scholarly journals An Atypical Protein Kinase C (PKCζ) Plays a Critical Role in Lipopolysaccharide-Activated NF-κB in Human Peripheral Blood Monocytes and Macrophages

2009 ◽  
Vol 182 (9) ◽  
pp. 5810-5815 ◽  
Author(s):  
XueSong Huang ◽  
Ling-Yu Chen ◽  
Astrid M. Doerner ◽  
Warren W. Pan ◽  
Laura Smith ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Critical Role ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Monocytes And Macrophages

scholarly journals A Novel Protein Kinase C (PKCϵ) Is Required for fMet-Leu-Phe-induced Activation of NF-κB in Human Peripheral Blood Monocytes

2005 ◽  
Vol 280 (23) ◽  
pp. 22497-22501 ◽  
Author(s):  
Ling-Yu Chen ◽  
Astrid Doerner ◽  
Paul F. Lehmann ◽  
Shuang Huang ◽  
Guangming Zhong ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Peripheral Blood ◽  
Rho Gtpase ◽  
Human Peripheral Blood ◽  
Small Gtpase ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Kinase C ◽  
Novel Protein

We have reported that the chemoattractant, fMet-Leu-Phe (fMLP), induces the activation of NF-κB in human peripheral blood monocytes and that this requires the activity of small GTPase, RhoA (Huang, S., Chen, L.-Y., Zuraw, B. L., Ye, R. D., and Pan, Z. K. (2001) J. Biol. Chem. 276, 40977-40981). Here we showed that the novel protein kinase C isozyme, PKCϵ, associates functionally with RhoA in fMLP-stimulated monocytes and that PKCϵ acted as a signaling component downstream of the GTPase RhoA during fMLP-induced activation of NF-κB. Stimulation of monocytes with fMLP resulted in activation of both PKCϵ and NF-κB. This latter activation was largely blocked by specific inhibitors of PKCϵ by transient expression of a dominant-negative form of PKCϵ and by PKCϵ-specific short interfering RNA. These findings demonstrate, for the first time, that fMLP-induced activation of NF-κB utilizes a signaling pathway, which requires activity of PKCϵ, and that PKCϵ acts as a signaling component downstream of RhoA in cytokine gene transcription stimulated by a chemoattractant. The specificity of this response suggests an important role for the Rho GTPase-PKCϵ-NF-κB pathway in host defense and represents a novel and potentially important mechanism through which fMLP not only attracts leukocytes but may also contribute directly to inflammation.

scholarly journals The critical role of atypical protein kinase C in activating hepatic SREBP-1c and NFκB in obesity

2009 ◽  
Vol 50 (6) ◽  
pp. 1133-1145 ◽  
Author(s):  
Mini P. Sajan ◽  
Mary L. Standaert ◽  
Sonali Nimal ◽  
Usha Varanasi ◽  
Tina Pastoor ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Critical Role ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C

scholarly journals The Drosophila Atypical Protein Kinase C-Ref(2)P Complex Constitutes a Conserved Module for Signaling in the Toll Pathway

2002 ◽  
Vol 22 (24) ◽  
pp. 8787-8795 ◽  
Author(s):  
Antonia Avila ◽  
Neal Silverman ◽  
María T. Diaz-Meco ◽  
Jorge Moscat
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Nuclear Translocation ◽  
Critical Role ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
P Protein ◽  
Toll Signaling

ABSTRACT Recent results showed the critical role of the mammalian p62-atypical protein kinase C (aPKC) complex in the activation of NF-κB in response to different stimuli. Here we demonstrate using the RNA interference technique on Schneider cells that the Drosophila aPKC (DaPKC) is required for the stimulation of the Toll-signaling pathway, which activates the NF-κB homologues Dif and Dorsal. However, DaPKC does not appear to be important for the other Drosophila NF-κB signaling cascade, which activates the NF-κB homologue Relish in response to lipopolysaccharides. Interestingly, DaPKC functions downstream of the nuclear translocation of Dorsal or Dif, controlling the transcriptional activity of the Drosomycin promoter. We also show that the Drosophila Ref(2)P protein is the homologue of mammalian p62 as it binds to DaPKC, its overexpression is sufficient to activate the Drosomycin but not the Attacin promoter, and its depletion severely impairs Toll signaling. Collectively, these results demonstrate the conservation of the p62-aPKC complex for the control of innate immunity signal transduction in Drosophila melanogaster.

scholarly journals Tat Protein of Human Immunodeficiency Virus Type 1 Induces Interleukin-10 in Human Peripheral Blood Monocytes: Implication of Protein Kinase C-Dependent Pathway

2000 ◽  
Vol 74 (22) ◽  
pp. 10551-10562 ◽  
Author(s):  
Abdallah Badou ◽  
Yamina Bennasser ◽  
Marc Moreau ◽  
Catherine Leclerc ◽  
Monsef Benkirane ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Interleukin 10 ◽  
Tat Protein ◽  
Blood Monocytes ◽  
Peripheral Blood Monocytes ◽  
Kinase C ◽  
Immunodeficiency Virus ◽  
Hiv 1

ABSTRACT The clinical manifestations observed in human immunodeficiency virus type 1 (HIV-1)-infected patients are primarily due to the capacity of the virus and its components to inactivate the immune system. HIV-1 Tat protein could participate in this immune system disorder. This protein is secreted by infected cells of HIV-infected patients and is free in the plasma, where it can interact and be taken up by both infected and noninfected cells. In asymptomatic patients infected by HIV-1, production of interleukin-10 (IL-10), a highly immunosuppressive cytokine, is associated with disease progression to AIDS. In the present work, we tested the capacity of Tat to induce IL-10 production by peripheral blood monocytes of healthy donors. The results show that Tat causes the production of IL-10 in a dose- and stimulation time-dependent manner. Investigations of the mechanisms involved in signal transduction show that (i) the calcium pathway is not or only slightly involved in Tat-induced IL-10 production, (ii) the protein kinase C pathway plays an essential role, and (iii) monocyte stimulation by Tat results in the intranuclear translocation of transcription factor NF-κB and in the induction of phosphorylation of the mitogen-activated protein kinases ERK1 and ERK2; activation of these two potential substrates of protein kinase C is required for the production of IL-10. Finally, our results suggest that the effect of Tat is exerted at the membrane level and that the active domain is located within N-terminal residues 1 to 45. This production of IL-10 induced by Tat could participate in the progression of HIV infection to AIDS.

Cyclosporine inhibits protein kinase C-dependent signals in human peripheral blood lymphocytes

1989 ◽  
Vol 46 (4) ◽  
pp. 292-295 ◽  
Author(s):  
Marvin A. McMillen ◽  
Harold A. Schaefer ◽  
John D. MacArthur ◽  
Thomas A. Adrian ◽  
Irvin M. Modlin
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Peripheral Blood ◽  
Human Peripheral Blood ◽  
Peripheral Blood Lymphocytes ◽  
Blood Lymphocytes ◽  
Human Peripheral Blood Lymphocytes ◽  
Kinase C
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