Glutathione S-transferase in human hepatocellular carcinoma

• Published in: Hepatology (Baltimore, Md.) Vol. 3; no. 2; p. 170
• Main Authors: Sherman, M, Campbell, J A, Titmuss, S A, Kew, M C, Kirsch, R E
• Format: Journal Article
• Language: English
• Published: United States 01.03.1983
• Subjects: Biopsy; Carcinoma, Hepatocellular - enzymology; Cytosol - enzymology; Dinitrochlorobenzene - metabolism; Glutathione Transferase - isolation & purification; Histocytochemistry; Humans; Hydrogen-Ion Concentration; Isoelectric Focusing; Liver Neoplasms - enzymology; Staining and Labeling
• ISSN: 0270-9139
• DOI: 10.1002/hep.1840030206

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.