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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...

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Detalles Bibliográficos
Autores principales: Canbay, Vahap, auf dem Keller, Ulrich
Formato: Online Artículo Texto
Lenguaje:English
Publicado: John Wiley and Sons Inc. 2022
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
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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
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