Differential Expression of Five Protein Kinase C Isoenzymes in FAO and HEPG2 Hepatoma Cell Lines Compared with Normal Rat Hepatocytes

1995 ◽  
Vol 217 (2) ◽  
pp. 546-553 ◽  
Author(s):  
L. Ducher ◽  
F. Croquet ◽  
S. Gil ◽  
J. Davy ◽  
J. Feger ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Differential Expression ◽  
Cell Lines ◽  
Hepatoma Cell ◽  
Rat Hepatocytes ◽  
Hepatoma Cell Lines ◽  
Kinase C ◽  
Normal Rat ◽  
Hepg2 Hepatoma Cell

Use of Cultured Hepatoma Cell Lines in the Assessment of Aldehyde Metabolism

1992 ◽  
Vol 20 (1) ◽  
pp. 77-83
Author(s):  
Margherita Ferro ◽  
Anna Maria Bassi ◽  
Susanna Penco ◽  
Sandra Piana ◽  
Giambattista Ravera ◽  
...  
Keyword(s):  
Cell Line ◽  
Cell Lines ◽  
Hepatoma Cell ◽  
Rat Hepatocytes ◽  
Experimental Conditions ◽  
Major Pathway ◽  
Hepatoma Cell Lines ◽  
Normal Rat ◽  
Htc Cells

Aldehyde dehydrogenases (ALDH) represent a major pathway for the enzymatic removal of many potentially toxic aldehydes. The purpose of this study was to examine the basal levels of ALDH in five hepatoma cell lines chosen as representatives of three different species (man, rat, mouse) and their inducibility by some xenobiotics. Human HepG2, rat MH1C1, HTC, H4IIEC3 and mouse Hepa 1c1c7 cell lines were grown as monolayers. The ALDH activities were determined in cell homogenates from both unexposed control cultures and cells exposed to phenobarbital (PB), 3-methylcholanthrene (MC) and β-naphthoflavone (BNF). The ALDH activity was detected using benzaldehyde (BA) and propionaldehyde (PA) as substrates and both NAD and NADP as co-enzymes. Great variability in basal ALDH levels was found in the five cell lines: BA/NAD and BA/NADP enzyme activities were very high in the HTC cell line, intermediate in MH1C1 cells (near to normal rat hepatocytes) and very low in the remaining three cell lines. In HTC cells only, the PA/NAD activity was slightly induced by PB, but it remained unchanged under all the other experimental conditions. MH1C1 cells showed highly significant increases of all the activities with MC and BNF (up to 10-fold). The low basal activity of the H4IIEC3 cell line was significantly increased by MC and BNF, but only with BA/NADP. The Hepa 1c1c7 cell line responded only to BNF, as inducing compound, whereas the low basal enzyme levels of the human-derived HepG2 cell line were not significantly increased. These results suggest various applications of hepatoma cell cultures in in vitro toxicology.

Differential Expression of Protein Kinase C Genes in Cultured Mast Cells Derived from Normal and Mast-Cell-Deficient Mice and Mast Cell Lines

1994 ◽  
Vol 105 (3) ◽  
pp. 258-263 ◽  
Author(s):  
Hyung-Min Kim ◽  
Seiichi Hirota ◽  
Hun-Taeg Chung ◽  
Shigeo Ohno ◽  
Shin-Ichi Osada ◽  
...  
Keyword(s):  
Mast Cell ◽  
Protein Kinase C ◽  
Mast Cells ◽  
Protein Kinase ◽  
Differential Expression ◽  
Cell Lines ◽  
Kinase C ◽  
Deficient Mice

scholarly journals Nanog expression is negatively regulated by protein kinase C activities in human cancer cell lines

2013 ◽  
Vol 34 (7) ◽  
pp. 1497-1509 ◽  
Author(s):  
Wing-Keung Chu ◽  
Pei-Min Dai ◽  
Hsin-Lun Li ◽  
Chia-Chu Pao ◽  
Jan-Kan Chen
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Lines ◽  
Cancer Cell ◽  
Human Cancer ◽  
Cancer Cell Lines ◽  
Human Cancer Cell ◽  
Human Cancer Cell Lines ◽  
Nanog Expression ◽  
Kinase C

scholarly journals Differential responsiveness of intestinal epithelial cells to 1,25-dihydroxyvitamin D3--role of protein kinase C

2001 ◽  
Vol 169 (1) ◽  
pp. 145-151 ◽  
Author(s):  
HJ Armbrecht ◽  
MA Boltz ◽  
TL Hodam ◽  
VB Kumar
Keyword(s):  
Vitamin D ◽  
Protein Kinase C ◽  
Protein Kinase ◽  
Cell Lines ◽  
Phorbol Esters ◽  
Mrna Levels ◽  
Intestinal Epithelial ◽  
Vitamin D Receptors ◽  
Kinase C ◽  
Crypt Cells

Non-transformed rat intestinal epithelial cell (IEC) lines were used to study the action of 1,25-dihydroxyvitamin D(3) (1,25(OH)2D) in the intestine. The capacity of 1,25(OH)2D to increase the expression of the cytochrome P450 component of the vitamin D 24-hydroxylase (CYP24) was determined in IEC-6 and IEC-18 cell lines. In IEC-6 cells, which are derived from crypt cells isolated from the whole small intestine, 1,25(OH)2D markedly increased expression of CYP24 protein and mRNA within 12 h. In contrast, in IEC-18 cells, which are derived from crypt cells from the ileum only, 1,25(OH)2D did not increase expression of CYP24 until 24-48 h. The maximal levels of CYP24 mRNA seen in the IEC-18 cells were only 31% of the maximal levels seen in the IEC-6 cells. In the presence of 1,25(OH)2D, phorbol esters rapidly increased CYP24 mRNA levels in IEC-18 cells from almost undetectable to levels seen in IEC-6 cells. Protein kinase inhibitors abolished the stimulation by 1,25(OH)2D and by phorbol esters in both cell lines. Stimulation of mRNA levels by phorbol esters required new protein synthesis but stimulation by 1,25(OH)2D did not. These studies demonstrated that the rapid action of 1,25(OH)2D in IEC-6 cells is related to the activation of protein kinase C, an event which is missing in the IEC-18 cells. This differential response to 1,25(OH)2D probably takes place at a post-receptor site, since the number of vitamin D receptors in each cell line was found to be similar.

Different Expression of Esterase Variants in Rat Hepatic and Hepatom a-Derived Cell Lines Detected by Electrophoresis

1995 ◽  
Vol 50 (9-10) ◽  
pp. 664-668 ◽  
Author(s):  
Adel S. Afify ◽  
Yoshimitsu Yamazaki ◽  
Yu-ichi Kageyama ◽  
Shiro Yusa ◽  
Yoshikatsu Ogawa ◽  
...  
Keyword(s):  
Cell Lines ◽  
Rat Liver ◽  
Hepatoma Cell ◽  
Polyacrylamide Gel Electrophoresis ◽  
Liver Homogenate ◽  
Normal Liver ◽  
Liver Parenchyma ◽  
Hepatoma Cell Lines ◽  
Normal Rat ◽  
Transformed Cell Lines

Abstract Esterases in nine rat hepatic and hepatoma-derived cell lines and normal rat liver homogenate were detected by polyacrylamide gel electrophoresis coupled with active staining with a-naphthyl acetate or butyrate as a substrate. The esterase band patterns of the non-cancerous and oncogene-transformed cell lines were alike, but different from those of hepatoma cell lines and normal rat liver homogenate. The former groups of cells might have completely lost the characteristics of rat liver parenchymal cells, or else they might have their origin at cells other than liver parenchyma. The esterase patterns of the hepatoma cell lines (e.g., McA-RH7777) and the normal rat liver highly resembled with each other, exemplifying the slight biochemical deviation of cancer from normal cells. However, two-dimensional electrophoretogram for the McA-RH7777 cell line showed a prominent esterase spot {p/ 6.0-Mr 110 kDa) that was lacking in the normal liver. This result indicates that there is invariably some change in esterase expression between the cancer cells and the normal liver cells

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