Spatiotemporal changes in the human lens proteome: Critical insights into long-lived proteins.
Aging
Cataract
Lens
Long-lived protein
Mass spectrometry
Post-translational modification
Proteoform
Proteome
Journal
Progress in retinal and eye research
ISSN: 1873-1635
Titre abrégé: Prog Retin Eye Res
Pays: England
ID NLM: 9431859
Informations de publication
Date de publication:
05 2020
05 2020
Historique:
received:
05
08
2019
revised:
24
10
2019
accepted:
30
10
2019
pubmed:
11
11
2019
medline:
20
5
2021
entrez:
10
11
2019
Statut:
ppublish
Résumé
The ocular lens is a unique tissue that contains an age gradient of cells and proteins ranging from newly differentiated cells containing newly synthesized proteins to cells and proteins that are as old as the organism. Thus, the ocular lens is an excellent model for studying long-lived proteins (LLPs) and the effects of aging and post-translational modifications on protein structure and function. Given the architecture of the lens, with young fiber cells in the outer cortex and the oldest cells in the lens nucleus, spatially-resolved studies provide information on age-specific protein changes. In this review, experimental strategies and proteomic methods that have been used to examine age-related and cataract-specific changes to the human lens proteome are described. Measured spatio-temporal changes in the human lens proteome are summarized and reveal a highly consistent, time-dependent set of modifications observed in transparent human lenses. Such measurements have led to the discovery of cataract-specific modifications and the realization that many animal systems are unsuitable to study many of these modifications. Mechanisms of protein modifications such as deamidation, racemization, truncation, and protein-protein crosslinking are presented and the implications of such mechanisms for other long-lived proteins in other tissues are discussed in the context of age-related neurological diseases. A comprehensive understanding of LLP modifications will enhance our ability to develop new therapies for the delay, prevention or reversal of age-related diseases.
Identifiants
pubmed: 31704338
pii: S1350-9462(19)30089-8
doi: 10.1016/j.preteyeres.2019.100802
pmc: PMC7328127
mid: NIHMS1599473
pii:
doi:
Substances chimiques
Crystallins
0
Proteome
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
100802Subventions
Organisme : NEI NIH HHS
ID : R01 EY024258
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY013462
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY013570
Pays : United States
Organisme : NEI NIH HHS
ID : P30 EY008126
Pays : United States
Organisme : NEI NIH HHS
ID : R21 EY019728
Pays : United States
Informations de copyright
Copyright © 2019. Published by Elsevier Ltd.
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