A native chemical chaperone in the human eye lens.
biochemistry
cataract
chemical biology
chemical chaperone
crystallin
disulfide
eye lens
none
protein aggregation
Journal
eLife
ISSN: 2050-084X
Titre abrégé: Elife
Pays: England
ID NLM: 101579614
Informations de publication
Date de publication:
20 06 2022
20 06 2022
Historique:
received:
11
01
2022
accepted:
13
06
2022
pubmed:
21
6
2022
medline:
6
7
2022
entrez:
20
6
2022
Statut:
epublish
Résumé
Cataract is one of the most prevalent protein aggregation disorders and still the most common cause of vision loss worldwide. The metabolically quiescent core region of the human lens lacks cellular or protein turnover; it has therefore evolved remarkable mechanisms to resist light-scattering protein aggregation for a lifetime. We now report that one such mechanism involves an unusually abundant lens metabolite,
Identifiants
pubmed: 35723573
doi: 10.7554/eLife.76923
pii: 76923
pmc: PMC9246369
doi:
pii:
Substances chimiques
Molecular Chaperones
0
Protein Aggregates
0
Inositol
4L6452S749
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Subventions
Organisme : NIGMS NIH HHS
ID : R35 GM139571
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY030444
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY017370
Pays : United States
Organisme : NIGMS NIH HHS
ID : K99 GM141459
Pays : United States
Organisme : NIGMS NIH HHS
ID : F32 GM126651
Pays : United States
Informations de copyright
© 2022, Serebryany et al.
Déclaration de conflit d'intérêts
ES, SC, CW, DT, NW, AM, RK, ES No competing interests declared
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