Unsaturated fatty acids inhibit lymphocyte protein kinase C activity

1993 ◽  
Vol 21 (4) ◽  
pp. 377S-377S ◽  
Author(s):  
CHARLOTTE L. MAY ◽  
PHILIP C. CALDER
Keyword(s):  
Fatty Acids ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Unsaturated Fatty Acids ◽  
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+.

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 Cytoplasmic lipid bodies of neutrophils: formation induced by cis-unsaturated fatty acids and mediated by protein kinase C.

1991 ◽  
Vol 113 (1) ◽  
pp. 137-146 ◽  
Author(s):  
P F Weller ◽  
S W Ryeom ◽  
S T Picard ◽  
S J Ackerman ◽  
A M Dvorak
Keyword(s):  
Fatty Acids ◽  
Protein Kinase C ◽  
Fatty Acid ◽  
Protein Kinase ◽  
Unsaturated Fatty Acids ◽  
Lipid Body ◽  
Lipid Bodies ◽  
Myristate Acetate ◽  
Body Formation ◽  
Kinase C

Lipid bodies, nonmembrane-bound cytoplasmic inclusions, serve as repositories of esterified arachidonate and are increased in cells associated with inflammatory reactions. We have evaluated stimuli and mechanisms responsible for lipid body formation within human polymorphonuclear leukocytes (PMNs). Arachidonic acid and oleic acid stimulated dose-dependent formation of lipid bodies over 0.5-1 h. Other C20 and C18 fatty acids were less active and demonstrated rank orders as follows: cis-unsaturated fatty acids were much more active than trans-fatty acids, and activity diminished with decreasing numbers of double bonds. Lipid bodies elicited in vitro with cis-fatty acids were ultrastructurally identical to lipid bodies present in PMNs in vivo. Lipid body induction was not because of fatty acid-elicited oxidants or fatty acid-induced ATP depletion. Cis-fatty acid-induced activation of protein kinase C (PKC) was involved in lipid body formation as evidenced by the capacity of other PKC activators, 1-oleoyl-2-acetyl-glycerol and two active phorbol esters, phorbol myristate acetate, and phorbol 12,13 dibutyrate, but not an inactive phorbol, to induce lipid body formation. The PKC inhibitor, 1-O-hexadecyl-2-O-methyl-glycerol, inhibited PMN lipid body formation induced by oleic and arachidonic acids and by 1-oleoyl-2-acetyl-glycerol and phorbol myristate acetate. Other PKC inhibitors (staurosporine, H-7) also inhibited lipid body formation. Formation of lipid bodies in PMNs is a specific cellular response, stimulated by cis-fatty acids and diglycerides and apparently mediated by PKC, which results in the mobilization and deposition of lipids within discrete, ultrastructurally defined cytoplasmic domains.

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