Hydrolysis and association of leucine enkephalin to lymphomic and erythroleukaemic cell lines — III. Soluble enzymes

Abstract

The possible existence of soluble proteolytic enzymes released by cells of lymphomic (U937 and 1301) and erythroleukaemic (K562) lines was studied measuring the hydrolysis of 3H-leucine enkephalin in the presence of cell-free supernatants. Results obtained indicate that in the presence of these supernatants leu-enkephalin rapidly disappears and that enkephalin disappearance is paralleled by the formation of peptides that can be interpreted as its hydrolysis fragments. Chromatograph analyses of cell supernatants indicate the presence of three groups of proteins active in leu-enkephalin degradation: aminopeptidases, dipeptidylaminopeptidases and dipeptidylcarboxypeptidases. In all three lines soluble enzymes are represented by a sizeable number (from 13 to 25) of distinct activities. The number of enzymes identified and their considerable total activity suggest a possible role in the regulatory degradation of informational peptides, as proposed by several groups for the membrane-bound proteolytic enzymes of immunocompetent cells.