Degradation of interleukin 1beta by matrix metalloproteinases.

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 (in...

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Main Authors: Ito, A, Mukaiyama, A, Itoh, Y, Nagase, H, Thogersen, I, Enghild, J, Sasaguri, Y, Mori, Y
Format: Journal article
Language:English
Published: 1996
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author Ito, A
Mukaiyama, A
Itoh, Y
Nagase, H
Thogersen, I
Enghild, J
Sasaguri, Y
Mori, Y
author_facet Ito, A
Mukaiyama, A
Itoh, Y
Nagase, H
Thogersen, I
Enghild, J
Sasaguri, Y
Mori, Y
author_sort Ito, A
collection OXFORD
description 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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spelling oxford-uuid:40586e86-7180-48c0-b4cd-b7a6d122b3fe2022-03-26T14:37:21ZDegradation of interleukin 1beta by matrix metalloproteinases.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:40586e86-7180-48c0-b4cd-b7a6d122b3feEnglishSymplectic Elements at Oxford1996Ito, AMukaiyama, AItoh, YNagase, HThogersen, IEnghild, JSasaguri, YMori, YMatrix 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.
spellingShingle Ito, A
Mukaiyama, A
Itoh, Y
Nagase, H
Thogersen, I
Enghild, J
Sasaguri, Y
Mori, Y
Degradation of interleukin 1beta by matrix metalloproteinases.
title Degradation of interleukin 1beta by matrix metalloproteinases.
title_full Degradation of interleukin 1beta by matrix metalloproteinases.
title_fullStr Degradation of interleukin 1beta by matrix metalloproteinases.
title_full_unstemmed Degradation of interleukin 1beta by matrix metalloproteinases.
title_short Degradation of interleukin 1beta by matrix metalloproteinases.
title_sort degradation of interleukin 1beta by matrix metalloproteinases
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