Protein kinase C is crucial in signal transduction during IFN‐γ induction in endothelial cells

Mattila, Pirkko; Häyry, P; Renkonen, Risto

doi:10.1016/0014-5793(89)80756-2

Cited by 31 publications

(16 citation statements)

References 16 publications

(17 reference statements)

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“…Several lines of evidence in our study support the direct role of cAMP as a second messenger in [28, 291, H7 has been reported to be able to totally block the IFN-y induced PKC activation in endothelial cells [27].…”

Section: Discussionsupporting

confidence: 86%

Interleukin 1‐induced lymphocyte binding to endothelial cells. Role of cAMP as a second messenger

et al. 1990

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Interleukin 1 (IL 1) is a potent protein mediator of inflammation. Among other things it increases the number of lymphocytes adhering to endothelial cell monolayers. We analyzed the signal transduction during IL 1-induced lymphocyte binding. Dibutyryl cyclic AMP, which is a cAMP analog able to penetrate into the cytosol, increased lymphocyte binding to the same extent as IL 1. Direct activation of adenylate cyclase by forskolin enhanced also lymphocyte binding. IL 1 increased the level of cytosolic cAMP in a time- and dose-dependent manner measured with radioimmunoassay. 2',5'-Dideoxyadenosine, which is an inhibitor of adenylate cyclase, decreased both the IL 1-induced lymphocyte binding to endothelial cells and elevation in cytosolic cAMP levels. Lymphocyte binding increased with cytosolic cAMP levels in accordance with elevation of IL 1 concentration. These results suggest that cAMP is essential in signal transduction during IL 1-induced lymphocyte binding to cultured endothelial cell monolayers.

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Section: Discussionsupporting

confidence: 86%

Interleukin 1‐induced lymphocyte binding to endothelial cells. Role of cAMP as a second messenger

et al. 1990

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“…Relatively little is known about the molecular mechanisms of IFN^y induction of class II genes. Studies on second messenger systems have implicated protein kinase C (PKC) (Fan et al, 1988;Mattila et al, 1989;Nezu et al, 1990), Ca2+-dependent processes (Koide et al, 1988; Celada and Maki,1991), cAMP (Frohman et al, 1988;Basta et al, 1989) and changes in intracellular pH as important second messengers in the IFN-y regulation of class II genes (Prpic et al, 1989). However, these observations vary between different cell lines.…”

Section: Introductionmentioning

confidence: 99%

Dissection of the interferon gamma-MHC class II signal transduction pathway reveals that type I and type II interferon systems share common signalling component(s).

et al. 1992

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We have used a herpes virus thymidine kinase (HSV‐TK) based metabolic selection system to isolate mutants defective in the interferon gamma mediated induction of the MHC class II promoter. All the mutations act in trans and result in no detectable induction of MHC and invariant chain (Ii) gene expression. Scatchard analysis indicates that the mutants have a normal number of surface IFN gamma receptors with the same affinity constant. The mutants fall into two broad categories. One class of mutants is still able to induce MHC class I, IRF‐1, 9–27, 1–8 and GBP genes by IFN gamma. A second class of mutants is defective for the IFN gamma induction of all the genes tested; surprisingly, the IFN alpha/beta induction of MHC class I, 9–27, ISG54 and ISG15 genes is also defective in these mutants, although different members of this class can be discriminated by the response of the GBP and IRF‐1 genes to type I interferons. These data demonstrate that the signalling pathways of both type I and type II interferon systems share common signal transduction component(s). These mutants will be useful for the study of IFN gamma regulation of class II genes and Ii chain, and to elucidate molecular components of type I and type II interferon signal transduction.

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“…Previous work with PMA had shown that it stimulates protein kinase C in many cell types, like in normal white cells, hematopoietic tumor cells and in endothelial cells [20,21]. Concomitantly PMA induces many cell types to adhere onto plastic surfaces, to each other and to endothelial monolayers [18].…”

Section: Discussionmentioning

confidence: 99%

Activation of protein kinases A and C increase lymphocyte penetration through endothelial monolayers

Renkonen

1990

FEBS Letters

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A brief incubation of lymphocytes with either PMA, stimulating protein kinase C, or with dibutyryl‐cAMP, leading to protein kinase A activation, led to increased lymphocyte penetration through intact endothelial monolayers in vitro. The PMA‐induced penetration could be dose‐dependently down‐regulated with a protein kinase C inhibitor, H7. Similarly HA 1004, being mainly a protein kinase A inhibitor, decreased the dibutyryl‐cAMP induced penetration. Treatment of lymphocytes with PMA and cAMP did not alter the expression of CD44 homing receptors on lymphocytes. Stimulation of lymphocytes with dibutyryl‐cGMP or calcium ionophore had no effect on lymphocyte penetration. These results suggest that activation of both protein kinases A and C is important in the lymphocyte binding to endothelium.

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Protein kinase C is crucial in signal transduction during IFN‐γ induction in endothelial cells

Cited by 31 publications

References 16 publications

Interleukin 1‐induced lymphocyte binding to endothelial cells. Role of cAMP as a second messenger

Interleukin 1‐induced lymphocyte binding to endothelial cells. Role of cAMP as a second messenger

Dissection of the interferon gamma-MHC class II signal transduction pathway reveals that type I and type II interferon systems share common signalling component(s).

Activation of protein kinases A and C increase lymphocyte penetration through endothelial monolayers

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