Mammalian Neuraminidases in Immune-Mediated Diseases: Mucins and Beyond.
autoimmunity
fibrosis
infection
inflammation
post-translational modification
sialic acid
sialidase
Journal
Frontiers in immunology
ISSN: 1664-3224
Titre abrégé: Front Immunol
Pays: Switzerland
ID NLM: 101560960
Informations de publication
Date de publication:
2022
2022
Historique:
received:
24
02
2022
accepted:
21
03
2022
entrez:
28
4
2022
pubmed:
29
4
2022
medline:
30
4
2022
Statut:
epublish
Résumé
Mammalian neuraminidases (NEUs), also known as sialidases, are enzymes that cleave off the terminal neuraminic, or sialic, acid resides from the carbohydrate moieties of glycolipids and glycoproteins. A rapidly growing body of literature indicates that in addition to their metabolic functions, NEUs also regulate the activity of their glycoprotein targets. The simple post-translational modification of NEU protein targets-removal of the highly electronegative sialic acid-affects protein folding, alters protein interactions with their ligands, and exposes or covers proteolytic sites. Through such effects, NEUs regulate the downstream processes in which their glycoprotein targets participate. A major target of desialylation by NEUs are mucins (MUCs), and such post-translational modification contributes to regulation of disease processes. In this review, we focus on the regulatory roles of NEU-modified MUCs as coordinators of disease pathogenesis in fibrotic, inflammatory, infectious, and autoimmune diseases. Special attention is placed on the most abundant and best studied NEU1, and its recently discovered important target, mucin-1 (MUC1). The role of the NEU1 - MUC1 axis in disease pathogenesis is discussed, along with regulatory contributions from other MUCs and other pathophysiologically important NEU targets.
Identifiants
pubmed: 35479093
doi: 10.3389/fimmu.2022.883079
pmc: PMC9035539
doi:
Substances chimiques
Glycoproteins
0
Mucins
0
Neuraminidase
EC 3.2.1.18
N-Acetylneuraminic Acid
GZP2782OP0
Types de publication
Systematic Review
Research Support, U.S. Gov't, Non-P.H.S.
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
883079Subventions
Organisme : NIAID NIH HHS
ID : R21 AI144497
Pays : United States
Informations de copyright
Copyright © 2022 Lillehoj, Luzina and Atamas.
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.
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