Secretion of matrix metalloproteinase (MMP) from human osteosarcoma cells was affected by culture conditions.
Analyzing the conditioned medium using SDS-polyacrylamide gel electrophoresis (SDS-PAGE), the cells were shown to secrete MMP-2 with an Mr of 72 KDa. When the cells were ireated with interleukin-1 (IL-1) they secreted MMP-3 with an Mr of 57 KDa. When cultured in a type I collagen-coated or a gelatin-coated dish, MMP-1 was detected in both culture mediums, although more was found the gelatin coated dish. Analysis by SDS-PAGE containing gelatin, revealed gelatinolytic activities with an Mr of 72 KDa and 66 KDa in the conditioned medium from cells in the standard dish.
When heated with IL-1, these achuihes covered a wide spectrum. Gelatinolytic activities were most detected in the type 1 collagen-coated dish. Considering the differences seen in MMPs and gelatinolytic activities, secretion of MMPs appears to be modulated by in vivo factovs.
