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Protein kinase C (PKC) is an important enzyme in mediating cellular signal transduction and neuronal plasticity. Extremely low concentrations (picomolar range) of Pb++ have been reported to activate partially purified PKC from rat brain (Markovac and Goldstein, 1988). However, the lead activation of PKC at such low concentrations is still a matter of discussion (Simons, 1989). To clarify this point, we have examined the lead effect on highly purified PKC subtypes. Pb++ was found to be a potent inhibitor for all three PKC subtypes (types I, II and III) with IC50 of 2 to 10 microM. Characterization of this lead inhibition of PKC suggests that 1) the inhibition is not due to the competition with Ca++, 2) the site of action of lead is on the catalytic domain of PKC, 3) the inhibition is not dependent on the mode of activation (phosphatidylserine/diacylglycerol vs. cis-unsaturated fatty acid) and 4) the inhibition is totally reversible.
K Murakami, and
G Feng, and
S G Chen
June 1990,
Biochemical and biophysical research communications,
K Murakami, and
G Feng, and
S G Chen
July 1988,
Nature,
K Murakami, and
G Feng, and
S G Chen
January 1997,
Neurochemical research,
K Murakami, and
G Feng, and
S G Chen
March 1999,
Neurochemical research,
K Murakami, and
G Feng, and
S G Chen
July 1990,
FEBS letters,
K Murakami, and
G Feng, and
S G Chen
July 1986,
Brain research,
K Murakami, and
G Feng, and
S G Chen
October 1988,
Toxicology and applied pharmacology,
K Murakami, and
G Feng, and
S G Chen
June 1985,
Cancer research,
K Murakami, and
G Feng, and
S G Chen
January 2003,
Biochimica et biophysica acta,
K Murakami, and
G Feng, and
S G Chen
January 1994,
Yao xue xue bao = Acta pharmaceutica Sinica,
