Activation signals in human lymphocytes. Incorporation of polyunsaturated fatty acids into plasma membrane phospholipids regulates IL-2 synthesis via sustained activation of protein kinase C

Human PBL activated with anti-TCR/CD3 mAb express high affinity receptors for IL-2, synthesize IL-2, and subsequently proliferate. In contrast, lymphocytes activated by dioctanoylglycerol (DiC8) and ionomycin express high affinity receptors; however, no IL-2 synthesis is detectable. Anti-TCR/CD3 ant...

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Veröffentlicht in:The Journal of immunology (1950) 1989-11, Vol.143 (9), p.2806-2813
Hauptverfasser: Szamel, M, Rehermann, B, Krebs, B, Kurrle, R, Resch, K
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container_end_page 2813
container_issue 9
container_start_page 2806
container_title The Journal of immunology (1950)
container_volume 143
creator Szamel, M
Rehermann, B
Krebs, B
Kurrle, R
Resch, K
description Human PBL activated with anti-TCR/CD3 mAb express high affinity receptors for IL-2, synthesize IL-2, and subsequently proliferate. In contrast, lymphocytes activated by dioctanoylglycerol (DiC8) and ionomycin express high affinity receptors; however, no IL-2 synthesis is detectable. Anti-TCR/CD3 antibodies, as well as DiC8 cause translocation of protein kinase C (PKC) from the cytosol to the plasma membrane. In DiC8-stimulated cells translocation of PKC is detectable after 15 min, then it declines to control levels. In lymphocytes activated by antiTCR/CD3 mAb translocation of PKC is detectable after 15 min, then it declines to control levels, followed by a second, long lasting activation of the enzyme up to 4 h. Addition of polyunsaturated fatty acids to DiC8 + ionomycin-treated cells leads to IL-2 synthesis and proliferation. Incorporation of poly-unsaturated fatty acids into plasma membrane phospholipids results in long term activation of PKC. The results suggest that elevated incorporation of polyunsaturated fatty acids and thus continuous activation and translocation of PKC represents a necessary early signal for IL-2 synthesis and proliferation in human lymphocytes.
doi_str_mv 10.4049/jimmunol.143.9.2806
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Incorporation of polyunsaturated fatty acids into plasma membrane phospholipids regulates IL-2 synthesis via sustained activation of protein kinase C</title><title>The Journal of immunology (1950)</title><addtitle>J Immunol</addtitle><description>Human PBL activated with anti-TCR/CD3 mAb express high affinity receptors for IL-2, synthesize IL-2, and subsequently proliferate. In contrast, lymphocytes activated by dioctanoylglycerol (DiC8) and ionomycin express high affinity receptors; however, no IL-2 synthesis is detectable. Anti-TCR/CD3 antibodies, as well as DiC8 cause translocation of protein kinase C (PKC) from the cytosol to the plasma membrane. In DiC8-stimulated cells translocation of PKC is detectable after 15 min, then it declines to control levels. In lymphocytes activated by antiTCR/CD3 mAb translocation of PKC is detectable after 15 min, then it declines to control levels, followed by a second, long lasting activation of the enzyme up to 4 h. Addition of polyunsaturated fatty acids to DiC8 + ionomycin-treated cells leads to IL-2 synthesis and proliferation. Incorporation of poly-unsaturated fatty acids into plasma membrane phospholipids results in long term activation of PKC. 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subjects 1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine
Antigens, Differentiation, T-Lymphocyte - physiology
CD3 Complex
Cells, Cultured
Diglycerides - pharmacology
DNA - biosynthesis
fatty acids
Fatty Acids, Unsaturated - physiology
Humans
In Vitro Techniques
Indomethacin - pharmacology
Interleukin-2 - biosynthesis
Ionomycin - pharmacology
Isoquinolines - pharmacology
Linoleic Acid
Linoleic Acids - pharmacology
Lymphocyte Activation - drug effects
Lymphocytes - immunology
Masoprocol - pharmacology
Membrane Lipids - physiology
phospholipids
Phospholipids - physiology
Piperazines - pharmacology
plasma membranes
Protein Kinase C - physiology
Receptors, Antigen, T-Cell - physiology
Sphingosine - pharmacology
title Activation signals in human lymphocytes. Incorporation of polyunsaturated fatty acids into plasma membrane phospholipids regulates IL-2 synthesis via sustained activation of protein kinase C
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