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Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies

Heparan sulfate is a crucial extracellular matrix component that organizes structural features and functional protein processes. This occurs through the formation of protein–heparan sulfate assemblies around cell surfaces, which allow for the deliberate local and temporal control of cellular signali...

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Autores principales: Heide, Fabian, Koch, Manuel, Stetefeld, Jörg
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10059586/
https://www.ncbi.nlm.nih.gov/pubmed/36986571
http://dx.doi.org/10.3390/ph16030471
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author Heide, Fabian
Koch, Manuel
Stetefeld, Jörg
author_facet Heide, Fabian
Koch, Manuel
Stetefeld, Jörg
author_sort Heide, Fabian
collection PubMed
description Heparan sulfate is a crucial extracellular matrix component that organizes structural features and functional protein processes. This occurs through the formation of protein–heparan sulfate assemblies around cell surfaces, which allow for the deliberate local and temporal control of cellular signaling. As such, heparin-mimicking drugs can directly affect these processes by competing with naturally occurring heparan sulfate and heparin chains that then disturb protein assemblies and decrease regulatory capacities. The high number of heparan-sulfate-binding proteins that are present in the extracellular matrix can cause obscure pathological effects that should be considered and examined in more detail, especially when developing novel mimetics for clinical use. The objective of this article is to investigate recent studies that present heparan-sulfate-mediated protein assemblies and the impact of heparin mimetics on the assembly and function of these protein complexes.
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spelling pubmed-100595862023-03-30 Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies Heide, Fabian Koch, Manuel Stetefeld, Jörg Pharmaceuticals (Basel) Opinion Heparan sulfate is a crucial extracellular matrix component that organizes structural features and functional protein processes. This occurs through the formation of protein–heparan sulfate assemblies around cell surfaces, which allow for the deliberate local and temporal control of cellular signaling. As such, heparin-mimicking drugs can directly affect these processes by competing with naturally occurring heparan sulfate and heparin chains that then disturb protein assemblies and decrease regulatory capacities. The high number of heparan-sulfate-binding proteins that are present in the extracellular matrix can cause obscure pathological effects that should be considered and examined in more detail, especially when developing novel mimetics for clinical use. The objective of this article is to investigate recent studies that present heparan-sulfate-mediated protein assemblies and the impact of heparin mimetics on the assembly and function of these protein complexes. MDPI 2023-03-22 /pmc/articles/PMC10059586/ /pubmed/36986571 http://dx.doi.org/10.3390/ph16030471 Text en © 2023 by the authors. https://creativecommons.org/licenses/by/4.0/Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https://creativecommons.org/licenses/by/4.0/).
spellingShingle Opinion
Heide, Fabian
Koch, Manuel
Stetefeld, Jörg
Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies
title Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies
title_full Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies
title_fullStr Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies
title_full_unstemmed Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies
title_short Heparin Mimetics and Their Impact on Extracellular Matrix Protein Assemblies
title_sort heparin mimetics and their impact on extracellular matrix protein assemblies
topic Opinion
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10059586/
https://www.ncbi.nlm.nih.gov/pubmed/36986571
http://dx.doi.org/10.3390/ph16030471
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