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Incubation of human platelets with 12-0-tetradecanoylphorbol-13-acetate (TPA) caused a rapid decrease in soluble Ca2+, phospholipid-dependent protein kinase activity (protein kinase C) and an increase in protein kinase C associated with the particulate fraction. TPA also induced an increased activity of a Ca2+, phospholipid-independent protein kinase activity in both the soluble and the particulate fractions of platelets. This latter kinase eluted from DEAE cellulose columns at a higher salt concentration than protein kinase C, and was shown by Sephadex G-100 chromatography to have a MW of approx. 50,000 compared with an MW of 80,000 for protein kinase C. The data suggest that TPA treatment of platelets causes irreversible activation of protein kinase C by proteolysis of the enzyme to a form active in the absence of Ca2+ and phospholipid.
P M Tapley, and
A W Murray
May 1984,
Biochemical and biophysical research communications,
P M Tapley, and
A W Murray
July 1982,
The Journal of biological chemistry,
P M Tapley, and
A W Murray
April 1986,
Carcinogenesis,
P M Tapley, and
A W Murray
January 1986,
The Biochemical journal,
P M Tapley, and
A W Murray
December 1990,
Revista espanola de fisiologia,
P M Tapley, and
A W Murray
September 1985,
Biochimica et biophysica acta,
P M Tapley, and
A W Murray
November 1989,
Biochemical and biophysical research communications,
P M Tapley, and
A W Murray
January 2002,
Planta,
P M Tapley, and
A W Murray
June 1984,
FEBS letters,
P M Tapley, and
A W Murray
May 1984,
FEBS letters,
