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

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

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

scholarly journals Vasopressin-induced activation of protein kinase C in renal epithelial cells

1998 ◽  
Vol 1402 (2) ◽  
pp. 188-196 ◽  
Author(s):  
Nawab Ali ◽  
Surasak Kantachuvesiri ◽  
Joan I Smallwood ◽  
Lawrence J Macala ◽  
Carlos Isales ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Epithelial Cells ◽  
Renal Epithelial Cells ◽  
Kinase C

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

Stimulus-secretion coupling in parathyroid cells deficient in protein kinase C activity

1994 ◽  
Vol 267 (3) ◽  
pp. E429-E438
Author(s):  
F. K. Racke ◽  
E. F. Nemeth
Keyword(s):  
Protein Kinase C ◽  
Parathyroid Hormone ◽  
Protein Kinase ◽  
Kinase C ◽  
Protein Kinase C Activity ◽  
Low Concentrations ◽  
Stimulus Secretion Coupling ◽  
Subsequent Addition ◽  
In Cells

The role of protein kinase C (PKC) in regulating cytosolic Ca2+ concentrations ([Ca2+]i) and parathyroid hormone (PTH) secretion was studied in bovine parathyroid cells rendered deficient in PKC activity by incubation with phorbol 12-myristate 13-acetate (PMA). Pretreatment with PMA caused a time- and concentration-dependent loss of functional PKC activity as assessed by the failure of [Ca2+]i and PTH secretion to respond to the subsequent addition of PKC activators or the inhibitor staurosporine. Pretreatment for 24 h with 1 microM PMA caused a loss of 85% of the total and 98% of the cytosolic PKC activity. Cells so pretreated were considered to be "PKC downregulated." Increasing the concentration of extracellular Ca2+ or Mg2+ caused corresponding increases in [Ca2+]i that were similar in control and in PKC-downregulated cells. PTH secretion regulated by extracellular Ca2+ or Mg2+ was likewise similar in control and PKC-downregulated cells. Stimulus-secretion coupling is thus unimpaired in parathyroid cells deficient in PKC activity. Cytosolic Ca2+ responses remained depressed in cells incubated for 24 h with low concentrations of PMA (30 or 100 nM). However, under these conditions, extracellular Ca2+ still suppressed PTH secretion similarly to control cells. These results reveal a dissociation between cytosolic Ca2+ and PTH secretion and suggest that signals other than cytosolic Ca2+ are involved in the regulation of PTH secretion.

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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