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Inhibition of Na,K‐ATPase activity by cGMP is isoform‐specific in brain endothelial cells
Author(s) -
Pontiggia Luca,
Winterhalter Kaspar,
Gloor Sergio M
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)01183-1
Subject(s) - gene isoform , chemistry , microbiology and biotechnology , atpase , biochemistry , biophysics , biology , enzyme , gene
cGMP has been shown to either activate or inhibit Na,K‐ATPase activity. Using mouse brain endothelial cells which express both ouabain‐resistant α1 and ouabain‐sensitive α2 and α3 isoforms, we show that cGMP reduces total Na,K‐ATPase activity to about 58%. The inhibition is prevented by the protein kinase G (PKG)‐specific inhibitor KT5823, indicating that cGMP‐mediated activation of PKG leads to inhibition of the pump. A similar extent of inhibition is obtained with nitric oxide. cGMP‐induced inhibition acts mainly on α1 isoforms but hardly affects α2/α3 isoforms. These data suggest that inhibition of Na,K‐ATPase activity by cGMP occurs in an isoform‐selective manner in brain endothelial cells.