Characterization of transglutaminases in normal and malignant human leukocytes.

Using the fluorescent activity staining procedure, transglutaminases in human monocytes, granulocytes and lymphocytes have been characterized with respect to agarose gel electrophoretic mobility and thrombin dependence. A thrombin dependent transglutaminase was found in concanavalin A stimulated peripheral monocytes. The electrophoretic mobility of this zymogen and of platelet and plasma factor XIII was similar. With stimulated peripheral lymphocytes a similar pattern was observed. However, the potential transglutaminase activity in the lymphocyte factor XIII was lower than that in monocytes. Similar results were obtained when lymphocytes from chronic myeloid and chronic lymphocytic leukaemia patients were examined. Quantitatively, the transglutaminase activity in the leukaemic cells was estimated to be lower than the activity in normal cells. With respect to agarose gel electrophoretic mobility, a similar transglutaminase was found in concanavalin A stimulated human peripheral granulocytes. Although electrophoretically clearly separated from tissues transglutaminase, the granulocyte enzyme did not seem to require thrombin for activation.