Synergistic Effects of Diacylglycerols and Fatty Acids on Membrane Structure and Protein Kinase C Activity

Biochemistry ◽  
1998 ◽  
Vol 37 (16) ◽  
pp. 5623-5632 ◽  
Author(s):  
Edward M. Goldberg ◽  
Raphael Zidovetzki
Keyword(s):  
Fatty Acids ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Membrane Structure ◽  
Synergistic Effects ◽  
Kinase C ◽  
Protein Kinase C Activity

scholarly journals Inhibitory effects of omega-3 fatty acids on protein kinase C activity in vitro

2001 ◽  
Vol 6 (2) ◽  
pp. 246-248 ◽  
Author(s):  
H F Seung Kim ◽  
E J Weeber ◽  
J D Sweatt ◽  
A L Stoll ◽  
L B Marangell
Keyword(s):  
Fatty Acids ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Omega 3 Fatty Acids ◽  
Omega 3 ◽  
Inhibitory Effects ◽  
Kinase C ◽  
Protein Kinase C Activity

39. Inhibitory effects of omega-3 fatty acids on protein kinase C activity in vitro

2000 ◽  
Vol 47 (8) ◽  
pp. S12
Author(s):  
H.F. Kim ◽  
E.J. Weeber ◽  
J.D. Sweatt ◽  
A.L. Stoll ◽  
L.B. Marangell
Keyword(s):  
Fatty Acids ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Omega 3 Fatty Acids ◽  
Omega 3 ◽  
Inhibitory Effects ◽  
Kinase C ◽  
Protein Kinase C Activity

scholarly journals Effect of cis-unsaturated fatty acids on aortic protein kinase C activity

1989 ◽  
Vol 258 (1) ◽  
pp. 171-175 ◽  
Author(s):  
K R Dell ◽  
D L Severson
Keyword(s):  
Fatty Acids ◽  
Protein Kinase C ◽  
Oleic Acid ◽  
Fatty Acid ◽  
Protein Kinase ◽  
Unsaturated Fatty Acids ◽  
Acid Activation ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Fatty Acid Activation

Long-chain cis-unsaturated fatty acids could substitute for phosphatidylserine and activate bovine aortic protein kinase C in assays with histone as substrate. The optimal concentration was 24-40 microM for oleic, linoleic and arachidonic acids. With arachidonic acid, the Ka for Ca2+ was 130 microM and kinase activity was maximal at 0.5 mM-Ca2+. Diolein only slightly activated the oleic acid-stimulated enzyme at low physiological Ca2+ concentrations (0.1 and 10 microM). Oleic acid also stimulated kinase C activity, determined with a Triton X-100 mixed-micellar assay. Under these conditions, the fatty acid activation was absolutely dependent on the presence of diolein, but a Ca2+ concentration of 0.5 mM was still required for maximum kinase C activity. The effect of fatty acids on protein kinase C activity was also investigated with the platelet protein P47 as a substrate, since the properties of kinase C can be influenced by the choice of substrate. In contrast with the results with histone, fatty acids did not stimulate the phosphorylation of P47 by the aortic protein kinase C. Activation of protein kinase C by fatty acids may allow the selective phosphorylation of substrates, but the physiological significance of fatty acid activation is questionable because of the requirement for high concentrations of Ca2+.

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