STRUCTURE AND EXPRESSION OF A HUMAN CLASS PI-GLUTATHIONE S-TRANSFERASE MESSENGER-RNA

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  • 1 November 1987
    • journal article
    • research article
    • Vol. 47  (21) , 5626-5630
Abstract
We have used a rat glutathione-S transferase P (GST-P) complementary DNA as a probe to screen a human placenta complementary DNA library constructed in the .lambda.gt11 vector. One of the positive clones contained the complete coding region (630 base pair) and the entire 3''-noncoding region (78 base pair) of the putative human glutathione-S-transferase .pi. (GST-.pi.) subunit mRNA. From the nucleotide sequence we deduced the complete amino acid sequence of the GST-.pi. subunit. It contained 209 amino acids with the relative molecular mass of Mr 23,224. Comparison of the amino acid sequences between GST-.pi. and GST-P subunits suggests that they are the corresponding enzymes in these species. GST-.pi. and GST-P both consist of 209 amino acids and differ in only 30 amino acids (85.6% homology). The difference in amino acid composition can explain the large difference in isoelectric point between GST-.pi. subunit (pI 5.5) and GST-P subunit (pI 6.9). The expression of GST-.pi. mRNA in some normal and cancerous tissues, including some hepatoma cell lines, hepatoma, and colon carcinoma specimens was determined using complementary DNA as a probe. The results indicate that the node of the expression of GST-.pi. in humans is different from that of GST-P in rats.

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