Membrane fluidity and enzyme activities in brush border and basolateral membranes of the dog kidney

C. Le Grimellec, M. C. Giocondi, B. Carriere, S. Carriere and J. Cardinal The physical state of membrane lipids and relationships with the activity of Na+-K+-ATPase and alkaline phosphatase were studied in basolateral and brush border membranes of the dog kidney. Fluorescence polarization and electr...

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Veröffentlicht in:American journal of physiology. Renal physiology 1982-03, Vol.242 (3), p.246-F253
Hauptverfasser: Le Grimellec, C, Giocondi, M. C, Carriere, B, Carriere, S, Cardinal, J
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Sprache:eng
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Zusammenfassung:C. Le Grimellec, M. C. Giocondi, B. Carriere, S. Carriere and J. Cardinal The physical state of membrane lipids and relationships with the activity of Na+-K+-ATPase and alkaline phosphatase were studied in basolateral and brush border membranes of the dog kidney. Fluorescence polarization and electron spin resonance experiments demonstrate that basolateral membranes are much more fluid than brush border membranes. This can be accounted for by a difference in fluidity of the lipid part of the membranes. Broad (43-17 degrees C) thermotropic transitions are observed in liposomes made from total lipid extracts of brush border and basolateral membranes. Fluorescence data strongly suggest that thermotropic transitions also occur in intact membranes and that a change in membrane physical state may take place around the physiological temperature. A nonlinear Arrhenius plot for the Na+-K+-ATPase activity in basolateral membranes (breakpoint 21 degrees C) provides additional support for the existence of a lipid liquid leads to gel transition in antiluminal plasma membranes. A break in the Arrhenius plot of alkaline phosphatase activity is also observed but at a temperature significantly higher (26 degrees C) than that of the end of the thermotropic transition. "Room temperature" appears as a critical zone for lipid physical state and activities of both enzymes.
ISSN:0363-6127
0002-9513
1931-857X
2161-1157
1522-1466
DOI:10.1152/ajprenal.1982.242.3.f246