scholarly journals Mechanism of HIV-1-TAT induction of interleukin-1β from human monocytes: Involvement of the phospholipase C/protein kinase C signaling cascade

2010 ◽  
Vol 82 (5) ◽  
pp. 735-746 ◽  
Author(s):  
Yongbo Yang ◽  
Jianguo Wu ◽  
Yuanan Lu
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Interleukin 1Β ◽  
Signaling Cascade ◽  
Human Monocytes ◽  
C Protein ◽  
Kinase C ◽  
Hiv 1

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.

Assembly and sealing of tight junctions: Possible participation of G-proteins, phospholipase C, protein kinase C and calmodulin

1991 ◽  
Vol 122 (3) ◽  
pp. 193-202 ◽  
Author(s):  
M. S. Balda ◽  
L. González-Mariscal ◽  
R. G. Contreras ◽  
M. Macias-Silva ◽  
M. E. Torres-Marquez ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Tight Junctions ◽  
G Proteins ◽  
C Protein ◽  
Kinase C

Phospholipase C-protein kinase C mediated phospholipase D activation pathway is involved in tamoxifen induced apoptosis

2003 ◽  
Vol 89 (3) ◽  
pp. 520-528 ◽  
Author(s):  
Soo-Jung Ahn ◽  
Mee-Sup Yoon ◽  
Shin Hyuk ◽  
Wonshik Han ◽  
Yong-Dal Yoon ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase C ◽  
Phospholipase D ◽  
C Protein ◽  
Activation Pathway ◽  
Kinase C ◽  
Induced Apoptosis

Leishmania amazonensis: Heme stimulates (Na++K+)ATPase activity via phosphatidylinositol-specific phospholipase C/protein kinase C-like (PI-PLC/PKC) signaling pathways

2010 ◽  
Vol 124 (4) ◽  
pp. 436-441 ◽  
Author(s):  
Elmo Eduardo Almeida-Amaral ◽  
Viviane Carrozino Cardoso ◽  
Fernanda Gomes Francioli ◽  
José Roberto Meyer-Fernandes
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atpase Activity ◽  
Signaling Pathways ◽  
Phospholipase C ◽  
Leishmania Amazonensis ◽  
C Protein ◽  
Kinase C ◽  
Pkc Signaling

Human interleukin 1β stimulates islet insulin release by a mechanism not dependent on changes in phospholipase C and protein kinase C activities or Ca2+ handling

1989 ◽  
Vol 121 (5) ◽  
pp. 698-704 ◽  
Author(s):  
Nils Welsh ◽  
Thomas Nilsson ◽  
Anders Hallberg ◽  
Per Arkhammar ◽  
Per-Olof Berggren ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Protein Phosphorylation ◽  
Phospholipase C ◽  
Insulin Release ◽  
Interleukin 1Β ◽  
High Concentration ◽  
Adult Rats ◽  
Kinase C ◽  
Protein Kinase C Activity

Abstract. Isolated islets from adult rats or obese hyperglycemic (ob/ob) mice were incubated with human recombinant interleukin 1β in order to study whether the acute effects of the cytokine on islet insulin release are associated with changes in islet phospholipase C activity, Ca2+ handling or protein phosphorylation. The cytokine stimulated insulin release both at low and high glucose concentrations during one hour incubations. In shortterm incubations (<1 min) interleukin 1β did not affect the production of inositoltrisphosphate. Addition of interleukin 1β affected neither the cytoplasmic free Ca2+ concentration at rest nor that observed subsequent to stimulation with a high concentration of glucose. Furthermore, the endogenous protein kinase C activity, as visualized by immunoprecipitation of a 32P-labelled substrate for this enzyme, was not altered by interleukin 1β. Separation of 32P-labelled proteins by means of 2-dimensional gel electrophoresis failed to reveal any specific effects of the cytokine on the total protein phosphorylation activity. These results suggest that the stimulatory effects on insulin release exerted by interleukin 1β are not caused by acute activation of phospholipase C and protein kinase C or by an alteration of islet Ca2+ handling of the B-cells.

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