| Intracellular sodium sensing: SIK1 network, hormone action and high blood pressure. | |
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MedLine Citation:
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PMID: 20347966 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Sodium is the main determinant of body fluid distribution. Sodium accumulation causes water retention and, often, high blood pressure. At the cellular level, the concentration and active transport of sodium is handled by the enzyme Na(+),K(+)-ATPase, whose appearance enabled evolving primitive cells to cope with osmotic stress and contributed to the complexity of mammalian organisms. Na(+),K(+)-ATPase is a platform at the hub of many cellular signaling pathways related to sensing intracellular sodium and dealing with its detrimental excess. One of these pathways relies on an intracellular sodium-sensor network with the salt-inducible kinase 1 (SIK1) at its core. When intracellular sodium levels rise, and after the activation of calcium-related signals, this network activates the Na(+),K(+)-ATPase and expel the excess of sodium from the cytosol. The SIK1 network also mediates sodium-independent signals that modulate the activity of the Na(+),K(+)-ATPase, like dopamine and angiotensin, which are relevant per se in the development of high blood pressure. Animal models of high blood pressure, with identified mutations in components of multiple pathways, also have alterations in the SIK1 network. The introduction of some of these mutants into normal cells causes changes in SIK1 activity as well. Some cellular processes related to the metabolic syndrome, such as insulin effects on the kidney and other tissues, also appear to involve the SIK1. Therefore, it is likely that this protein, by modulating active sodium transport and numerous hormonal responses, represents a "crossroad" in the development and adaptation to high blood pressure and associated diseases. |
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Authors:
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Ariel Jaitovich; Alejandro M Bertorello |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't; Review Date: 2010-03-27 |
Journal Detail:
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Title: Biochimica et biophysica acta Volume: 1802 ISSN: 0006-3002 ISO Abbreviation: Biochim. Biophys. Acta Publication Date: 2010 Dec |
Date Detail:
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Created Date: 2010-11-01 Completed Date: 2010-12-21 Revised Date: 2011-11-01 |
Medline Journal Info:
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Nlm Unique ID: 0217513 Medline TA: Biochim Biophys Acta Country: Netherlands |
Other Details:
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Languages: eng Pagination: 1140-9 Citation Subset: IM |
Copyright Information:
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Copyright © 2010 Elsevier B.V. All rights reserved. |
Affiliation:
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Department of Medicine, Karolinska Institutet, Karolinska University Hospital-Solna, 171 76 Stockholm, Sweden. ajaitovich@ccbhs.org |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Blood Pressure* Calcium Signaling* Cytosol / enzymology* Humans Insulin / genetics, metabolism Kidney / enzymology* Metabolic Syndrome X / enzymology, genetics Mice Mutation Protein-Serine-Threonine Kinases / genetics, metabolism* Sodium / metabolism* Sodium-Potassium-Exchanging ATPase / genetics, metabolism |
| Chemical | |
Reg. No./Substance:
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11061-68-0/Insulin; 7440-23-5/Sodium; EC 2.7.11.1/Protein-Serine-Threonine Kinases; EC 2.7.11.1/Sik1 protein, mouse; EC 3.6.3.9/Sodium-Potassium-Exchanging ATPase |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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