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Volume 272, Number 52, Issue of December 26, 1997 pp. 32743-32749

Genomic Cloning of hGSTP1*C, an Allelic Human Pi Class Glutathione S-Transferase Gene Variant and Functional Characterization of Its Retinoic Acid Response Elements

(Received for publication, June 18, 1996, and in revised form, July 3, 1997)

From the Section of Molecular Therapeutics, Department of Experimental Pediatrics, University of Texas MD Anderson Cancer Center, Houston, Texas 77030

The complete hGSTP1*C, consisting of 7 exons and 6 introns contained in 3116 base pairs, was isolated from a cosmid genomic library of a glioblastoma multiforme cell line. Although the promoter of hGSTP1*C was identical to that of the previously reported GST-Pi gene, several of its structural features had not been previously described. These include several nucleotide transitions and transversions. Transitions of A  G at +1404 and C  T at +2294 in exons 5 and 6, respectively, changed codons Ile¹⁰⁴ to Val¹⁰⁴ and Ala¹¹³ to Val¹¹³. The gene also contained a guanine insertion at +51 in the insulin response element in intron 1 and six tandem repeats and one palindromic retinoic acid response element (RARE) consensus half-sites, A(G)GG(T)TC(G)A in intron 5. Retinoic acid (RA) treatment increased GST-Pi gene expression significantly in MGR3 cells. GST-Pi gene constructs with and without RARE deletion were used to show the RARE requirement for GST-Pi gene induction by RA. The isolation of the hGSTP1*C gene and the evidence that it contains functional RAREs should contribute to a better understanding of the molecular regulation of the GST-Pi gene in human cells.

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