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New links for meprin β within the protease web
Proteases are organised in interconnected networks, together forming the protease web whose disturbance can have detrimental consequences for tissue homeostasis and response to environmental insults. Membrane‐anchored sheddases are proteases that themselves can be released into the pericellular spac...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2022
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10087362/ https://www.ncbi.nlm.nih.gov/pubmed/36102354 http://dx.doi.org/10.1111/febs.16621 |
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author | Canbay, Vahap auf dem Keller, Ulrich |
author_facet | Canbay, Vahap auf dem Keller, Ulrich |
author_sort | Canbay, Vahap |
collection | PubMed |
description | Proteases are organised in interconnected networks, together forming the protease web whose disturbance can have detrimental consequences for tissue homeostasis and response to environmental insults. Membrane‐anchored sheddases are proteases that themselves can be released into the pericellular space by ectodomain shedding. Werny et al. have uncovered unexpected promiscuity in ectodomain shedding of meprin β, a metalloprotease with critical functions in inflammation and fibrosis. These findings suggest new links within complex proteolytic networks like the epidermal protease network with potential implications for skin homeostasis, inflammation and response to injury. Comment on: https://doi.org/10.1111/febs.16586 |
format | Online Article Text |
id | pubmed-10087362 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2022 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-100873622023-04-12 New links for meprin β within the protease web Canbay, Vahap auf dem Keller, Ulrich FEBS J Commentary Proteases are organised in interconnected networks, together forming the protease web whose disturbance can have detrimental consequences for tissue homeostasis and response to environmental insults. Membrane‐anchored sheddases are proteases that themselves can be released into the pericellular space by ectodomain shedding. Werny et al. have uncovered unexpected promiscuity in ectodomain shedding of meprin β, a metalloprotease with critical functions in inflammation and fibrosis. These findings suggest new links within complex proteolytic networks like the epidermal protease network with potential implications for skin homeostasis, inflammation and response to injury. Comment on: https://doi.org/10.1111/febs.16586 John Wiley and Sons Inc. 2022-09-14 2023-01 /pmc/articles/PMC10087362/ /pubmed/36102354 http://dx.doi.org/10.1111/febs.16621 Text en © 2022 The Authors. The FEBS Journal published by John Wiley & Sons Ltd on behalf of Federation of European Biochemical Societies. https://creativecommons.org/licenses/by-nc-nd/4.0/This is an open access article under the terms of the http://creativecommons.org/licenses/by-nc-nd/4.0/ (https://creativecommons.org/licenses/by-nc-nd/4.0/) License, which permits use and distribution in any medium, provided the original work is properly cited, the use is non‐commercial and no modifications or adaptations are made. |
spellingShingle | Commentary Canbay, Vahap auf dem Keller, Ulrich New links for meprin β within the protease web |
title | New links for meprin β within the protease web |
title_full | New links for meprin β within the protease web |
title_fullStr | New links for meprin β within the protease web |
title_full_unstemmed | New links for meprin β within the protease web |
title_short | New links for meprin β within the protease web |
title_sort | new links for meprin β within the protease web |
topic | Commentary |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10087362/ https://www.ncbi.nlm.nih.gov/pubmed/36102354 http://dx.doi.org/10.1111/febs.16621 |
work_keys_str_mv | AT canbayvahap newlinksformeprinbwithintheproteaseweb AT aufdemkellerulrich newlinksformeprinbwithintheproteaseweb |