Protein Kinase C Isoenzyme Expression in Normal Mouse Mammary Epithelial Cells Grown in Primary Culture

1996 ◽  
Vol 213 (1) ◽  
pp. 65-70 ◽  
Author(s):  
H. P. Birkenfeld ◽  
B. S. McIntyre ◽  
K. P. Briski ◽  
P. W. Sylvester
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Primary Culture ◽  
Normal Mouse ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Kinase C

scholarly journals The α isoform of protein kinase C mediates phorbol ester-induced growth inhibition and p21cip1 induction in HC11 mammary epithelial cells

Oncogene ◽  
1999 ◽  
Vol 18 (48) ◽  
pp. 6658-6666 ◽  
Author(s):  
Eric D Slosberg ◽  
Michael G Klein ◽  
Yao Yao ◽  
Edward Kyu-Ho Han ◽  
Ira Schieren ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Growth Inhibition ◽  
Phorbol Ester ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Kinase C

Protein Kinase C Enhances Tight Junction Barrier Function of Human Nasal Epithelial Cells in Primary Culture by Transcriptional Regulation

2008 ◽  
Vol 74 (2) ◽  
pp. 432-442 ◽  
Author(s):  
Jun-ichi Koizumi ◽  
Takashi Kojima ◽  
Noriko Ogasawara ◽  
Ryuta Kamekura ◽  
Makoto Kurose ◽  
...  
Keyword(s):  
Transcriptional Regulation ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Tight Junction ◽  
Primary Culture ◽  
Barrier Function ◽  
Nasal Epithelial Cells ◽  
Kinase C ◽  
Human Nasal Epithelial Cells

Regulation of phospholipase D isoenzymes by transforming Ras and atypical protein kinase C-ι

2001 ◽  
Vol 359 (1) ◽  
pp. 211-217 ◽  
Author(s):  
James MWANJEWE ◽  
Martin SPITALER ◽  
Maria EBNER ◽  
Michaela WINDEGGER ◽  
Markus GEIGER ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phospholipase D ◽  
Mammalian Cells ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Common Mechanism ◽  
Kinase C ◽  
Hc11 Cells

The activation of phospholipase D (PLD) by transforming Ras is well documented. Although two distinct PLD isoforms, PLD1 and PLD2, have been cloned from mammalian cells, it has remained unclear whether both isoenzymes are activated by Ras and, if this is the case, whether they are stimulated by a common mechanism. In the present study we show that expression of transforming Ras in HC11 mouse mammary epithelial cells enhanced the activity of endogenous PLD. Co-expression of Ras with either PLD1b or PLD2 resulted in elevated activities of both PLD isoenzymes in HC11 cells, indicating that transforming Ras was capable of activating both PLD isoforms in vivo. Ras-induced activation of PLD was resistant to the protein kinase C (PKC) inhibitor GF109203X, which preferentially affects conventional- and novel-type PKCs, but sensitive to Ro-31-8220, which inhibits atypical PKCs more effectively. Co-transfection of atypical PKC-ι with either PLD1b or PLD2 led to a selective activation of PLD2 by PKC-ι, whereas PLD1b was not affected. PLD1b, however, was found to be a potent activator of PKC-ι, whereas PLD2 was less effective in this respect. The data suggest that PKC-ι acts upstream of PLD2 and that PLD1b is implicated in the activation of PKC-ι. The data are discussed as indicating a putative signalling cascade comprising Ras → PLD1b →PKC-ι → PLD2. Evidence for the implication of this pathway in the transcriptional regulation of cyclin D1 is also presented.

A Study of Protein Kinase C Isozyme Distribution in Relation to Bcl-2 Expression during Apoptosis of Epithelial Cells in Vivo

1993 ◽  
Vol 207 (1) ◽  
pp. 68-73 ◽  
Author(s):  
Kirstine A. Knox ◽  
Gerald D. Johnson ◽  
John Gordon
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Kinase C

scholarly journals Atypical protein kinase C induces cell transformation by disrupting Hippo/Yap signaling

2015 ◽  
Vol 26 (20) ◽  
pp. 3578-3595 ◽  
Author(s):  
Andrew Archibald ◽  
Maia Al-Masri ◽  
Alyson Liew-Spilger ◽  
Luke McCaffrey
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
3D Culture ◽  
Cell Junctions ◽  
Nuclear Accumulation ◽  
Cell Phenotype ◽  
Atypical Protein Kinase C ◽  
Atypical Protein Kinase ◽  
Kinase C

Epithelial cells are major sites of malignant transformation. Atypical protein kinase C (aPKC) isoforms are overexpressed and activated in many cancer types. Using normal, highly polarized epithelial cells (MDCK and NMuMG), we report that aPKC gain of function overcomes contact inhibited growth and is sufficient for a transformed epithelial phenotype. In 2D cultures, aPKC induced cells to grow as stratified epithelia, whereas cells grew as solid spheres of nonpolarized cells in 3D culture. aPKC associated with Mst1/2, which uncoupled Mst1/2 from Lats1/2 and promoted nuclear accumulation of Yap1. Of importance, Yap1 was necessary for aPKC-mediated overgrowth but did not restore cell polarity defects, indicating that the two are separable events. In MDCK cells, Yap1 was sequestered to cell–cell junctions by Amot, and aPKC overexpression resulted in loss of Amot expression and a spindle-like cell phenotype. Reexpression of Amot was sufficient to restore an epithelial cobblestone appearance, Yap1 localization, and growth control. In contrast, the effect of aPKC on Hippo/Yap signaling and overgrowth in NMuMG cells was independent of Amot. Finally, increased expression of aPKC in human cancers strongly correlated with increased nuclear accumulation of Yap1, indicating that the effect of aPKC on transformed growth by deregulating Hippo/Yap1 signaling may be clinically relevant.

Parathyroid hormone stimulates ecto-5'-nucleotidase activity in renal epithelial cells: role of protein kinase-C.

Endocrinology ◽  
1995 ◽  
Vol 136 (3) ◽  
pp. 1267-1275 ◽  
Author(s):  
G Siegfried ◽  
F Vrtovsnik ◽  
D Prié ◽  
C Amiel ◽  
G Friedlander
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Nucleotidase Activity ◽  
Renal Epithelial Cells ◽  
Kinase C
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