[HTML][HTML] Phosphorylation of Na, K-ATPase by protein kinase C at Ser18 occurs in intact cells but does not result in direct inhibition of ATP hydrolysis
MS Feschenko, KJ Sweadner - Journal of Biological Chemistry, 1997 - ASBMB
Na, K-ATPase activity has been demonstrated to be regulated by a variety of hormones in
different tissues. It is known to be directly phosphorylated on its α-subunit, but the functional
effects of protein kinases remain controversial. We have developed a sensitive, antibody-
based assay for detection of the level of phosphorylation of the α1-isoform of rat Na, K-
ATPase at the serine residue that is most readily phosphorylated by protein kinase C (PKC)
in vitro, Ser 18. By stimulation of endogenous PKC and inhibition of phosphatase activity, it …
different tissues. It is known to be directly phosphorylated on its α-subunit, but the functional
effects of protein kinases remain controversial. We have developed a sensitive, antibody-
based assay for detection of the level of phosphorylation of the α1-isoform of rat Na, K-
ATPase at the serine residue that is most readily phosphorylated by protein kinase C (PKC)
in vitro, Ser 18. By stimulation of endogenous PKC and inhibition of phosphatase activity, it …