scholarly journals Role of protein kinase C in cytokine secretion by lung epithelial cells during infection withParacoccidioides brasiliensis

2015 ◽  
Vol 73 (7) ◽  
pp. ftv045 ◽  
Author(s):  
Cristiane Alcantara ◽  
Paloma Korehisa Maza ◽  
Bianca Carla Silva Campitelli Barros ◽  
Erika Suzuki
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Lung Epithelial Cells ◽  
Cytokine Secretion ◽  
Kinase C ◽  
Lung Epithelial

Cytoskeletal architecture in mouse lung epithelial cells is regulated by protein-kinase C-alpha and calpain II

1996 ◽  
Vol 270 (4) ◽  
pp. L526-L534 ◽  
Author(s):  
L. D. Dwyer-Nield ◽  
A. C. Miller ◽  
B. W. Neighbors ◽  
D. Dinsdale ◽  
A. M. Malkinson
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Lung Epithelial Cells ◽  
Mouse Lung ◽  
Actin Stress Fiber ◽  
Kinase C ◽  
Lung Epithelial ◽  
Pkc Alpha ◽  
Calpain Ii

Brief exposure to 12-O-tetradecanoylphorbol 13-acetate (TPA) caused a uniformly flattened population of mouse lung epithelial cells to become more heterogeneous; some cells rounded up, and others detached to overlap with flatter cells. Actin stress fiber organization was disrupted, and F-actin accumulated in lemellipodia. Vinculin dissociated from the focal adhesion plaques to diffuse throughout the cytoplasm. Inhibition of protein kinase C (PKC) activity blocked these effects of TPA. After 8 h of TPA exposure, actin filaments reassembled and vinculin again localized to the cell periphery. Calpain inhibition attenuated the decrease of PKC-alpha protein and PKC activity from the membrane fraction, and prevented the redistribution of cytoskeletal elements. Talin immunostaining was widespread throughout control cells but was localized to the periphery 8 h after treatment with TPA or with inhibitors of PKC and calpain. Both vinculin and talin concentrations increased with prolonged TPA treatment. PKC-zeta and calpain II were not appreciably affected by TPA exposure. Translocation of PKC-alpha to the membrane, followed by its calpain-induced downmodulation, is apparently required for the reversible pattern of cytoskeletal changes caused by TPA.

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

scholarly journals Role of Protein Kinase C‐alpha in Listeriolysin‐induced ENaC dysfunction in human airway epithelial cells

2011 ◽  
Vol 25 (S1) ◽  
Author(s):  
Guang Yang ◽  
Richard White ◽  
Martin Leustik ◽  
Aluya Oseghale ◽  
Mario Marrero ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Airway Epithelial Cells ◽  
Airway Epithelial ◽  
Human Airway ◽  
Kinase C ◽  
Protein Kinase C Alpha ◽  
Human Airway Epithelial Cells

Role of the protein kinase C signaling pathway in the regulation of claudin-4 in normal human pancreatic duct epithelial cells and cancer cells

Pancreatology ◽  
2012 ◽  
Vol 12 (6) ◽  
pp. 584-585
Author(s):  
H. Yamaguchi ◽  
T. Kojima ◽  
D. Kyuno ◽  
T. Ito ◽  
Y. Kimura ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Pancreatic Duct ◽  
Cancer Cells ◽  
Signaling Pathway ◽  
Kinase C ◽  
Normal Human

Effects of sex steroids on the proliferation of thymic epithelial cells in a culture model: A role of protein kinase C

1994 ◽  
Vol 72 (3) ◽  
pp. 193-199 ◽  
Author(s):  
KOU SAKABE ◽  
ISSEI KAWASHIMA ◽  
RIE URANO ◽  
KANJI SEIKI ◽  
TSUNETOSHI ITOH
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Sex Steroids ◽  
Thymic Epithelial Cells ◽  
Kinase C ◽  
Culture Model

Regulation of mucin secretion in human gallbladder epithelial cells: Predominant role of calcium and protein kinase C

1997 ◽  
Vol 112 (3) ◽  
pp. 978-990 ◽  
Author(s):  
N Dray-Charier ◽  
A Paul ◽  
L Combettes ◽  
M Bouin ◽  
M Mergey ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Mucin Secretion ◽  
Predominant Role ◽  
Human Gallbladder ◽  
Kinase C

Role of protein kinase C in beta 2-adrenoceptor function in cultured rat proximal tubule epithelial cells

1997 ◽  
Vol 273 (2) ◽  
pp. F193-F199 ◽  
Author(s):  
H. Singh ◽  
S. L. Linas
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Atpase Activity ◽  
Proximal Tubule ◽  
Sodium Transport ◽  
Kinase C ◽  
Beta 2 ◽  
Rat Proximal Tubule

Renal sodium excretion is regulated by the adrenergic system. We recently demonstrated the presence of functional beta 2-adrenoceptors (beta 2-AR) in cultured rat proximal tubule epithelial cells beta 2-AR activation resulted in increases in Na-K-adenosinetriphosphatase (Na-K-ATPase) activity and transcellular sodium transport as a consequence of increased apical sodium entry. The purpose of this study was to determine the role of protein kinase C (PKC) on beta 2-AR-dependent increases in Na-K-ATPase activity and sodium transport in proximal tubules. To determine the effect of PKC on basal function, cultured rat proximal tubule cells were exposed to phorbol 12-myristate 13-acetate (PMA). PMA increased apical Na entry (+/-80%), decreased Na-K-ATPase activity (+/-25%), and prevented increases in Na-K-ATPase activity after sodium entry facilitation with monensin. Decreases in Na-K-ATPase activity were associated with decreases in sodium transport (+/-30%). To determine whether beta 2-AR function was transduced by PKC, PKC activity was measured in cells exposed to the selective beta 2-AR agonist metaproterenol. Metaproterenol caused increases in PKC activity, which were blocked by a beta 2-AR but not by a beta 1-AR-receptor antagonist. beta 2-AR-dependent increases in apical Na entry, Na-K-ATPase activity, and sodium transport were blocked by calphostin C or staurosporine. To determine whether PKC had additional effects on beta 2-AR function, cells were exposed to metaproterenol and PMA. Metaproterenol-induced increases in Na-K-ATPase activity and sodium transport were blocked by PMA. In conclusion, beta 2-AR-mediated increases in Na-K-ATPase activity and sodium flux are transduced by PKC acting through increases in apical Na entry. However, activation of PKC by phorbol esters inhibits beta 2-AR-dependent increases in Na-K-ATPase activity and sodium transport.

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