Acyl chain dependence of diacylglycerol activation of protein kinase C activity in vitro

Paola A. Marignani; Richard M. Epand; Rolf J. Sebaldt

doi:10.1006/bbrc.1996.1196

Acyl chain dependence of diacylglycerol activation of protein kinase C activity in vitro

Paola A. Marignani, Richard M. Epand, Rolf J. Sebaldt

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65 Citations (Scopus)

Résumé

Stimulation of protein kinase C (PKC) activity in lipid vesicles in vitro was achieved by pure molecular species of diacylglycerol (DAG), specifically 1-stearoyl-2-acyl-sn-glycerol substituted with 2-arachidonoyl,2-eicosapentaenoyl or 2-docosahexaenoyl (SAG, SEG, and SDG, respectively). PKC activity was measured in lipid vesicles containing 30 mol% 1-palmitoyl-2-oleoyl-sn-glycerol-3-phospho-L-serine (POPS), 68-70 mol% 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (POPC), and 0-2 mol% DAG in the presence of 20 μM calcium. Our results demonstrate that amplification of PKC activity differs significantly among these molecular species of DAG. In particular, SDG at 0.5 mol% is more potent in increasing PKC activity than is dioleoylglycerol (DOG), SEG, or SAG, and SAG and SDG at 1.0 and 2.0 mol% have similar potencies which are greater than those of DOG or SEG. These findings demonstrate that sn-2 substitutions in DAG by specific n-3 and n-6 polyunsaturated fatty acids increase the potency of DAG to stimulate PKC activity in vitro.

Langue d'origine	English
Pages (de-à)	469-473
Nombre de pages	5
Journal	Biochemical and Biophysical Research Communications
Volume	225
Numéro de publication	2
DOI	https://doi.org/10.1006/bbrc.1996.1196
Statut de publication	Published - août 14 1996
Publié à l'externe	Oui

Note bibliographique

Funding Information:
This work was supported by grants from the Arthritis Society of Canada. R.J.S. is the recipient of a Career Award from the Pharmaceutical Manufacturers’ Association of Canada-Health Research Foundation and the Medical Research Council of Canada. P.A.M. is the recipient of a Graduate Research Studentship from the Pharmaceutical Manufacturers’ Association of Canada-Health Research Foundation and the Medical Research Council of Canada. We are greatful to Dr. Klaus Gawrisch for providing us with his NMR results (25) prior to publication.

ASJC Scopus Subject Areas

Biophysics
Biochemistry
Molecular Biology
Cell Biology

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10.1006/bbrc.1996.1196

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title = "Acyl chain dependence of diacylglycerol activation of protein kinase C activity in vitro",

abstract = "Stimulation of protein kinase C (PKC) activity in lipid vesicles in vitro was achieved by pure molecular species of diacylglycerol (DAG), specifically 1-stearoyl-2-acyl-sn-glycerol substituted with 2-arachidonoyl,2-eicosapentaenoyl or 2-docosahexaenoyl (SAG, SEG, and SDG, respectively). PKC activity was measured in lipid vesicles containing 30 mol% 1-palmitoyl-2-oleoyl-sn-glycerol-3-phospho-L-serine (POPS), 68-70 mol% 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (POPC), and 0-2 mol% DAG in the presence of 20 μM calcium. Our results demonstrate that amplification of PKC activity differs significantly among these molecular species of DAG. In particular, SDG at 0.5 mol% is more potent in increasing PKC activity than is dioleoylglycerol (DOG), SEG, or SAG, and SAG and SDG at 1.0 and 2.0 mol% have similar potencies which are greater than those of DOG or SEG. These findings demonstrate that sn-2 substitutions in DAG by specific n-3 and n-6 polyunsaturated fatty acids increase the potency of DAG to stimulate PKC activity in vitro.",

author = "Marignani, {Paola A.} and Epand, {Richard M.} and Sebaldt, {Rolf J.}",

note = "Funding Information: This work was supported by grants from the Arthritis Society of Canada. R.J.S. is the recipient of a Career Award from the Pharmaceutical Manufacturers{\textquoteright} Association of Canada-Health Research Foundation and the Medical Research Council of Canada. P.A.M. is the recipient of a Graduate Research Studentship from the Pharmaceutical Manufacturers{\textquoteright} Association of Canada-Health Research Foundation and the Medical Research Council of Canada. We are greatful to Dr. Klaus Gawrisch for providing us with his NMR results (25) prior to publication.",

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AU - Sebaldt, Rolf J.

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AB - Stimulation of protein kinase C (PKC) activity in lipid vesicles in vitro was achieved by pure molecular species of diacylglycerol (DAG), specifically 1-stearoyl-2-acyl-sn-glycerol substituted with 2-arachidonoyl,2-eicosapentaenoyl or 2-docosahexaenoyl (SAG, SEG, and SDG, respectively). PKC activity was measured in lipid vesicles containing 30 mol% 1-palmitoyl-2-oleoyl-sn-glycerol-3-phospho-L-serine (POPS), 68-70 mol% 1-palmitoyl-2-oleoyl-sn-glycerol-3-phosphocholine (POPC), and 0-2 mol% DAG in the presence of 20 μM calcium. Our results demonstrate that amplification of PKC activity differs significantly among these molecular species of DAG. In particular, SDG at 0.5 mol% is more potent in increasing PKC activity than is dioleoylglycerol (DOG), SEG, or SAG, and SAG and SDG at 1.0 and 2.0 mol% have similar potencies which are greater than those of DOG or SEG. These findings demonstrate that sn-2 substitutions in DAG by specific n-3 and n-6 polyunsaturated fatty acids increase the potency of DAG to stimulate PKC activity in vitro.

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Acyl chain dependence of diacylglycerol activation of protein kinase C activity in vitro

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