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J. Biol. Chem., Vol. 275, Issue 39, 30668-30676, September 29, 2000
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From the Department of Oncology, Cross Cancer Institute and
University of Alberta, 11560 University Avenue, Edmonton,
Alberta T6G 1Z2, Canada
Brain fatty acid-binding protein (B-FABP) is
expressed in the radial glial cells of the developing central nervous
system as well as in a subset of human malignant glioma cell lines.
Most of the malignant glioma lines that express B-FABP also express GFAP, an intermediate filament protein found in mature astrocytes. We
are studying the regulation of the B-FABP gene to determine the basis for its differential expression in malignant glioma lines. By
DNase I footprinting, we have identified five DNA-binding sites located
within 400 base pairs (bp) of the B-FABP transcription start site, including two nuclear factor I (NFI)-binding sites at
Regulation of Brain Fatty Acid-binding Protein Expression
by Differential Phosphorylation of Nuclear Factor I in Malignant Glioma
Cell Lines*
,
35
to 58 bp (footprint 1, fp1) and 237 to 260 bp (fp3), respectively. Competition experiments, supershift experiments with
anti-NFI antibody, and methylation interference experiments all
indicate that the factor binding to fp1 and fp3 is NFI. By site-directed mutagenesis of both NFI-binding sites, we show that the
most proximal NFI site is essential for B-FABP promoter
activity in transiently transfected malignant glioma cells. Different
band shift patterns are observed with nuclear extracts from B-FABP(+) and B-FABP() malignant glioma lines, with the latter generating complexes that migrate more slowly than those obtained with B-FABP(+) extracts. All bands are converted to a faster migrating form with potato acid phosphatase treatment, indicating that NFI is
differentially phosphorylated in B-FABP(+) and B-FABP() lines. Our
results suggest that B-FABP expression in malignant glioma lines is
determined by the extent of NFI phosphorylation which, in turn, is
controlled by a phosphatase activity specific to B-FABP(+) lines.
*
This work was supported in part by a Research Initiative
Program grant from the Alberta Cancer Board and the Alberta Cancer Foundation.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Supported in part by a studentship from the Alberta Cancer Foundation.
§
To whom correspondence should be addressed: Dept. of Oncology,
Cross Cancer Institute, 11560 University Ave., Edmonton, Alberta T6G
1Z2, Canada. Tel.: 780-432-8901; Fax: 780-432-8892; E-mail: rgodbout@gpu.srv.ualberta.ca.
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