Lateral mobility of FcγRIIa is reduced by protein kinase C activation

Activation of Protein Kinase C

Activation of protein kinase C by short chain phosphatidylcholines.

The acidic phospholipid requirement for protein kinase C (Ca2+/phospholipid-dependent enzyme) activation has been well established, although the molecular nature of this lipid-protein interaction is unclear. The additional requirement for Ca2+ has provided the basis for several models involving charge interactions. We now report that short chain neutral phosphatidylcholines also activate the ki...

Activation of hepatocyte protein kinase C by redox-cycling quinones.

The effects of quinone-generated active oxygen species on rat hepatocyte protein kinase C were investigated. The specific activity of cytosolic protein kinase C was increased 2-3-fold in hepatocytes incubated with the redox-cycling quinones, menadione, duroquinone or 2,3-dimethoxy-1,4-naphthoquinone, without alterations in particulate protein kinase C specific activity or Ca2+- and lipid-indepe...

Activation of transfer RNA-guanine ribosyltransferase by protein kinase C

Transfer RNA-guanine ribosyltransferase (TGRase) irreversibly incorporates queuine into the first position in the anticodon of four tRNA isoacceptors. Rat brain protein kinase C (PKC) was shown to stimulate rat liver TGRase activity. TGRase preparations derived from rat liver have been observed to decrease in activity over time in storage at -20 or -70 degrees C. Contamination of the samples by...

Differential activation of adenylyl cyclase by protein kinase C isoenzymes.

Cyclic AMP production within cells is altered upon protein kinase C (PKC) activation; however, whether PKC directly modulates adenylyl cyclase (AC) catalytic activity has been controversial. Molecular studies have elucidated the existence of multiple PKC isoenzymes although the functional role of this diversity is not clear. Using purified PKC and AC isoenzymes, we demonstrate that PKC zeta dir...