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Structure and Expression of a Human Class Glutathione S-Transferase Messenger RNA¹

Department of Biochemistry, The University of Tokyo Faculty of Medicine, Hongo, Bunkyo-ku, Tokyo 113, Japan

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 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 (GST-) subunit mRNA. From the nucleotide sequence we deduced the complete amino acid sequence of the GST- subunit. It contained 209 amino acids with the relative molecular mass of M_r 23,224. Comparison of the amino acid sequences between GST- and GST-P subunits suggests that they are the corresponding enzymes in these species. GST- 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- subunit (pI 5.5) and GST-P subunit (pI 6.9). The expression of GST- 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 mode of the expression of GST- in humans is different from that of GST-P in rats.

¹ This work was supported in part by Grants-in-Aid from the Ministry of Education, Science and Culture (especially for Special Project Research, Cancer Bioscience) and from the Foundation for Promotion of Cancer Research backed by the Japan Shipbuilding Industry Foundation.

² Present address: Department of Dermatology, Jichi Medical School, Minamikawachi-machi, Kawachi-gun, Tochigi 329-04, Japan.

³ To whom requests for reprints should be addressed.

Received 5/ 4/87. Revised 7/27/87. Accepted 8/ 4/87.

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