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Glutathione S‐Transferase in Human Hepatocellular Carcinoma
Author(s) -
Sherman Morris,
Campbell John A. H.,
Titmuss Sally A.,
Kew Michael C.,
Kirsch Ralph E.
Publication year - 2007
Publication title -
hepatology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.488
H-Index - 361
eISSN - 1527-3350
pISSN - 0270-9139
DOI - 10.1002/hep.1840030206
Subject(s) - hepatocellular carcinoma , glutathione s transferase , carcinoma , glutathione transferase , transferase , cancer research , glutathione , medicine , chemistry , oncology , biochemistry , enzyme
Qualitative and quantitative changes in glutathione S‐transferase (GSH‐T) were studied in human hepatocellular carcinoma. GSH‐T specific activity (/imoles 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 were estimated after separation by isoelectric focusing. Tumor “cationic” transferase (pI ± 7.5) activity ranged from virtually absent to near normal values. “Neutral” (pI 6 to 6.5) and “anionic” (pI < 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.