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J Biol Chem, Vol. 273, Issue 41, 27026-27032, October 9, 1998
From the Institute of Experimental Dermatology, University of
Münster, von Esmarchstr. 56, D-48149 Münster, Germany
Myeloid-related proteins 8 and 14 (MRP8 and
MRP14) are two Ca2+-binding proteins of the S-100
family highly abundant in myelomonocytic cells. The expression is not
only dependent on the developmental status of the cell but also on the
inflammatory situation in the tissue. In order to identify regulatory
elements responsible for the high expression of MRP14 in myeloid cells,
reporter gene constructs have been transfected into HL-60 cells, Mono
Mac 6 cells, and L132 cells. We demonstrated that a DNA element in the
first intron (positions 153-361) enhances the transcriptional activity
of the homologous promoter and of the heterologous herpes simplex virus thymidine kinase promoter up to 37-fold. To further identify the functional site, the region between positions 153 and 192 was analyzed
functionally using the thymidine kinase promoter. The region increased
the expression in the same magnitude as the complete intron. This
enhancer is highly conserved in the human and murine MRP genes,
indicative of its involvement in the transcription of MRPs. Protein
binding to the region is demonstrated using EMSA, DNA cross-linking,
Southwestern blotting, and affinity purification. Affinity purification
confirms that four proteins bind to the enhancer element.
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