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ANG — MARCKS

Text-mined interactions from Literome

Rangel et al., Biochim Biophys Acta 2002 : Data in the present report suggest the participation of a protein kinase C ( PKC ) in the molecular mechanism of Ang II-mediated stimulation of the Na ( + ) -ATPase activity due to the following observations : ( i ) the stimulation of protein phosphorylation in BLM, induced by Ang II, is mimicked by the PKC activator TPA, and is completely reversed by the specific PKC inhibitor, calphostin C ; ( ii ) the Na ( + ) -ATPase activity is stimulated by Ang II and TPA in the same magnitude, being these effects abolished by the use of the PKC inhibitors, calphostin C and sphingosine ; ( iii ) the Na ( + ) -ATPase activity is activated by catalytic subunit of PKC ( PKC-M ), in a similar and nonadditive manner to Ang II ; and ( iv ) Ang II stimulates the phosphorylation of MARCKS , a specific substrate for PKC
Lu et al., J Cell Biol 1998 : Furthermore, depletion of MARCKS by MARCKS-AON treatment of neurons resulted in a significant decrease in Ang II-stimulated accumulation of TH and DbetaH immunoreactivities and [ 3H ] NE uptake activity in synaptosomes