Skip Navigation

This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (38)
Right arrowRequest Permissions
Google Scholar
Right arrow Articles by Sun, Y.
Right arrow Articles by Oberley, L. W.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sun, Y.
Right arrow Articles by Oberley, L. W.
Social Bookmarking
 Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

© 1993 Oxford University Press

research-article

Depression of catalase gene expression after immortalization and transformation of mouse liver cells

Yi Sun, Nancy H. Colburn and Larry W. Oberley 1

Cell Biology Section, Laboratory of Viral Carcinogenesis, National Cancer Institute, Frederick Cancer Research and Development Center Frederick, MD
1Radiation Research Laboratory, 14 Medical Laboratories, The University of lowa IA, USA

To understand the molecular basis of the remarkable decrease of catalase activity after immortalization and malignant transformation of mouse liver cells, expression of the catalase gene was studied in in vivo mouse liver cells and nontrans-formed normal mouse liver cell line as well as liver cell lines transformed by N-methyl-N-nitro-N-nitrosoguanidine, SV40 virus or by conventional subcultivation. In vivo liver cells had much greater levels of catalase mRNA and immunoreactive protein than in vitro cell lines, which correlates with elevated enzyme activity. Among the cell lines, normal cells had in general higher mRNA levels and more catalase protein than that of the transformed cell lines, also correlating with enzyme activity. The down regulation of catalase gene expression seen in transformed lines may occur transcriptionally rather than posttranscriptionally as demonstrated by cycloheximide and/or actinomycin D treatment. The striking difference in catalase gene expression seen between liver tissue and liver cell lines was unlikely due to gross structural alterations in the catalase gene, but might be explained by a remarkable difference in methylation status of the catalase gene, as demonstrated by Southern blot analysis following HpaII digestion. Our results suggested that during cellular immortalization and malignant transformation, a change in the oxidant stress ultimately led to a cellular response that, in turn, led to down regulation of the catalase gene.


Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
J. Nutr.Home page
Y. Li and H. E. Schellhorn
New Developments and Novel Therapeutic Perspectives for Vitamin C
J. Nutr., October 1, 2007; 137(10): 2171 - 2184.
[Abstract] [Full Text] [PDF]


Home page
Integr Cancer TherHome page
M. J. Gonzalez, J. R. Miranda-Massari, E. M. Mora, A. Guzman, N. H. Riordan, H. D. Riordan, J. J. Casciari, J. A. Jackson, and A. Roman-Franco
Orthomolecular Oncology Review: Ascorbic Acid and Cancer 25 Years Later
Integr Cancer Ther, March 1, 2005; 4(1): 32 - 44.
[Abstract] [PDF]


Home page
Mol. Endocrinol.Home page
G. D. Girnun, F. E. Domann, S. A. Moore, and M. E. C. Robbins
Identification of a Functional Peroxisome Proliferator-Activated Receptor Response Element in the Rat Catalase Promoter
Mol. Endocrinol., December 1, 2002; 16(12): 2793 - 2801.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
M. R. Brown, F. J. Miller Jr, W.-G. Li, A. N. Ellingson, J. D. Mozena, P. Chatterjee, J. F. Engelhardt, R. M. Zwacka, L. W. Oberley, X. Fang, et al.
Overexpression of Human Catalase Inhibits Proliferation and Promotes Apoptosis in Vascular Smooth Muscle Cells
Circ. Res., September 17, 1999; 85(6): 524 - 533.
[Abstract] [Full Text] [PDF]


Home page
CarcinogenesisHome page
C. Lauer, A. Volkl, S. Riedl, H. D. Fahimi, and K. Beier
Impairment of peroxisomal biogenesis in human colon carcinoma
Carcinogenesis, June 1, 1999; 20(6): 985 - 989.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
Y. Sun, G. Hegamyer, H. Kim, K. Sithanandam, H. Li, R. Watts, and N. H. Colburn
Molecular Cloning of Mouse Tissue Inhibitor of Metalloproteinases-3 and Its Promoter
J. Biol. Chem., August 18, 1995; 270(33): 19312 - 19319.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
S. Dayal, T. Bottiglieri, E. Arning, N. Maeda, M. R. Malinow, C. D. Sigmund, D. D. Heistad, F. M. Faraci, and S. R. Lentz
Endothelial Dysfunction and Elevation of S-Adenosylhomocysteine in Cystathionine {beta}-Synthase-Deficient Mice
Circ. Res., June 8, 2001; 88(11): 1203 - 1209.
[Abstract] [Full Text] [PDF]



Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.