PRESENCE OF GELATINASE A AND METALLOELASTASE TYPE PROTEASE AT THE PLASMA-MEMBRANE OF HUMAN SKIN FIBROBLASTS - INFLUENCE OF CYTOKINES AND GROWTH-FACTORS ON CELL-ASSOCIATED METALLOENDOPEPTIDASE LEVELS

Gelatinase A and elastase type proteinase (Homsy, et al, 1988) present at plasma membranes of human skin fibroblasts (HSF) were separated by anion exchange chromatography on a DEAE Tris acryl M column. Elastase type proteinase (HSFE(1)) was able to convert 72 kDa progelatinase A to a lower 66 kDa M.W. active enzyme. Several cytokines (IL-1 beta, IL 4, IL6), interferon gamma (IFN gamma) and tumor growth factor beta (TG F-beta) were studied for their ability to modify the levels of those p lasma membrane associated proteinases. Among these mediators, only IL- 1 beta was found to enhance the amounts of HSF membrane-bound HSFE(1) and Gelatinase A.