Heparan sulfates and heparan sulfate binding proteins in sepsis.
HMGB1 (high mobility group box 1)
heparan sulfate
heparan sulfate binding proteins
heparin
histones
Journal
Frontiers in molecular biosciences
ISSN: 2296-889X
Titre abrégé: Front Mol Biosci
Pays: Switzerland
ID NLM: 101653173
Informations de publication
Date de publication:
2023
2023
Historique:
received:
17
01
2023
accepted:
31
01
2023
entrez:
3
3
2023
pubmed:
4
3
2023
medline:
4
3
2023
Statut:
epublish
Résumé
Heparan sulfates (HSs) are the main components in the glycocalyx which covers endothelial cells and modulates vascular homeostasis through interactions with multiple Heparan sulfate binding proteins (HSBPs). During sepsis, heparanase increases and induces HS shedding. The process causes glycocalyx degradation, exacerbating inflammation and coagulation in sepsis. The circulating heparan sulfate fragments may serve as a host defense system by neutralizing dysregulated Heparan sulfate binding proteins or pro-inflammatory molecules in certain circumstances. Understanding heparan sulfates and heparan sulfate binding proteins in health and sepsis is critical to decipher the dysregulated host response in sepsis and advance drug development. In this review, we will overview the current understanding of HS in glycocalyx under septic condition and the dysfunctional heparan sulfate binding proteins as potential drug targets, particularly, high mobility group box 1 (HMGB1) and histones. Moreover, several drug candidates based on heparan sulfates or related to heparan sulfates, such as heparanase inhibitors or heparin-binding protein (HBP), will be discussed regarding their recent advances. By applying chemical or chemoenzymatic approaches, the structure-function relationship between heparan sulfates and heparan sulfate binding proteins is recently revealed with structurally defined heparan sulfates. Such homogenous heparan sulfates may further facilitate the investigation of the role of heparan sulfates in sepsis and the development of carbohydrate-based therapy.
Identifiants
pubmed: 36865384
doi: 10.3389/fmolb.2023.1146685
pii: 1146685
pmc: PMC9971734
doi:
Types de publication
Journal Article
Review
Langues
eng
Pagination
1146685Subventions
Organisme : NIGMS NIH HHS
ID : R43 GM144019
Pays : United States
Informations de copyright
Copyright © 2023 Liao, Liu and Arnold.
Déclaration de conflit d'intérêts
JL is a founder and chief scientific officer for Glycan Therapeutics. KA is a principal scientist at Glycan Therapeutics. The JL lab at UNC has received a gift from Glycan Therapeutics to support research in glycoscience. Y-EL declare no competing interests.
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