Induction of plasminogen activator synthesis by antibodies.

We have purified the immunoglobulins (IgG) from rabbit antisera raised against two cell lines--LLC-PK1 derived from pig kidney and from Kirsten sarcoma virus-transformed BALB/3T3--and have studied the effects of IgG on cultures of the respective target cells. The following observations were made with both cell types: (a) The addition of purified IgG produced a rapid change in morphology within 2 h. This consisted of cell rounding, agglutination, and detachment from the surface of the dish. (b) Beginning approximately 2 h after IgG addition there was a progressive rise in plasminogen activator production for 24--36 h. (c) Both the morphological change and the induction of plasminogen activator (PA) synthesis were reversible and required the continued presence of IgG for their maintenance. The increase in PA production, but not morphological change, depended on genetic transcription and translation, being inhibited by actinomycin and/or cycloheximide. (d). These effects of IgG were specific: they were not observed with preimmune or indifferent IgG and occurred only after interaction between an IgG preparation from antisera and the cells used to generate the particular antiserum. The divalent IgG fragments F(ab')2 retained fully the activities of the native IgG molecules from which they were derived.