The role of fibronectin and atypical protein kinase C iota in the development of notochord and chondrocytes

2013 ◽  
Author(s):  
Mo Wang
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Iota

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 Atypical protein kinase C iota (PKCλ/ι) ensures mammalian development by establishing the maternal–fetal exchange interface

2020 ◽  
Vol 117 (25) ◽  
pp. 14280-14291
Author(s):  
Bhaswati Bhattacharya ◽  
Pratik Home ◽  
Avishek Ganguly ◽  
Soma Ray ◽  
Ananya Ghosh ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Mammalian Development ◽  
Atypical Protein Kinase C ◽  
Differentiation Potential ◽  
Human Trophoblast ◽  
Atypical Protein Kinase ◽  
Kinase C ◽  
Trophoblast Stem ◽  
Protein Kinase C Iota

In utero mammalian development relies on the establishment of the maternal–fetal exchange interface, which ensures transportation of nutrients and gases between the mother and the fetus. This exchange interface is established via development of multinucleated syncytiotrophoblast cells (SynTs) during placentation. In mice, SynTs develop via differentiation of the trophoblast stem cell-like progenitor cells (TSPCs) of the placenta primordium, and in humans, SynTs are developed via differentiation of villous cytotrophoblast (CTB) progenitors. Despite the critical need in pregnancy progression, conserved signaling mechanisms that ensure SynT development are poorly understood. Herein, we show that atypical protein kinase C iota (PKCλ/ι) plays an essential role in establishing the SynT differentiation program in trophoblast progenitors. Loss of PKCλ/ι in the mouse TSPCs abrogates SynT development, leading to embryonic death at approximately embryonic day 9.0 (E9.0). We also show that PKCλ/ι-mediated priming of trophoblast progenitors for SynT differentiation is a conserved event during human placentation. PKCλ/ι is selectively expressed in the first-trimester CTBs of a developing human placenta. Furthermore, loss of PKCλ/ι in CTB-derived human trophoblast stem cells (human TSCs) impairs their SynT differentiation potential both in vitro and after transplantation in immunocompromised mice. Our mechanistic analyses indicate that PKCλ/ι signaling maintains expression of GCM1, GATA2, and PPARγ, which are key transcription factors to instigate SynT differentiation programs in both mouse and human trophoblast progenitors. Our study uncovers a conserved molecular mechanism, in which PKCλ/ι signaling regulates establishment of the maternal–fetal exchange surface by promoting trophoblast progenitor-to-SynT transition during placentation.

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.

Role of atypical protein kinase C isozymes and NF-κB in IL-1β-induced expression of cyclooxygenase-2 in human myometrial smooth muscle cells

2006 ◽  
Vol 210 (3) ◽  
pp. 637-643 ◽  
Author(s):  
Sara V. Duggan ◽  
Tamsin Lindstrom ◽  
Teresa Iglesias ◽  
Phillip R. Bennett ◽  
Giovanni E. Mann ◽  
...  
Keyword(s):  
Smooth Muscle ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Smooth Muscle Cells ◽  
Muscle Cells ◽  
Atypical Protein Kinase C ◽  
Induced Expression ◽  
Atypical Protein Kinase ◽  
Kinase C
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