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Department of Surgery, Beth Israel Deaconess Medical Center, Harvard Medical School and Harvard Digestive Diseases Center, Boston, Massachusetts 02215
We have used sodium butyrate-treated HT-29 cells
as an in vitro model system to study the molecular mechanisms
underlying intestinal alkaline phosphatase (IAP) gene activation.
Transient transfection assays using human IAP-CAT reporter genes along
with DNase I footprinting were used to localize a critical
cis element (IF-III) corresponding to
the sequence 5'-GACTGGGCGGGGTCAAGATGGA-3'. Deletion of the
IF-III element resulted in a dramatic reduction in reporter gene
activity, and IF-III was shown to function in the context of a
heterologous (SV40) promoter in a cell type-specific manner, further
supporting its functional role in IAP transactivation. Electrophoretic
mobility shift assays revealed that IF-III binds Sp1 and Sp3, but these
factors comprise only a portion of the total nuclear binding and appear
to mediate only a small portion of its transcriptional activity. IF-III
does not correspond to any previously characterized regulatory region
from other intestine-specific genes. We have thus identified a novel,
Sp1-related cis-regulatory element in
the human IAP gene that appears to play a role in its transcriptional
activation during differentiation in vitro.
phosphatase; sodium butyrate; small intestine; transcription factor
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