Lactase–phlorizin hydrolase is exclusively expressed in the small intestine and is often used as a marker for the differentiation of enterocytes. The cis-element CE-LPH1 found in the lactase–phlorizin hydrolase promoter has previously been shown to bind an intestinal-specific nuclear factor. By electrophoretic mobility-shift assay it was shown that the factor Cdx-2 (a homoeodomain-protein related to caudal) binds to a TTTAC sequence in the CE-LPH1. Furthermore it was demonstrated that Cdx-2 is able to activate reporter gene transcription by binding to CE-LPH1. A mutation in CE-LPH1, which does not affect Cdx-2 binding, results in a higher transcriptional activity, indicating that the CE-LPH1 site contains other binding site(s) in addition to the Cdx-2-binding site.
Regulation of lactase–phlorizin hydrolase gene expression by the caudal-related homoeodomain protein Cdx-2
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Jesper T. TROELSEN, Cathy MITCHELMORE, Nikolaj SPODSBERG, Anette M. JENSEN, Ove NORÉN, Hans SJÖSTRÖM; Regulation of lactase–phlorizin hydrolase gene expression by the caudal-related homoeodomain protein Cdx-2. Biochem J 15 March 1997; 322 (3): 833–838. doi: https://doi.org/10.1042/bj3220833
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