Sulfated glycosaminoglycans inhibit transglutaminase 2 by stabilizing its closed conformation.
Journal
Scientific reports
ISSN: 2045-2322
Titre abrégé: Sci Rep
Pays: England
ID NLM: 101563288
Informations de publication
Date de publication:
03 08 2022
03 08 2022
Historique:
received:
13
04
2022
accepted:
20
07
2022
entrez:
3
8
2022
pubmed:
4
8
2022
medline:
6
8
2022
Statut:
epublish
Résumé
Transglutaminases (TGs) catalyze the covalent crosslinking of proteins via isopeptide bonds. The most prominent isoform, TG2, is associated with physiological processes such as extracellular matrix (ECM) stabilization and plays a crucial role in the pathogenesis of e.g. fibrotic diseases, cancer and celiac disease. Therefore, TG2 represents a pharmacological target of increasing relevance. The glycosaminoglycans (GAG) heparin (HE) and heparan sulfate (HS) constitute high-affinity interaction partners of TG2 in the ECM. Chemically modified GAG are promising molecules for pharmacological applications as their composition and chemical functionalization may be used to tackle the function of ECM molecular systems, which has been recently described for hyaluronan (HA) and chondroitin sulfate (CS). Herein, we investigate the recognition of GAG derivatives by TG2 using an enzyme-crosslinking activity assay in combination with in silico molecular modeling and docking techniques. The study reveals that GAG represent potent inhibitors of TG2 crosslinking activity and offers atom-detailed mechanistic insights.
Identifiants
pubmed: 35922533
doi: 10.1038/s41598-022-17113-2
pii: 10.1038/s41598-022-17113-2
pmc: PMC9349199
doi:
Substances chimiques
Glycosaminoglycans
0
A73025
268AW7000T
Heparitin Sulfate
9050-30-0
Protein Glutamine gamma Glutamyltransferase 2
EC 2.3.2.13
Transglutaminases
EC 2.3.2.13
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
13326Commentaires et corrections
Type : ErratumIn
Informations de copyright
© 2022. The Author(s).
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