The Elastin Receptor Complex: An Emerging Therapeutic Target Against Age-Related Vascular Diseases.
aging
desialylation
elastin
extracellular matrix
neuraminidase
receptor
signaling
vascular remodeling
Journal
Frontiers in endocrinology
ISSN: 1664-2392
Titre abrégé: Front Endocrinol (Lausanne)
Pays: Switzerland
ID NLM: 101555782
Informations de publication
Date de publication:
2022
2022
Historique:
received:
15
11
2021
accepted:
20
01
2022
entrez:
28
2
2022
pubmed:
1
3
2022
medline:
1
4
2022
Statut:
epublish
Résumé
The incidence of cardiovascular diseases is increasing worldwide with the growing aging of the population. Biological aging has major influence on the vascular tree and is associated with critical changes in the morphology and function of the arterial wall together with an extensive remodeling of the vascular extracellular matrix. Elastic fibers fragmentation and release of elastin degradation products, also known as elastin-derived peptides (EDPs), are typical hallmarks of aged conduit arteries. Along with the direct consequences of elastin fragmentation on the mechanical properties of arteries, the release of EDPs has been shown to modulate the development and/or progression of diverse vascular and metabolic diseases including atherosclerosis, thrombosis, type 2 diabetes and nonalcoholic steatohepatitis. Most of the biological effects mediated by these bioactive peptides are due to a peculiar membrane receptor called elastin receptor complex (ERC). This heterotrimeric receptor contains a peripheral protein called elastin-binding protein, the protective protein/cathepsin A, and a transmembrane sialidase, the neuraminidase-1 (NEU1). In this review, after an introductive part on the consequences of aging on the vasculature and the release of EDPs, we describe the composition of the ERC, the signaling pathways triggered by this receptor, and the current pharmacological strategies targeting ERC activation. Finally, we present and discuss new regulatory functions that have emerged over the last few years for the ERC through desialylation of membrane glycoproteins by NEU1, and its potential implication in receptor transactivation.
Identifiants
pubmed: 35222273
doi: 10.3389/fendo.2022.815356
pmc: PMC8873114
doi:
Substances chimiques
Peptides
0
Receptors, Cell Surface
0
elastin-binding proteins
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
815356Informations de copyright
Copyright © 2022 Tembely, Henry, Vanalderwiert, Toussaint, Bennasroune, Blaise, Sartelet, Jaisson, Galés, Martiny, Duca, Romier-Crouzet and Maurice.
Déclaration de conflit d'intérêts
The authors declare that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. The reviewer, AP, declared a past collaboration with one of the authors, LM, to the handling editor.
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