Skip Navigation

This Article
Right arrow Print PDF (970K)
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 arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Frégeau, C. J.
Right arrow Articles by Bleackley, R.C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Frégeau, C. J.
Right arrow Articles by Bleackley, R.C.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, 1992, Vol. 20, No. 12 3113-3119
© 1992

MOLECULAR BIOLOGY

Two cytotoxic cell proteinase genes are differentially sensitive to sodium butyrate

Chantal J. Frégeau, Cheryl D. Helgason and R.Chris Bleackley*

Department of Biochemistry, University of Alberta Edmonton, Alberta, Canada

* To whom correspondence should be addressed

Received February 28, 1992. Revised April 30, 1992. Accepted April 30, 1992.

The 5'-flanklng regions of two cytotoxic cell protease genes, CCP1 and 2, are sufficient to confer cytotoxic T lymphocyte-specific expression when fused to a reporter gene. The two regulatory regions are, however, differentially sensitive to treatment of the recipient cell, MTL 2.8.2, with sodium butyrate. With CCP1 a six-fold increase in cat expression was observed, whereas CCP2 was insensitive to the butyrate treatment. One major butyrate-sensitive regions was defined in the CCP1 5'-flanking sequence between –243 to –112 and another less effective one between –682 to –427. These fragments of DNA were also able to confer responsiveness to butyrate when ligated to a heterologous fos promoter. These sequences within the 5' flank of CCP1 share homotogy with other elements that have been defined as butyrate-responsive. We believe that our results argue against a pleiotropic affect of butyrate such as histone acetylation. More likely sodium butyrate is mediating a specific stimulation of transcription through modification of the activities of selected transcriptional regulatory proteins that in turn affect their interactions with proteins bound to the promoter.


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. Leukoc. Biol.Home page
S. K. Gupta, K. Pillarisetti, and N. Aiyar
CXCR4 undergoes complex lineage and inducing agent-dependent dissociation of expression and functional responsiveness to SDF-1{alpha} during myeloid differentiation
J. Leukoc. Biol., September 1, 2001; 70(3): 431 - 438.
[Abstract] [Full Text] [PDF]

Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
K. Ranganna and F. M. Yatsu
Inhibition of Platelet-Derived Growth Factor BB–Induced Expression of Glyceraldehyde- 3-Phosphate Dehydrogenase by Sodium Butyrate in Rat Vascular Smooth Muscle Cells
Arterioscler. Thromb. Vasc. Biol., December 1, 1997; 17(12): 3420 - 3427.
[Abstract] [Full Text]

Home page
 Arterioscler. Thromb. Vasc. Bio.Home page
K. Ranganna, T. Joshi, and F. M. Yatsu
Sodium Butyrate Inhibits Platelet-Derived Growth Factor–Induced Proliferation of Vascular Smooth Muscle Cells
Arterioscler. Thromb. Vasc. Biol., December 1, 1995; 15(12): 2273 - 2283.
[Abstract] [Full Text]


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.