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Am J Physiol Renal Physiol 276: F10-F17, 1999;
0363-6127/99 $5.00
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Vol. 276, Issue 1, F10-F17, January 1999

Guanine nucleotide binding proteins in cultured renal epithelia: studies with pertussis toxin and aldosterone

Sarah Sariban-Sohraby1, Michal Svoboda2, and Frédérique Mies1

1 Laboratoire de Physiologie and 2 Laboratoire de Chimie Biologique, Université Libre de Bruxelles, 1070 Brussels, Belgium

The GTP-binding proteins from cultured A6 epithelia were examined in isolated membrane preparations. Binding of [35S]GTPgamma S revealed a class of binding sites with an apparent Kd value of 100 nM and a Bmax of 220 pmol/mg protein. Short-term aldosterone treatment of the cells did not modify the binding kinetics, whereas pertussis toxin (PTX) decreased Bmax by 50%. The mRNA levels for Galpha i-3, Galpha 0, Galpha s, and Galpha q were not increased after aldosterone. The patterns of small Mr G proteins and of PTX-ribosylated proteins were identical in membranes of both control and aldosterone-treated cells. Cross-linking of [alpha -32P]GTP, in control membranes, showed either no labeling or a faint band of Mr 59.5 kDa. This protein became prominent after aldosterone, and its labeling decreased with spironolactone. Thus short-term aldosterone does not promote increased expression of known heterotrimeric G proteins in epithelial membranes but activates resident PTX-sensitive Gi proteins and stimulates the expression of a specific GTP-binding protein of Mr 59.5 kDa.

A6 cells; photoaffinity labeling; sodium transport; GTP hydrolysis rate constant


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