Lysophosphatidylcholine stimulation of CGMP production in human endothelial cells involves tyrosine kinases, heterotrimeric GTP binding proteins, phosphatidylinositol 3-kinase and protein kinase C

2006 ◽  
Vol 45 (3) ◽  
pp. e142-e143
Author(s):  
J.L. Whatmore ◽  
O. Konopatskaya ◽  
A.C. Shore
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Tyrosine Kinases ◽  
Phosphatidylinositol 3 Kinase ◽  
Human Endothelial Cells ◽  
Cgmp Production ◽  
Kinase C ◽  
Gtp Binding ◽  
Stimulation Of

scholarly journals Heparin down-regulates the phorbol ester-induced protein kinase C gene expression in human endothelial cells: enzyme-mediated autoregulation of protein kinase C-α and -δ genes1

FEBS Letters ◽  
1999 ◽  
Vol 449 (2-3) ◽  
pp. 135-140 ◽  
Author(s):  
Gianfranco Pintus ◽  
Bruna Tadolini ◽  
Margherita Maioli ◽  
Anna M. Posadino ◽  
Leonardo Gaspa ◽  
...  
Keyword(s):  
Gene Expression ◽  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Phorbol Ester ◽  
Human Endothelial Cells ◽  
Kinase C

Different pathways of degradation of SP-A and saturated phosphatidylcholine by alveolar macrophages

2000 ◽  
Vol 279 (1) ◽  
pp. L91-L99 ◽  
Author(s):  
Aldo Baritussio ◽  
Antonella Alberti ◽  
Decio Armanini ◽  
Federica Meloni ◽  
Daniela Bruttomesso
Keyword(s):  
Plasma Membrane ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Alveolar Macrophages ◽  
Surfactant Protein ◽  
Phosphatidylinositol 3 Kinase ◽  
Lysosomal Compartment ◽  
Lysosomal Ph ◽  
Kinase C ◽  
Stimulation Of

Alveolar macrophages degrade surfactant protein (SP) A and saturated phosphatidycholine [dipalmitoylphosphatidylcholine (DPPC)]. To clarify this process, using rabbit alveolar macrophages, we analyzed the effect of drugs known to affect phagocytosis, pinocytosis, clathrin-mediated uptake, caveolae, the cytoskeleton, lysosomal pH, protein kinase C, and phosphatidylinositol 3-kinase (PI3K) on the degradation of SP-A and DPPC. We found the following: 1) SP-A binds to the plasma membrane, is rapidly internalized, and then moves toward degradative compartments. Uptake could be clathrin mediated, whereas phagocytosis, pinocytosis, or the use of caveolae are less likely. An intact cytoskeleton and an acidic milieu are necessary for the degradation of SP-A. 2) Stimulation of protein kinase C increases the degradation of SP-A. 3) PI3K influences the degradation of SP-A by regulating both the speed of internalization and subsequent intracellular steps, but its inhibition does not prevent SP-A from reaching the lysosomal compartment. 4) The degradation of DPPC is unaffected by most of the treatments able to influence the degradation of SP-A. Thus it appears that DPPC is degraded by alveolar macrophages through mechanisms very different from those utilized for the degradation of SP-A.

Leptin Constrains Phospholipase C-Protein Kinase C-Induced Insulin Secretion via a Phosphatidylinositol 3-Kinase-Dependent Pathway

2003 ◽  
Vol 228 (2) ◽  
pp. 175-182 ◽  
Author(s):  
Joo-Won Lee ◽  
Andrew G. Swick ◽  
Dale R. Romsos
Keyword(s):  
Protein Kinase C ◽  
Insulin Secretion ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Phosphatidylinositol 3 Kinase ◽  
C Protein ◽  
Kinase C ◽  
Pka Pathway ◽  
Stimulation Of ◽  
Phosphatidylinositol 3

Leptin-deficient Lepob/Lepob mice hypersecrete insulin in response to acetylcholine stimulation of the phospholipase C-protein kinase C (PLC-PKC) pathway, and leptin constrains this hypersecretion. Leptin has been reported to activate phosphatidylinositol 3-kinase (PI 3-K) and subsequently phosphodiesterase (PDE) to impair protein kinase A (PKA)-induced insulin secretion from cultured islets of neonatal rats. We determined if PKA-induced insulin secretion was also hyperresponsive in Islets from Lepob/Lepob mice, and if leptin impaired this pathway in islets from these mice. Additionally, the possible role for PI 3-K and PDE in leptin-induced control of acetylcholine-induced insulin secretion was examined. Stimulation of Insulin secretion with GLP-1, forskolin (an activator of adenylyl cyclase), or IBMX (an inhibitor of PDE) did not cause hypersecretion of insulin from islets of young Lepob/Lepob mice, and leptin did not inhibit GLP-1-induced insulin secretion from islets of these mice. Inhibition of PDE with IBMX also did not block leptin-induced inhibition of acetylcholine-mediated insulin secretion from islets of Lepob/Lepob mice. But, preincubation of islets with wortmannin, an Inhibitor of PI 3-K activity, blocked the ability of leptin to constrain acetylcholine-induced insulin secretion from islets of Lepob/Lepob mice. We conclude that the capacity of the PKA pathway to stimulate insulin secretion is not increased in islets from young Lepob/Lepob mice, and that leptin does not regulate this pathway in islets from mice. Leptin may stimulate PI 3-K to constrain PLC-PKC-induced insulin secretion from Islets of Lepob/Lepob mice.

scholarly journals Stimulation of tissue plasminogen activator production by retinoic acid: synergistic effect on protein kinase C-mediated activation

Blood ◽  
1992 ◽  
Vol 80 (4) ◽  
pp. 981-987 ◽  
Author(s):  
RD Medh ◽  
L Santell ◽  
EG Levin
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Retinoic Acid ◽  
Protein Kinase ◽  
Hela Cells ◽  
Additive Effect ◽  
Kinase C ◽  
Tissue Plasminogen ◽  
Camp Levels ◽  
Stimulation Of

Abstract Trans retinoic acid (t-RA) stimulated the production of tissue plasminogen activator (tPA) in HeLa-S3 and human umbilical vein endothelial cells (huvecs) in a dose-dependent manner with maximal release (four to five times control) at 40 nmol/L and 40 mumol/L, respectively. In endothelial cells, the stimulation of tPA production by phorbol 12-myristate 13-acetate (PMA) was potentiated 1.9-fold by 10 mumol/L t-RA, or 1.8 times the additive effect. In HeLa cells, total tPA secretion with 10 nmol/L PMA was increased from 43 ng/mL to 96 ng/mL by 40 nmol/L t-RA, which was two times the additive effect. Higher concentrations of t-RA (400 nmol/L) depressed tPA secretion by itself and also suppressed PMA-induced tPA production by 50%. Histamine and thrombin also synergized with t-RA. t-RA (40 nmol/L) and 10 micrograms/mL histamine or 10 U/mL thrombin combined to induce tPA production 3.4 and 1.3 times the additive effect in HeLa cells. Cyclic adenosine monophosphate (cAMP) levels were not significantly affected by 10 nmol/L to 10 mumol/L t-RA. Nor did 10 nmol/L PMA and 40 nmol/L t- RA together affect cAMP levels, suggesting that t-RA-mediated potentiation of PMA-induced tPA production occurred via a mechanism that was independent of cAMP levels. Downregulation of protein kinase C (PKC) by pretreatment of huvecs with 100 nmol/L PMA completely blocked a secondary response to PMA, but did not have a significant effect on t- RA induction. Pretreatment with 10 mumol/L t-RA, on the other hand, did not significantly affect a secondary stimulus by 100 nmol/L PMA, but completely suppressed a secondary stimulation by 10 mumol/L t-RA alone. These studies suggest that the mechanism mediating t-RA stimulation of tPA production interacts with the PKC pathway, resulting in synergism.

Protein kinase C and cyclic AMP modulate thrombin-induced platelet-activating factor synthesis in human endothelial cells

1991 ◽  
Vol 1093 (1) ◽  
pp. 55-64 ◽  
Author(s):  
Regine Heller ◽  
Federico Bussolino ◽  
Dario Ghigo ◽  
Giovanni Garbarino ◽  
Henning Schröder ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cyclic Amp ◽  
Platelet Activating Factor ◽  
Human Endothelial Cells ◽  
Kinase C

Biphasic regulation of NADPH oxidase expression by protein kinase C in human endothelial cells

2006 ◽  
Vol 2006 (Spring) ◽  
Author(s):  
Huige Li ◽  
Hui Xu ◽  
Isolde Brausch ◽  
Marcus Hortmann ◽  
Ulrich Förstermann
Keyword(s):  
Endothelial Cells ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Nadph Oxidase ◽  
Human Endothelial Cells ◽  
Kinase C
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