Document Detail


Na+-stimulated ATPase activities in basolateral plasma membranes from guinea-pig small intestinal epithelial cells.
MedLine Citation:
PMID:  2981548     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
Two ATPase activities, a Na+-ATPase and a (Na+ + K+)-ATPase, have been found associated with sheets of basolateral plasma membranes from guinea-pig small intestinal epithelial cells. The specific activity of the former is 10-15% of the latter. The two ATPase activities differ in their affinity for Na+, their optimal pH, their K+ requirement and particularly in their behaviour in the presence of some inhibitors and of Ca2+. Thus the Na+-ATPase is refractory to ouabain but it is strongly inhibited by ethacrynic acid and furosemide, whilst the (Na+ + K+)-ATPase is totally suppressed by ouabain, partially by ethacrynic acid and refractory to furosemide. In addition, the Na+-ATPase is activated by micromolar concentrations of calcium and by resuspension of the membrane preparation at pH 7.8. The Na+-ATPase is only stimulated by sodium and to a lesser extent by lithium; however, this stimulation is independent of the anion accompanying Na+. The latter rules out the participation of an anionic ATPase. The relation between the characteristics of the sodium transport mechanism in basolateral membrane vesicles (Del Castillo, J.R. and Robinson, J.W.L. (1983) Experientia 39,631) and those of the two ATPase activities present in the same membranes, allow us to postulate the existence of two separate sodium pumps in this membranes. Each pump would derive the necessary energy for active ion transport from the hydrolysis of ATP, catalyzed by different ATPase systems.
Authors:
J R Del Castillo; J W Robinson
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't    
Journal Detail:
Title:  Biochimica et biophysica acta     Volume:  812     ISSN:  0006-3002     ISO Abbreviation:  Biochim. Biophys. Acta     Publication Date:  1985 Jan 
Date Detail:
Created Date:  1985-03-11     Completed Date:  1985-03-11     Revised Date:  2007-11-15    
Medline Journal Info:
Nlm Unique ID:  0217513     Medline TA:  Biochim Biophys Acta     Country:  NETHERLANDS    
Other Details:
Languages:  eng     Pagination:  413-22     Citation Subset:  IM    
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MeSH Terms
Descriptor/Qualifier:
Adenosine Triphosphatases / metabolism*
Animals
Basement Membrane / enzymology
Ca(2+) Mg(2+)-ATPase
Calcium / metabolism
Cation Transport Proteins*
Cell Membrane / drug effects,  enzymology*
Epithelium / enzymology
Ethacrynic Acid / pharmacology
Furosemide / pharmacology
Guinea Pigs
Intestine, Small / cytology*,  enzymology
Nucleotides / pharmacology
Ouabain / pharmacology
Sodium-Potassium-Exchanging ATPase / metabolism
Chemical
Reg. No./Substance:
0/Cation Transport Proteins; 0/Nucleotides; 54-31-9/Furosemide; 58-54-8/Ethacrynic Acid; 630-60-4/Ouabain; 7440-70-2/Calcium; EC 3.6.1.-/Adenosine Triphosphatases; EC 3.6.1.-/Ca(2+) Mg(2+)-ATPase; 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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