Document Detail


High pressure-induced changes of biological membrane. Study on the membrane-bound Na(+)/K(+)-ATPase as a model system.
MedLine Citation:
PMID:  11784304     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
In order to study the pressure-induced changes of biological membrane, hydrostatic pressures of from 0.1 to 400 MPa were applied to membrane-bound Na(+)/K(+)-ATPase from pig kidney as a model system of protein and lipid membrane. The activity showed at least a three-step change induced by pressures of 0.1-100 MPa, 100-220 MPa, and 220 MPa or higher. At pressures of 100 MPa or lower a decrease in the fluidity of lipid bilayer and a reversible conformational change in transmembrane protein is induced, leading to the functional disorder of membrane-associated ATPase activity. A pressure of 100-220 MPa causes a reversible phase transition in parts of the lipid bilayer from the liquid crystalline to the gel phase and the dissociation of and/or conformational changes in the protein subunits. These changes could cause a separation of the interface between alpha and beta subunits and between protein and the lipid bilayer to create transmembrane tunnels at the interface. Tunnels would be filled with water from the aqueous environment and take up tritiated water. A pressure of 220 MPa or higher irreversibly destroys and fragments the gross membrane structure, due to protein unfolding and interface separation, which is amplified by the increased pressure. These findings provide an explanation for the high pressure-induced membrane-damage to subcellular organelles.
Authors:
Michiko Kato; Rikimaru Hayashi; Takeo Tsuda; Kazuya Taniguchi
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  European journal of biochemistry / FEBS     Volume:  269     ISSN:  0014-2956     ISO Abbreviation:  Eur. J. Biochem.     Publication Date:  2002 Jan 
Date Detail:
Created Date:  2002-01-10     Completed Date:  2002-02-21     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0107600     Medline TA:  Eur J Biochem     Country:  Germany    
Other Details:
Languages:  eng     Pagination:  110-8     Citation Subset:  IM    
Affiliation:
Division of Applied Life Sciences, Graduate School of Agriculture, Kyoto University, Japan. mk@kais.kyoto-u.ac.jp
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / metabolism
Animals
Cation Transport Proteins / metabolism
Cell Membrane / enzymology*
Fluorescence
Humans
Lipid Bilayers / chemistry
Membrane Proteins / chemistry
Phosphoric Monoester Hydrolases / metabolism
Pressure
Sodium-Potassium-Exchanging ATPase / metabolism*
Chemical
Reg. No./Substance:
0/Cation Transport Proteins; 0/Lipid Bilayers; 0/Membrane Proteins; EC 3.1.3.-/Phosphoric Monoester Hydrolases; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/sodium-translocating ATPase; 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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