Oleate-induced translocation of protein kinase C to hepatic microsomal membranes
- 1 May 1989
- journal article
- research article
- Published by Elsevier BV in Biochemical and Biophysical Research Communications
- Vol. 160 (3), 1243-1249
- https://doi.org/10.1016/s0006-291x(89)80137-8
Abstract
No abstract availableThis publication has 14 references indexed in Scilit:
- The protein kinase inhibitor staurosporine, like phorbol esters, induces the association of protein kinase C with membranesBiochemical and Biophysical Research Communications, 1988
- The molecular heterogeneity of protein kinase C and its implications for cellular regulationNature, 1988
- Activation of protein kinase C from B lymphocytes by lipid ABiochemical and Biophysical Research Communications, 1988
- Proteolytic activation of protein kinase C: a physiological reaction?Trends in Biochemical Sciences, 1987
- Identification of the structures of multiple subspecies of protein kinase C expressed in rat brainFEBS Letters, 1987
- Three distinct forms of rat brain protein kinase C: Differential response to unsaturated fatty acidsBiochemical and Biophysical Research Communications, 1987
- The Metabolism of Phosphoinositide-Derived Messenger MoleculesScience, 1986
- Direct activation of purified protein kinase C by unsaturated fatty acids (oleate and arachidonate) in the absence of phospholipids and Ca2+FEBS Letters, 1985
- Spermine promotes the translocation of phosphatidate phosphohydrolase from the cytosol to the microsomal fraction of rat liver and it enhances the effects of oleate in this respectFEBS Letters, 1985
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976