Effect of N-3, N-6 Fatty Acid and d-Limonene Treatment on Membrane Lipid Composition and Protein Kinase C Activity in Experimental Rat Hepatocarcinogenesis

A long-chain neutral phospholipid, dioleoylphosphatidylcholine, was found to support protein kinase C activation by cis-fatty acid and diacylglycerol (DAG). This effect of phosphatidylcholine (PC) is totally dependent on the presence of cis-fatty acid; PC greatly stimulates the cis-fatty acid-induced protein kinase C activity, but it does not activate protein kinase C at all, even in the presence of DAG, if cis-fatty acid is absent. DAG, however, plays a modulatory role in the presence of Ca2+; it further enhances the PC-potentiated cis-fatty acid activation of protein kinase C. Although the activities of all three protein kinase C subtypes tested (types I, II and III) are supported by this PC mechanism, type III is most sensitive to the DAG effect, and it is activated synergistically by cis-fatty acid and DAG. The potency of PC to support the synergistic activation of this subtype is equivalent to that of phosphatidylserine (PS). There are several differences, however, between PC- and PS-supported synergism observed in type III protein kinase C: (1) Ca(2+)-sensitivity is different; PC requires higher concentrations of Ca2+ (10-20 microM-Ca2+) than those required for PS (micromolar Ca2+); (2) PC/cis-fatty acid/DAG-induced autophosphorylation of protein kinase C subtypes (types I, II and III) is very weak, whereas PS/cis-fatty acid/DAG strongly stimulate autophosphorylation of these subtypes under the conditions at which both PC and PS systems fully activate the protein kinase C in terms of histone phosphorylation. These observations suggest that a neutral phospholipid such as PC may also participate in the activation and differential regulation of protein kinase C.

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N-3 polyunsaturated fatty acid supplementation alters inositol phosphate metabolism and protein kinase C activity in adult porcine cardiac myocytes

The Journal of Nutritional Biochemistry ◽

10.1016/s0955-2863(00)00139-x ◽

2001 ◽

Vol 12 (1) ◽

pp. 7-13 ◽

Cited By ~ 12

Author(s):

Sudheera S.D. Nair ◽

James Leitch ◽

Manohar L. Garg

Keyword(s):

Protein Kinase C ◽

Fatty Acid ◽

Protein Kinase ◽

Cardiac Myocytes ◽

Inositol Phosphate ◽

Phosphate Metabolism ◽

Fatty Acid Supplementation ◽

Inositol Phosphate Metabolism ◽

Kinase C ◽

Protein Kinase C Activity

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The modulation of protein kinase C activity by membrane lipid bilayer structure.

Journal of Biological Chemistry ◽

10.1016/s0021-9258(17)37624-x ◽

1994 ◽

Vol 269 (7) ◽

pp. 4866-4871 ◽

Cited By ~ 5

Author(s):

S.J. Slater ◽

M.B. Kelly ◽

F.J. Taddeo ◽

C. Ho ◽

E. Rubin ◽

...

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Lipid Bilayer ◽

Membrane Lipid ◽

Bilayer Structure ◽

Kinase C ◽

Protein Kinase C Activity ◽

Membrane Lipid Bilayer

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Alterations in Protein Kinase C Activity and Membrane Lipid Metabolism in Cerebral Vasospasm after Subarachnoid Hemorrhage

Journal of Cerebral Blood Flow & Metabolism ◽

10.1038/jcbfm.1993.55 ◽

1993 ◽

Vol 13 (3) ◽

pp. 409-415 ◽

Cited By ~ 45

Author(s):

Yoh Takuwa ◽

Toru Matsui ◽

Yoichiro Abe ◽

Toshiaki Nagafuji ◽

Kamejiro Yamashita ◽

...

Keyword(s):

Protein Kinase C ◽

Lipid Metabolism ◽

Subarachnoid Hemorrhage ◽

Protein Kinase ◽

Control Level ◽

Membrane Lipid ◽

Kinase C ◽

Protein Kinase C Activity ◽

Basilar Arteries ◽

Mlc Phosphorylation

Changes in protein kinase C (PKC) activity, membrane lipid metabolism, and the extent of 20-kDa myosin light chain (MLC) phosphorylation in spastic cerebral basilar arteries were examined by using the beagle “two-hemorrhage” model of subarachnoid hemorrhage. In spastic arteries at days 4 and 7, cytosolic PKC activity showed a decrease of 40–45% with no significant changes in membrane PKC activity as compared with nonspastic control arteries. Cytosolic PKC activity of the day 14 arteries returned toward the normal control level with the remission of vasospasm. Western blot analysis of the PKC isoforms revealed that the amounts of PKCα and PKCε but not PKCζ were decreased in spastic arteries. As compared with nonspastic arteries, spastic arteries showed higher rates of incorporation of [3H]choline into phosphatidylcholine (PC) and [14C]ethanolamine into phosphatidylethanolamine (PE), but not of [3H]myoinositol into phosphoinositides, suggesting the stimulated turnover of PC and PE. The extent of 20-kDa MLC phosphorylation was not increased in the spastic arteries at days 4 or 7 as compared with that in the nonspastic control arteries. These results demonstrate that PKC activity and related membrane lipid metabolism are altered in spastic basilar arteries after subarachnoid hemorrhage.

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

Biochemical Journal ◽

10.1042/bj2580171 ◽

1989 ◽

Vol 258 (1) ◽

pp. 171-175 ◽

Cited By ~ 19

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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Chronic treatment by the calcium channel blocker ± PN 200-110 in the rat counteracts the stimulations of pituitary weight, prolactin release and pituitary C-kinase activity induced by a chronic estradiol treatment, in vivo

Acta Endocrinologica ◽

10.1530/acta.0.1220403 ◽

1990 ◽

Vol 122 (3) ◽

pp. 403-408

Author(s):

Ph. Touraine ◽

P. Birman ◽

F. Bai-Grenier ◽

C. Dubray ◽

F. Peillon ◽

...

Keyword(s):

Protein Kinase C ◽

Protein Kinase ◽

Calcium Channel ◽

Calcium Channel Blocker ◽

Channel Blocker ◽

Plasma Prolactin ◽

Estradiol Treatment ◽

Kinase C ◽

Protein Kinase C Activity

Abstract In order to investigate whether a calcium channel blocker could modulate the protein kinase C activity in normal and estradiol pretreated rat pituitary, female Wistar rats were treated or not (controls) with ± PN 200-110 (3 mg · kg−1 · day−1, sc) for 8 days or with estradiol cervical implants for 8 or 15 days, alone or in combination with PN 200-110 the last 8 days. Estradiol treatment induced a significant increase in plasma prolactin levels and pituitary weight. PN 200-110 administered to normal rats did not modify these parameters, whereas it reduced the effects of the 15 days estradiol treatment on prolactin levels (53.1 ± 4.9 vs 95.0 ±9.1 μg/l, p<0.0001) and pituitary weight (19.9 ± 0.4 vs 23.0 ± 0.6 mg, p <0.001), to values statistically comparable to those measured after 8 days of estradiol treatment. PN 200-110 alone did not induce any change in protein kinase C activity as compared with controls. In contrast, PN 200-110 treatment significantly counteracted the large increase in soluble activity and the decrease in the particulate one induced by estradiol between day 8 and day 15. We conclude that PN 200-110 opposed the stimulatory effects of chronic in vivo estradiol treatment on plasma prolactin levels and pituitary weight and that this regulation was related to a concomitant modulation of the protein kinase C activity.

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