gamma-Glutamyltransferase in human diploid fibroblasts and other mammalian cells.
gamma-Glutamyltransferase was determined in WI-38 human diploid fibroblasts and compared to enzyme levels determined in several other mammalian cell lines including: fibroblast-like cells from human skin, tibia and foreskin; epithelial-like cells from human, bovine and monkey kidney; and transformed cells (Chinese hamster ovary, HeLa S3 and SV-40 transformed WI-38). Transformed cells had the lowest activity found followed in increasing order by fibroblasts, human and bovine epithelial cells and monkey kidney epithelial cells. The enzyme isolated from the plasma membrane of WI-38 cells, like the enzyme from kidney and brain, was found to be irreversibly inhibited by iodoacetamide, reversibly by serine-borate, and had a strong specificity for certain amino acids. The possibility exists that gamma-glutamyltransferase could be involved in transport of amino acids into cells in culture; and glutamine, used in media, is an excellent substrate for the enzyme.
D000818:Animals; D002460:Cell Line; D002462:Cell Membrane / Q000201:enzymology; D002471:Cell Transformation, Neoplastic; D004171:Diploidy; D005347:Fibroblasts; D005973:Glutamine / Q000378:metabolism; D006801:Humans; D007460:Iodoacetamide / Q000494:pharmacology; D008322:Mammals; D013379:Substrate Specificity; D005723:gamma-Glutamyltransferase / Q000037:antagonists & inhibitors / Q000378:metabolism*
D005973:Glutamine; D005723:gamma-Glutamyltransferase; D007460:Iodoacetamide