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J. Biol. Chem., Vol. 265, Issue 22, 12940-12948, Aug, 1990

Human placental lactogen transcriptional enhancer. Tissue specificity and binding with specific proteins

WH Walker, SL Fitzpatrick and GF Saunders
Department of Biochemistry and Molecular Biology, University of Texas M.D. Anderson Cancer Center, Houston 77030.

Human placental lactogen (hPL) and growth hormone (hGH) are thought to be derived from a common ancestral gene and have similar nucleotide and amino acid sequences. Although the genes are similar in structure, they are expressed in different tissues. A transcriptional enhancer has been found 2.2 kilobases 3' of the hPL3 gene at the distal extreme of the hPL/hGH gene cluster. This enhancer is at least 20-fold more active in hPL-producing human choriocarcinoma JEG-3 cells than in non-hPL- producing cells. The enhancer is active when linked to either the hPL3 or SV40 promoter. We have localized the hPL enhancer to a 138-base pair (bp) region that retains tissue specificity in transient transfection assays. Gel mobility shift assays showed that the hPL enhancer interacted specifically with nuclear proteins from JEG-3 cells and placental tissue. Within the 138-bp enhancer, a 22-bp region overlapping a TEF-1 binding site was shown to be protected from DNase I digestion by placental and HeLa nuclear extracts. Placental protein(s) binding this region may be instrumental in tissue-specific activity of the hPL enhancer.
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