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J. Biol. Chem., Vol. 269, Issue 39, 23944-23948, 09, 1994
SE Daly, LK Lane and R Blostein
One region of marked sequence diversity among the highly homologous alpha
isoforms of the Na,K-ATPase is the lysine-rich NH2 terminus. Expression of
a mutant cDNA encoding an alpha 1 protein, minus the 32 NH2-terminal
residues, results in a modified enzyme (alpha 1M32), which behaves
similarly to alpha 1 in overall Na/K exchange activity (Vmax) and apparent
affinities for intracellular Na+ and extracellular K+. However, with
membranes isolated from HeLa cells expressing the rat alpha 1M32 mutant, as
well as membranes from cells expressing the rat alpha 1 and the
ouabain-resistant mutated forms of rat alpha 2 (alpha 2*) and alpha 3
(alpha 3*) developed by Jewell and Lingrel (Jewell, E. A., and Lingrel, J.
B. (1991) J. Biol. Chem. 266, 16925-16930), distinct Na,K-ATPase kinetics
are observed. Thus, at 1 microM ATP, the effects of K+ on the Na-ATPase
activity of alpha 2* and alpha 1M32 are similar; both are activated,
whereas alpha 1 and alpha 3 are inhibited by the addition of K+ at low (0.1
mM) concentration. These effects are attributed to different rates of a
step involved in K+ deocclusion (E2(K)<-->E1K<-->E1 + K+) and
are consistent with our earlier evidence (Wierzbicki, W., and Blostein, R.
(1993) Proc. Natl. Acad. Sci. U. S. A. 90, 70-74) for a role of the NH2
terminus in the K+ deocclusion pathway of the Na,K-ATPase reaction. These
differences are not directly related to differences in apparent affinities
for ATP, since alpha 3* has alpha 1-like high affinity K+ inhibition but
resembles alpha 2* and alpha 1M32 with respect to a lower K'ATP. Na-ATPase
activities of alpha 2*, alpha 3*, and alpha 1M32, but not alpha 1, are
activated by Li+ but not Rb+, consistent with a relatively faster rate of
Li+ deocclusion (Post, R. L., Hegyvary, C., and Kume, S. (1972) J. Biol.
Chem. 247, 6530-6540), as well as higher affinity of alpha 3 for
extracellular K+ (Li+) activation of dephosphorylation (E2P +
K+<-->E2(K) + Pi). Inhibition of Na-ATPase by higher concentrations
(> or = 1 mM) K+ is observed with all isoforms and is attributed to K+
acting at inhibitory cytoplasmic sites.(ABSTRACT TRUNCATED AT 400 WORDS)
Functional consequences of amino-terminal diversity of the catalytic subunit of the Na,K-ATPase
Department of Medicine, McGill University, Montreal, Quebec, Canada.
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