Native Mass Spectrometry and Surface Induced Dissociation Provide Insight into the Post-Translational Modifications of Tetrameric AQP0 Isolated from Bovine Eye Lens.
Journal
Analytical chemistry
ISSN: 1520-6882
Titre abrégé: Anal Chem
Pays: United States
ID NLM: 0370536
Informations de publication
Date de publication:
25 01 2022
25 01 2022
Historique:
pubmed:
12
1
2022
medline:
15
3
2022
entrez:
11
1
2022
Statut:
ppublish
Résumé
Aquaporin-0 (AQP0) is a tetrameric membrane protein and the most abundant membrane protein in the eye lens. Interestingly, there is little to no cellular turnover once mature lens fiber cells are formed, and hence, age-related modifications accumulate with time. While bottom-up mass spectrometry-based approaches can provide identification of post-translational modifications, they cannot provide information on how these modifications coexist in a single chain or complex. Native mass spectrometry, however, enables the transfer of the intact complex into the gas-phase allowing modifications to be identified at the tetramer level. Here, we present the use of native mass spectrometry and surface-induced dissociation to study the post-translational modifications of AQP0 isolated and purified from bovine eye lens, existing as multiple forms due to the different modification states naturally present.
Identifiants
pubmed: 35015511
doi: 10.1021/acs.analchem.1c04322
pmc: PMC9161558
mid: NIHMS1799643
doi:
Substances chimiques
Aquaporins
0
Types de publication
Journal Article
Research Support, N.I.H., Extramural
Langues
eng
Sous-ensembles de citation
IM
Pagination
1515-1519Subventions
Organisme : NIGMS NIH HHS
ID : P41 GM128577
Pays : United States
Organisme : NEI NIH HHS
ID : R01 EY013462
Pays : United States
Organisme : NIGMS NIH HHS
ID : R01 GM113658
Pays : United States
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