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Inhibition of deoxygenation-induced membrane protein dephosphorylation and
cell dehydration by phorbol esters and okadaic acid in sickle cells
H Fathallah, E Coezy, RS de Neef, MD Hardy-Dessources and F Giraud
Laboratoire de Biomembranes et Messagers Cellulaires, Universite Paris XI,
Orsay, France.
Deoxygenation (DO) of sickle cell anemia red blood cells (SS cells) induces
membrane permeabilization to Ca2+, Na+, and K+ and cell dehydration mostly
through the activation of the Ca(2+)-dependent K+ channels. We show that DO
of both SS cells and normal red blood cells was accompanied by a
nonspecific dephosphorylation of membrane proteins. After treatment with a
protein kinase C activator (phorbol myristate acetate) or a phosphoprotein
phosphatase inhibitor (okadaic acid), the level of membrane protein
phosphorylation in deoxygenated cells was maintained higher or equal,
respectively, to that of the oxygenated controls. We found that these drugs
in SS cells (1) inhibited by 40% the DO-stimulated net Ca2+ uptake, without
affecting the DO-stimulated Ca2+ influx, suggesting that they activated the
Ca2+ efflux; (2) slightly increased the DO-induced Na+ uptake and decreased
the DO-induced K+ loss; and (3) prevented the DO-induced cell dehydration.
Both drugs are known to stimulate both phosphorylation and activity of the
Ca pump and of the Na/H antiport. Inhibition of SS cell dehydration might
be due to an activation of the Ca pump preventing [Ca2+]i elevation
responsible for the stimulation of the K+ channels and/or to an activation
of the Na/H exchange resulting in cell water gain.
Volume 86,
Issue 5,
pp. 1999-2007,
09/01/1995
Copyright © 1995 by The American Society of Hematology
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