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J. Biol. Chem., Vol. 265, Issue 1, 70-75, Jan, 1990
K Oishi, B Zheng and JF Kuo
The effects and modes of action of certain lipid second messengers and
protein kinase C regulators, such as sphingosine, lysophosphatidylcholine
(lyso-PC), and oleic acid, on Na,K-ATPase and sodium pump were examined.
Inhibition of purified rat brain synaptosome Na,K-ATPase by these lipid
metabolites, unlike that by ouabain, was subject to membrane dilution (i.e.
inhibition being counteracted by increasing amounts of membrane lipids).
Kinetic analysis, using the purified enzyme, indicated that sphingosine and
lyso-PC were likely to interact, directly or indirectly, with Na+-binding
sites of Na,K-ATPase located at the intracellular face of plasma membranes,
a conclusion also supported by studies on Na,K-ATPase and 22Na uptake using
the inside-out vesicles of human erythrocyte membranes. The studies also
showed that ouabain (but not sphingosine and lyso-PC) increased the
affinity constant (K0.5) for K+, whereas sphingosine and lyso-PC (but not
ouabain) increased K0.5 for Na+. Sphingosine and lyso-PC inhibited 86Rb
uptake by intact human leukemia HL-60 cells at potencies comparable to
those for inhibitions of purified Na,K-ATPase and protein kinase C. It is
suggested that Na,K-ATPase (sodium pump) might represent an additional
target system, besides protein kinase C, for sphingosine and possibly other
lipid second messengers.
Inhibition of Na,K-ATPase and sodium pump by protein kinase C regulators sphingosine, lysophosphatidylcholine, and oleic acid
Department of Pharmacology, Emory University School of Medicine, Atlanta, Georgia 30322.
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