Glutathione S-Transferase in Human Hepatocellular Carcinoma
β Scribed by Morris Sherman; John A. H. Campbell; Sally A. Titmuss; Michael C. Kew; Ralph E. Kirsch
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 786 KB
- Volume
- 3
- Category
- Article
- ISSN
- 0270-9139
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β¦ Synopsis
Qualitative and quantitative changes in glutathione S-transferase (GSH-T) were studied in human hepatocellular carcinoma. GSH-T specific activity (mumoles per min per mg protein) was variably reduced in hepatocellular carcinoma. Similar changes were seen in "cationic" GSH-T (ligandin) concentration determined by radioimmunoassay. Immunohistochemical studies with antihuman liver ligandin suggest that positive staining was more frequently found in well-differentiated tumors. The relative activities of "cationic," "neutral," and "anionic" transferases (pI greater than 7.5) activity ranged from virtually absent to near normal values. "Neutral" (pI 6 to 6.5) and "anionic" (pI less than 5.4) species were present more often in tumors than in normal liver. In two cases, normal liver tissue and tumor were obtained from the same patient. In one, only quantitative differences were present, while in the other "cationic" and "neutral" GSH-Ts were present in the normal liver tissue while both "cationic" and "anionic" species were found in the tumor. Our studies indicate that qualitative as well as quantitative changes of GSH-T occur in human hepatocellular carcinoma.
π SIMILAR VOLUMES
Glutathione S-transferase (GST) was investigated with benzo(a)pyrene-4,5-oxide (BPO) as substrate in tissue specimens from 26 fetal and 27 adult livers and 27 placentas. The average (\_ SEM) of GST activity in the cytosol was 1.80\_ 0.18 (fetal liver), 3.05 \_\_\_ 0.30 (adult liver) and 1.18 + 0.07