Presence of gelatinase A and etalloelastase type protease at the plasma membrane of human skin fibroblasts. Influence of cytokines and growth factors on cell-associated metalloendopeptidase levels

Abstract

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 (HSFE1) was able to convert 72 kDa progelatinase A to a lower 66 kDa M.W. active enzyme. Several cytokines (IL-1 beta, IL4, IL6), interferon gamma (IFN gamma) and tumor growth factor beta (TGF-beta) were studied for their ability to modify the levels of those plasma membrane associated proteinases. Among these mediators, only IL-1 beta was found to enhance the amounts of HSF membrane-bound HSFE1 and Gelatinase A.