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...
Main Authors: | , , , , , , , |
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Format: | Journal article |
Language: | English |
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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. |
first_indexed | 2024-03-06T21:17:41Z |
format | Journal article |
id | oxford-uuid:40586e86-7180-48c0-b4cd-b7a6d122b3fe |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T21:17:41Z |
publishDate | 1996 |
record_format | dspace |
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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