rosa
Peruzzi, Niccolò
Ninham, Barry W.
Dei, Luigi
Nostro, Pierandrea Lo
author_facet Tadini-Buoninsegni, Francesco
Moncelli, Maria Rosa
Peruzzi, Niccolò
Ninham, Barry W.
Dei, Luigi
Nostro, Pierandrea Lo
author_sort Tadini-Buoninsegni, Francesco
collection PubMed
description The occurrence of Hofmeister (specific ion) effects in various membrane-related physiological processes is well documented. For example the effect of anions on the transport activity of the ion pump Na(+), K(+)-ATPase has been investigated. Here we report on specific anion effects on the ATP-dependent Ca(2+) translocation by the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA). Current measurements following ATP concentration jumps on SERCA-containing vesicles adsorbed on solid supported membranes were carried out in the presence of different potassium salts. We found that monovalent anions strongly interfere with ATP-induced Ca(2+) translocation by SERCA, according to their increasing chaotropicity in the Hofmeister series. On the contrary, a significant increase in Ca(2+) translocation was observed in the presence of sulphate. We suggest that the anions can affect the conformational transition between the phosphorylated intermediates E(1)P and E(2)P of the SERCA cycle. In particular, the stabilization of the E(1)P conformation by chaotropic anions seems to be related to their adsorption at the enzyme/water and/or at the membrane/water interface, while the more kosmotropic species affect SERCA conformation and functionality by modifying the hydration layers of the enzyme.
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spelling pubmed-45930482015-10-19 Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase Tadini-Buoninsegni, Francesco Moncelli, Maria Rosa Peruzzi, Niccolò Ninham, Barry W. Dei, Luigi Nostro, Pierandrea Lo Sci Rep Article The occurrence of Hofmeister (specific ion) effects in various membrane-related physiological processes is well documented. For example the effect of anions on the transport activity of the ion pump Na(+), K(+)-ATPase has been investigated. Here we report on specific anion effects on the ATP-dependent Ca(2+) translocation by the sarcoplasmic reticulum Ca(2+)-ATPase (SERCA). Current measurements following ATP concentration jumps on SERCA-containing vesicles adsorbed on solid supported membranes were carried out in the presence of different potassium salts. We found that monovalent anions strongly interfere with ATP-induced Ca(2+) translocation by SERCA, according to their increasing chaotropicity in the Hofmeister series. On the contrary, a significant increase in Ca(2+) translocation was observed in the presence of sulphate. We suggest that the anions can affect the conformational transition between the phosphorylated intermediates E(1)P and E(2)P of the SERCA cycle. In particular, the stabilization of the E(1)P conformation by chaotropic anions seems to be related to their adsorption at the enzyme/water and/or at the membrane/water interface, while the more kosmotropic species affect SERCA conformation and functionality by modifying the hydration layers of the enzyme. Nature Publishing Group 2015-10-05 /pmc/articles/PMC4593048/ /pubmed/26435197 http://dx.doi.org/10.1038/srep14282 Text en Copyright © 2015, Macmillan Publishers Limited http://creativecommons.org/licenses/by/4.0/ This work is licensed under a Creative Commons Attribution 4.0 International License. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in the credit line; if the material is not included under the Creative Commons license, users will need to obtain permission from the license holder to reproduce the material. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/
spellingShingle Article
Tadini-Buoninsegni, Francesco
Moncelli, Maria Rosa
Peruzzi, Niccolò
Ninham, Barry W.
Dei, Luigi
Nostro, Pierandrea Lo
Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase
title Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase
title_full Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase
title_fullStr Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase
title_full_unstemmed Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase
title_short Hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum Ca(2+)-ATPase
title_sort hofmeister effect of anions on calcium translocation by sarcoplasmic reticulum ca(2+)-atpase
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4593048/
https://www.ncbi.nlm.nih.gov/pubmed/26435197
http://dx.doi.org/10.1038/srep14282
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