Evidence map›Paper›PMID 26574799›Full record

ArticleInvestigative ophthalmology & visual science2015

MALDI Imaging Mass Spectrometry Spatially Maps Age-Related Deamidation and Truncation of Human Lens Aquaporin-0.

Jamie L Wenke, Kristie L Rose, Jeffrey M Spraggins, Kevin L Schey

Open access · hybridAbstract read
In one paragraph

Article in Investigative ophthalmology & visual science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.2field-weighted citation impact, top 13% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

29 citing papers in PubMed, 44 citations in OpenAlex.

  1. CatExperimental eye research · 2026
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Jamie L Wenke
Kristie L Rose
Jeffrey M Spraggins
Kevin L Schey
Vanderbilt University · US

Funding

Research Resource for Human Organs and Tissues (U42)U42OD011158 · OD · NATIONAL DISEASE RESEARCH INTERCHANGE · PI BELL, THOMAS J · 2012 to 2025
$25.0M
Shop Module CoreP30EY008126 · NEI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI Kevin L Schey · 1989 to 2026
$19.6M
Training (pp 214-245)P41GM103391 · NIGMS · VANDERBILT UNIVERSITY · PI REYZER, MICHELLE L · 2012 to 2020
$17.7M
THE ROLE OF LENS MIP IN AGING AND CATARACTOGENESISR01EY013462 · NEI · VANDERBILT UNIVERSITY · PI Kevin L Schey · 2001 to 2026
$8.2M
Training in Vision ResearchT32EY007135 · NEI · VANDERBILT UNIVERSITY · PI GEOFFREY F WOODMAN · 1994 to 2026
$5.8M
15 Tesla Bruker SolariX FT-ICR mass spectrometerS10OD012359 · OD · VANDERBILT UNIVERSITY · PI CAPRIOLI, RICHARD M · 2012 to 2012
$1.6M
LTQ Orbitrap XL ETD Hybrid FT High Resolution Mass SpectrometerS10RR027714 · NCRR · VANDERBILT UNIVERSITY · PI HACHEY, DAVID L · 2010 to 2010
$479k
NCRR NIH HHS S10 RR027714NCRR NIH HHS S10RR027714NEI NIH HHS EY-13462NEI NIH HHS P30 EY008126NEI NIH HHS P30-EY08126NEI NIH HHS R01 EY013462NEI NIH HHS T32 EY007135NEI NIH HHS T32-EY07135NIGMS NIH HHS 5P41-GM103391-05NIGMS NIH HHS P41 GM103391NIH HHS 1S10OD012359-01NIH HHS 3U42OD011158NIH HHS S10 OD012359NIH HHS U42 OD011158
6 · The paper itself

Abstract

purposeTo spatially map human lens Aquaporin-0 (AQP0) protein modifications, including lipidation, truncation, and deamidation, from birth through middle age using matrix-assisted laser desorption ionization (MALDI) imaging mass spectrometry (IMS).

methodsHuman lens sections were water-washed to facilitate detection of membrane protein AQP0. We acquired MALDI images from eight human lenses ranging in age from 2 months to 63 years. In situ tryptic digestion was used to generate peptides of AQP0 and peptide images were acquired on a 15T Fourier transform ion cyclotron resonance (FTICR) mass spectrometer. Peptide extracts were analyzed by liquid chromatography-tandem mass spectrometry (LC-MS/MS) and database searched to identify peptides observed in MALDI imaging experiments.

resultsUnmodified, truncated, and fatty acid-acylated forms of AQP0 were detected in protein imaging experiments. Full-length AQP0 was fatty acid acylated in the core and cortex of young (2- and 4-month) lenses. Acylated and unmodified AQP0 were C-terminally truncated in older lens cores. Deamidated tryptic peptides (+0.9847 Da) were mass resolved from unmodified peptides by FTICR MS. Peptide images revealed differential localization of un-, singly-, and doubly-deamidated AQP0 C-terminal peptide (239-263). Deamidation was present at 4 months and increases with age. Liquid chromatography-MS/MS results indicated N246 undergoes deamidation more rapidly than N259.

conclusionsResults indicated AQP0 fatty acid acylation and deamidation occur during early development. Progressive age-related AQP0 processing, including deamidation and truncation, was mapped in human lenses as a function of age. The localization of these modified AQP0 forms suggests where AQP0 functions may change throughout lens development and aging.

Indexed as

AdultAgingAquaporinsCataractEye ProteinsFemaleFourier AnalysisHumansLens, CrystallineMaleMiddle AgedProtein Processing, Post-TranslationalSpectrometry, Mass, Matrix-Assisted Laser Desorption-IonizationTandem Mass SpectrometryYoung Adultaquaporin 0AquaporinsEye Proteins

Identifiers

PMID26574799
PMCPMC4675204
OpenAlexW2472270761

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.