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Science 9 February 1990: Vol. 247. no. 4943, pp. 723 - 726 DOI: 10.1126/science.2154036
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Articles
Science, Vol 247, Issue 4943, 723-726
Copyright © 1990 by American Association for the Advancement of Science
Growth factors induce phosphorylation of the Na+/H+ antiporter, glycoprotein of 110 kD
C Sardet,
L Counillon,
A Franchi,
and
J Pouyssegur
Centre de Biochimie-CNRS, Nice, France.
The Na+/H+ antiporter, which regulates intracellular pH in virtually all cells, is one of the best examples of a mitogen- and oncogene-activated membrane target whose activity rapidly changes on stimulation. The activating mechanism is unknown. A Na+/H+ antiporter complementary DNA fragment was expressed in Escherichia coli as a beta-galactosidase fusion protein, and a specific antibody to the fusion protein was prepared. Use of this antibody revealed that the Na+/H+ antiporter is a 110-kilodalton glycoprotein that is phosphorylated in growing cells. Mitogenic activation of resting hamster fibroblasts and A431 human epidermoid cells with epidermal growth factor, thrombin, phorbol esters, or serum, stimulated phosphorylation of the Na+/H+ antiporter with a time course similar to that of the rise in intracellular pH.
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