Ethoxylated alcohol (Neodol-12) and other surfactants in the assay of protein kinase C.

  title={Ethoxylated alcohol (Neodol-12) and other surfactants in the assay of protein kinase C.},
  author={T F Abidi and Carol A. Faaland and Diana Scala and Linda D. Rhein and Jeffrey D Laskin},
  journal={Biochimica et biophysica acta},
  volume={992 3},
Inhibitory effects of curcumin on in vitro lipoxygenase and cyclooxygenase activities in mouse epidermis.
The inhibitory effects of curcumin, chlorogenic acid, caffeic acid, and ferulic acid on TPA-induced tumor promotion in mouse epidermis parallel their inhibitory effect on T PA-induced epidermal inflammation and epider mal lipoxygenase and cyclo oxygengenase activities.
Cellular and molecular mechanisms in photochemical sensitization: studies on the mechanism of action of psoralens.
  • J. Laskin
  • Chemistry, Medicine
    Food and chemical toxicology : an international journal published for the British Industrial Biological Research Association
  • 1994
Annual Review of Cosmetic Ingredient Safety Assessments—2002/20031
This annual review covers all ingredients re-reviewed from February, 2002, to June, 2003, and covers the industry’s current practices of ingredient use, updating the data available in the earlier report.


Calcium-activated, phospholipid-dependent protein kinases from rat liver: subcellular distribution, purification, and characterization of multiple forms.
Three forms of Ca2+- and phospholipid-dependent protein kinase (protein kinase C) were extensively purified from rat liver homogenate and exhibited nearly identical enzymatic properties.
Phorbol esters increase the amount of Ca2+, phospholipid-dependent protein kinase associated with plasma membrane
Treatment of parietal yolk sacs cells with biologically active 12-O-tetradecanoyl phorbol-13-acetate (TPA) provokes a rapid decrease in cytosolic Ca,PL-PK activity that is accompanied by a significant increase in the amount of Ca, PL- PK activity associated with the plasma membrane fraction.
Role of substrate in imparting calcium and phospholipid requirements to protein kinase C activation.
Substrate-phospholipid interaction and substrate phosphorylation were inhibited by increasing salt concentrations, but the amount needed depended upon the substrate.
Purification of stable protein kinase C from mouse brain cytosol by specific ligand elution using fast protein liquid chromatography.
The Ca2+- and phospholipid-dependent protein kinase (protein kinase C) has been purified to electrophoretic homogeneity from mouse brain cytosol and phorbol ester binding activities were stable for 2 mo when stored in the presence of 0.01% Triton X-100 at -70 degrees C.