The l-isoaspartate modification within protein fragments in the aging lens can promote protein aggregation.
Amino Acid Sequence
Chromatography, High Pressure Liquid
Crystallins
/ chemistry
Humans
Isoaspartic Acid
/ chemistry
Isomerism
Lens, Crystalline
/ metabolism
Mass Spectrometry
Peptides
/ analysis
Protein Aggregates
Protein D-Aspartate-L-Isoaspartate Methyltransferase
/ genetics
Recombinant Proteins
/ biosynthesis
alpha-Crystallin A Chain
/ chemistry
alpha-Crystallin B Chain
/ chemistry
L-isoaspartate
aging
lens
post-translational modification (PTM)
protein aggregation
protein degradation
Journal
The Journal of biological chemistry
ISSN: 1083-351X
Titre abrégé: J Biol Chem
Pays: United States
ID NLM: 2985121R
Informations de publication
Date de publication:
09 08 2019
09 08 2019
Historique:
received:
25
04
2019
revised:
05
06
2019
pubmed:
27
6
2019
medline:
17
3
2020
entrez:
27
6
2019
Statut:
ppublish
Résumé
Transparency in the lens is accomplished by the dense packing and short-range order interactions of the crystallin proteins in fiber cells lacking organelles. These features are accompanied by a lack of protein turnover, leaving lens proteins susceptible to a number of damaging modifications and aggregation. The loss of lens transparency is attributed in part to such aggregation during aging. Among the damaging post-translational modifications that accumulate in long-lived proteins, isomerization at aspartate residues has been shown to be extensive throughout the crystallins. In this study of the human lens, we localize the accumulation of l-isoaspartate within water-soluble protein extracts primarily to crystallin peptides in high-molecular weight aggregates and show with MS that these peptides are from a variety of crystallins. To investigate the consequences of aspartate isomerization, we investigated two αA crystallin peptides
Identifiants
pubmed: 31239355
pii: S0021-9258(20)30169-1
doi: 10.1074/jbc.RA119.009052
pmc: PMC6690693
pii:
doi:
Substances chimiques
Crystallins
0
Isoaspartic Acid
0
Peptides
0
Protein Aggregates
0
Recombinant Proteins
0
alpha-Crystallin A Chain
0
alpha-Crystallin B Chain
0
PCMT1 protein, human
EC 2.1.1.77
Protein D-Aspartate-L-Isoaspartate Methyltransferase
EC 2.1.1.77
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
Pagination
12203-12219Subventions
Organisme : NEI NIH HHS
ID : R01 EY008313
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY023588
Pays : United States
Organisme : NIGMS NIH HHS
ID : T32 GM007185
Pays : United States
Informations de copyright
© 2019 Warmack et al.
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