Flavin-containing monooxygenase-3: Induction by 3-methylcholanthrene and complex regulation by xenobiotic chemicals in hepatoma cells and mouse liver

We characterized alpha-amylase expression in the hepatoma cell line Hepa 1-6 and in normal mouse liver. Both Amy-1 and Amy-2 were expressed in Hepa 1-6 and were regulated by glucocorticoids. Transcription in the hepatoma cells was initiated at the same start sites as in mouse tissues. Glucocorticoid treatment increased the abundance of Amy-1 and Amy-2 transcripts by 10 to 20-fold. This increase was detected within 4 h and was maximal by 24 h. The pattern of amylase expression in this hepatoma cell line accurately reflects amylase expression in the liver in vivo. During liver development, we observed a large increase in the abundance of Amy-1 transcripts just before birth, at a time when circulating glucocorticoids are also elevated. Adult mouse liver expressed Amy-1 and Amy-2 at levels comparable to those of fully induced hepatoma cells. Liver is thus a likely source of both amylase isozymes in mouse serum. These studies demonstrate that Amy-2 expression is not limited to the pancreas but also occurs at a low level in liver cells.

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Selective poisoning of Ctnnb1-mutated hepatoma cells in mouse liver tumors by a single application of acetaminophen

Archives of Toxicology ◽

10.1007/s00204-013-1030-8 ◽

2013 ◽

Vol 87 (8) ◽

pp. 1595-1607 ◽

Cited By ~ 8

Author(s):

Yasmin Singh ◽

Albert Braeuning ◽

Andreas Schmid ◽

Bernd J. Pichler ◽

Michael Schwarz

Keyword(s):

Mouse Liver ◽

Liver Tumors ◽

Hepatoma Cells ◽

Single Application

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Identification of oxidized mitochondrial proteins in alcohol-exposed human hepatoma cells and mouse liver

PROTEOMICS ◽

10.1002/pmic.200400971 ◽

2004 ◽

Vol 4 (11) ◽

pp. 3401-3412 ◽

Cited By ~ 61

Author(s):

Soo-Kyung Suh ◽

Brian L. Hood ◽

Bong-Jo Kim ◽

Thomas P. Conrads ◽

Timothy D. Veenstra ◽

...

Keyword(s):

Mouse Liver ◽

Hepatoma Cells ◽

Mitochondrial Proteins ◽

Human Hepatoma ◽

Human Hepatoma Cells

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Effect of Standardized Decoction of Nigella sativa Seed, Hemidesmus indicus Root and Smilax glabra Rhizome on the Expression of p53 and p21 Genes in Human Hepatoma Cells (HepG2) and Mouse Liver with Chemically-Induced Hepatocarcinogenesis

Tropical Journal of Pharmaceutical Research ◽

10.4314/tjpr.v11i1.7 ◽

2012 ◽

Vol 11 (1) ◽

Cited By ~ 5

Author(s):

SR Samarakoon ◽

I Thabrew ◽

PB Galhena ◽

KH Tennekoon

Keyword(s):

Mouse Liver ◽

Nigella Sativa ◽

Hepatoma Cells ◽

Human Hepatoma ◽

Human Hepatoma Cells ◽

Hemidesmus Indicus ◽

Chemically Induced

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Glucocorticoid and developmental regulation of amylase mRNAs in mouse liver cells.

Molecular and Cellular Biology ◽

10.1128/mcb.8.9.3857 ◽

1988 ◽

Vol 8 (9) ◽

pp. 3857-3863 ◽

Cited By ~ 14

Author(s):

L C Samuelson ◽

P R Keller ◽

G J Darlington ◽

M H Meisler

Keyword(s):

Cell Line ◽

Mouse Liver ◽

Hepatoma Cell ◽

Hepatoma Cells ◽

Liver Cells ◽

Mouse Serum ◽

Hepatoma Cell Line ◽

Glucocorticoid Treatment ◽

Mouse Tissues

We characterized alpha-amylase expression in the hepatoma cell line Hepa 1-6 and in normal mouse liver. Both Amy-1 and Amy-2 were expressed in Hepa 1-6 and were regulated by glucocorticoids. Transcription in the hepatoma cells was initiated at the same start sites as in mouse tissues. Glucocorticoid treatment increased the abundance of Amy-1 and Amy-2 transcripts by 10 to 20-fold. This increase was detected within 4 h and was maximal by 24 h. The pattern of amylase expression in this hepatoma cell line accurately reflects amylase expression in the liver in vivo. During liver development, we observed a large increase in the abundance of Amy-1 transcripts just before birth, at a time when circulating glucocorticoids are also elevated. Adult mouse liver expressed Amy-1 and Amy-2 at levels comparable to those of fully induced hepatoma cells. Liver is thus a likely source of both amylase isozymes in mouse serum. These studies demonstrate that Amy-2 expression is not limited to the pancreas but also occurs at a low level in liver cells.

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Ultrastructural localization of specific nucleoprotein fractions

Proceedings, annual meeting, Electron Microscopy Society of America ◽

10.1017/s0424820100081887 ◽

1978 ◽

Vol 36 (2) ◽

pp. 204-205

Author(s):

G. L. Brown

Keyword(s):

Gel Electrophoresis ◽

Mouse Liver ◽

Polyacrylamide Gel Electrophoresis ◽

Ultrastructural Localization ◽

Polyacrylamide Gel ◽

Acid Extraction ◽

Acid Solutions ◽

Low Salt ◽

Liver Nuclei ◽

Phosphate Groups

Bismuth (Bi) stains nucleoproteins (NPs) by interacting with available amino and primary phosphate groups. These two staining mechanisms are distinguishable by glutaraldehyde crosslinking (Fig. 1,2).Isolated mouse liver nuclei, extracted with salt and acid solutions, fixed in either formaldehyde (form.) or gl utaraldehyde (glut.) and stained with Bi, were viewed to determine the effect of the extractions on Bi stainina. Solubilized NPs were analyzed by SDS-polyacrylamide gel electrophoresis.Extraction with 0.14 M salt does not change the Bi staining characteristics (Fig. 3). 0.34 M salt reduces nucleolar (Nu) staining but has no effect on interchromatinic (IC) staining (Fig. 4). Proteins responsible for Nu and glut.- insensitive IC staining are removed when nuclei are extracted with 0.6 M salt (Fig. 5, 6). Low salt and acid extraction prevents Bi-Nu staining but has no effect on IC staining (Fig. 7). When nuclei are extracted with 0.6 M salt followed by low salt and acid, all Bi-staining components are removed (Fig. 8).

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