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J. Biol. Chem., Vol. 266, Issue 32, 21335-21338, Nov, 1991
BM Rayson
The Na+/K(+)-ATPase enzyme is a pivotal regulator of intracellular
electrolyte levels in animal cells. Changes in the rate of its synthesis
have been demonstrated to mediate a number of physiological responses. The
cellular mechanisms implicated in such regulatory responses though remain
poorly defined. Specifically, no intracellular mediators have previously
been established. We now describe for the first time, one putative
mediator: [Ca2+]i. Elevations in [Ca2+]i stimulate levels of mRNA alpha 1
and mRNA beta 1, sequences which encode both the catalytic subunit of the
enzyme, the alpha subunit, and the glycosylated subunit, the beta subunit.
These results suggest that elevations in [Ca2+]i modulate the synthetic
rate of the active enzyme, and consequently changes in [Ca2+]i may mediate
the regulation of its synthetic rate in a range of physiological settings.
The mRNA alpha 1 response to the elevation of [Ca2+]i appears, at least
partly, to reflect an increase in transcription rate. However, no such
increase in transcription rate of the beta 1 subunit gene was detectable.
Thus the mRNA beta 1 response, under conditions of elevated [Ca2+]i, may be
explained by a decrease in specific mRNA degradation rate.
[Ca2+]i regulates transcription rate of the Na+/K(+)-ATPase alpha 1 subunit
Department of Physiology, Cornell University Medical College, New York, New York 10021.
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