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Extracellular: Plasma Membrane Proteases – Serine Proteases
Membrane-anchored serine proteases are a group of extracellular serine proteases tethered directly to plasma membranes, via a C-terminal glycosylphosphatidylinositol linkage (GPI-anchored), a C-terminal transmembrane domain (Type I), or an N-terminal transmembrane domain (Type II). A variety of bioc...
Autores principales: | , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7149991/ http://dx.doi.org/10.1016/B978-0-12-394447-4.10076-8 |
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author | Antalis, T.M. Buzza, M.S. |
author_facet | Antalis, T.M. Buzza, M.S. |
author_sort | Antalis, T.M. |
collection | PubMed |
description | Membrane-anchored serine proteases are a group of extracellular serine proteases tethered directly to plasma membranes, via a C-terminal glycosylphosphatidylinositol linkage (GPI-anchored), a C-terminal transmembrane domain (Type I), or an N-terminal transmembrane domain (Type II). A variety of biochemical, cellular, and in vivo studies have established that these proteases are important pericellular contributors to processes vital for the maintenance of homeostasis, including food digestion, blood pressure regulation, hearing, epithelial permeability, sperm maturation, and iron homeostasis. These enzymes are hijacked by viruses to facilitate infection and propagation, and their misregulation is associated with a wide range of diseases, including cancer malignancy. |
format | Online Article Text |
id | pubmed-7149991 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
record_format | MEDLINE/PubMed |
spelling | pubmed-71499912020-04-13 Extracellular: Plasma Membrane Proteases – Serine Proteases Antalis, T.M. Buzza, M.S. Encyclopedia of Cell Biology Article Membrane-anchored serine proteases are a group of extracellular serine proteases tethered directly to plasma membranes, via a C-terminal glycosylphosphatidylinositol linkage (GPI-anchored), a C-terminal transmembrane domain (Type I), or an N-terminal transmembrane domain (Type II). A variety of biochemical, cellular, and in vivo studies have established that these proteases are important pericellular contributors to processes vital for the maintenance of homeostasis, including food digestion, blood pressure regulation, hearing, epithelial permeability, sperm maturation, and iron homeostasis. These enzymes are hijacked by viruses to facilitate infection and propagation, and their misregulation is associated with a wide range of diseases, including cancer malignancy. 2016 2015-08-20 /pmc/articles/PMC7149991/ http://dx.doi.org/10.1016/B978-0-12-394447-4.10076-8 Text en Copyright © 2016 Elsevier Inc. All rights reserved. Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active. |
spellingShingle | Article Antalis, T.M. Buzza, M.S. Extracellular: Plasma Membrane Proteases – Serine Proteases |
title | Extracellular: Plasma Membrane Proteases – Serine Proteases |
title_full | Extracellular: Plasma Membrane Proteases – Serine Proteases |
title_fullStr | Extracellular: Plasma Membrane Proteases – Serine Proteases |
title_full_unstemmed | Extracellular: Plasma Membrane Proteases – Serine Proteases |
title_short | Extracellular: Plasma Membrane Proteases – Serine Proteases |
title_sort | extracellular: plasma membrane proteases – serine proteases |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7149991/ http://dx.doi.org/10.1016/B978-0-12-394447-4.10076-8 |
work_keys_str_mv | AT antalistm extracellularplasmamembraneproteasesserineproteases AT buzzams extracellularplasmamembraneproteasesserineproteases |