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Matrix metalloproteinases (MMPs) and interleukin 1 (IL-1) are implicated in inflammation and tissue destruction, where IL-1 is a potent stimulator of connective tissue cells to produce the extracellular matrix-degrading MMPs. Here, we report that IL-1beta, but not IL-1alpha, is degraded by MMP-1 (interstitial collagenase), MMP-2 (gelatinase A), MMP-3 (stromelysin 1), and MMP-9 (gelatinase B). This degradation was effectively blocked by tissue inhibitor of metalloproteinases (TIMP)-1. When IL-1beta was treated with MMPs it lost the ability to enhance the synthesis of prostaglandin E2 and pro-MMP-3 in human fibroblasts. The primary cleavage site of IL-1beta by MMP-2 was identified at the Glu25-Leu26 bond. These results suggest that IL-1beta stimulates connective tissue cells to produce MMPs, but activated MMPs in turn negatively regulate the activity of IL-1beta.

Original publication




Journal article


J biol chem

Publication Date





14657 - 14660


Amino Acid Sequence, Cell Line, Collagenases, Dinoprostone, Enzyme Activation, Fibroblasts, Fibrosarcoma, Gelatinases, Glycoproteins, Humans, Inflammation, Interleukin-1, Kinetics, Matrix Metalloproteinase 1, Matrix Metalloproteinase 2, Matrix Metalloproteinase 3, Matrix Metalloproteinase 9, Metalloendopeptidases, Molecular Sequence Data, Phenylmercuric Acetate, Substrate Specificity, Sulfhydryl Reagents, Tissue Inhibitor of Metalloproteinases