An anticatalytic monoclonal antibody to avian plasminogen activator: its effect on behavior of RSV-transformed chick fibroblasts.

A monoclonal antibody has been raised against the serine protease, plasminogen activator (PA) produced by Rous sarcoma virus-transformed chick embryo fibroblasts (RSVCEF), and selected for its ability to inhibit the catalytic activity of PA. The high specificity and anticatalytic nature of the antibody has allowed probing of the direct role of PA in cellular behavior. Microgram quantities of monoclonal IgG inhibit the overgrowth and the morphological changes associated with RSVCEF transformation and the degradation of extracellular matrix mediated by RSVCEF, indicating a catalytic role for PA in these cellular processes. Specific cleavage of extracellular matrix proteins by immunoaffinity-purified PA in the complete absence of plasminogen demonstrates a direct catalytic involvement of PA in matrix degradation.