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      Degradation of interleukin 1beta by matrix metalloproteinases.

      The Journal of Biological Chemistry
      Amino Acid Sequence, Cell Line, Collagenases, metabolism, Dinoprostone, biosynthesis, Enzyme Activation, Fibroblasts, drug effects, Fibrosarcoma, Gelatinases, Glycoproteins, pharmacology, Humans, Inflammation, Interleukin-1, chemistry, Kinetics, Matrix Metalloproteinase 1, Matrix Metalloproteinase 2, Matrix Metalloproteinase 3, Matrix Metalloproteinase 9, Metalloendopeptidases, Molecular Sequence Data, Phenylmercuric Acetate, analogs & derivatives, Substrate Specificity, Sulfhydryl Reagents, Tissue Inhibitor of Metalloproteinases

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          Abstract

          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.

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