Inhibitors of the Sialidase NEU3 as Potential Therapeutics for Fibrosis.
biomarker
desialylation
idiopathic pulmonary fibrosis
neuraminidase
pentraxin
serum amyloid P
sialylation
transforming growth factor
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
23 Dec 2022
23 Dec 2022
Historique:
received:
09
11
2022
revised:
09
12
2022
accepted:
13
12
2022
entrez:
8
1
2023
pubmed:
9
1
2023
medline:
11
1
2023
Statut:
epublish
Résumé
Fibrosing diseases are a major medical problem, and are associated with more deaths per year than cancer in the US. Sialidases are enzymes that remove the sugar sialic acid from glycoconjugates. In this review, we describe efforts to inhibit fibrosis by inhibiting sialidases, and describe the following rationale for considering sialidases to be a potential target to inhibit fibrosis. First, sialidases are upregulated in fibrotic lesions in humans and in a mouse model of pulmonary fibrosis. Second, the extracellular sialidase NEU3 appears to be both necessary and sufficient for pulmonary fibrosis in mice. Third, there exist at least three mechanistic ways in which NEU3 potentiates fibrosis, with two of them being positive feedback loops where a profibrotic cytokine upregulates NEU3, and the upregulated NEU3 then upregulates the profibrotic cytokine. Fourth, a variety of NEU3 inhibitors block pulmonary fibrosis in a mouse model. Finally, the high sialidase levels in a fibrotic lesion cause an easily observed desialylation of serum proteins, and in a mouse model, sialidase inhibitors that stop fibrosis reverse the serum protein desialylation. This then indicates that serum protein sialylation is a potential surrogate biomarker for the effect of sialidase inhibitors, which would facilitate clinical trials to test the exciting possibility that sialidase inhibitors could be used as therapeutics for fibrosis.
Identifiants
pubmed: 36613682
pii: ijms24010239
doi: 10.3390/ijms24010239
pmc: PMC9820515
pii:
doi:
Substances chimiques
Neuraminidase
EC 3.2.1.18
N-Acetylneuraminic Acid
GZP2782OP0
Cytokines
0
Glycoconjugates
0
Neu3 protein, human
EC 3.2.1.18
Neu3 protein, mouse
EC 3.2.1.18
Types de publication
Journal Article
Review
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIH HHS
ID : R01 HL132919
Pays : United States
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