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and inhibits
Na+-K+-ATPase
in opossum kidney cells
Departments of Medicine and Physiology and Biophysics, Mayo Clinic and Foundation, Rochester, Minnesota 55905
Nitric oxide (NO)
reduces the molecular activity of
Na+-K+-ATPase
in opossum kidney (OK) cells, a proximal tubule cell line. In the
present study, we investigated the cellular mechanisms for the
inhibitory effect of NO on
Na+-K+-ATPase.
Sodium nitroprusside (SNP), a NO donor, inhibited
Na+-K+-ATPase
in OK cells, but not in LLC-PK1
cells, another proximal tubule cell line. Similarly, phorbol
12-myristate 13-acetate, a protein kinase C (PKC) activator, inhibited
Na+-K+-ATPase
in OK, but not in LLC-PK1, cells.
PKC inhibitors staurosporine or calphostin C, but not the protein
kinase G inhibitor KT-5823, abolished the inhibitory effect of NO on
Na+-K+-ATPase
in OK cells. Immunoblotting demonstrated that treatment with NO donors
caused significant translocation of PKC
from cytosolic to
particulate fractions in OK, but not in
LLC-PK1, cells. Furthermore, the
translocation of PKC in OK cells was attenuated by either the
phospholipase C inhibitor U-73122 or the soluble guanylate cyclase
inhibitor
1H-[1,2,4]oxadiazolo-[4,3-a]quinoxalin-1-one. U-73122 also blunted the inhibitory effect of SNP on
Na+-K+-ATPase
in OK cells. The phospholipase A2
inhibitor AACOCF3 did not blunt the inhibitory effect of SNP on
Na+-K+-ATPase
in OK cells. AACOCF3 alone, however, also decreased
Na+-K+-ATPase
activity in OK cells. In conclusion, our results demonstrate that NO
activates PKC in OK, but not in
LLC-PK1, cells. The activation of
PKC in OK cells by NO is associated with inhibition of
Na+-K+-ATPase.
proximal tubule; LLC-PK1 cells; phospholipase C; guanosine 3',5'-cyclic monophosphate; phospholipase A2; protein kinase C
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