Evidence map›Paper›PMID 35163454›Full record

ArticleInternational journal of molecular sciences2022

Water-Soluble Products of Photooxidative Destruction of the Bisretinoid A2E Cause Proteins Modification in the Dark.

Alexander Dontsov, Marina Yakovleva, Natalia Trofimova, Natalia Sakina, Alexander Gulin, Arseny Aybush, Fedor Gostev, Alexander Vasin, Tatiana Feldman, Mikhail Ostrovsky

Abstract read
In one paragraph

Article in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
–field-weighted citation impact
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

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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

6 citing papers in PubMed.

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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

10 authors.

Alexander DontsovEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.
Marina YakovlevaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.
Natalia TrofimovaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.
Natalia SakinaEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.
Alexander GulinN.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, 119991 Moscow, Russia.
Arseny AybushN.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, 119991 Moscow, Russia.
Fedor GostevN.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, 119991 Moscow, Russia.ORCID 0000-0003-4532-778X
Alexander VasinN.N. Semenov Federal Research Center for Chemical Physics, Russian Academy of Sciences, 119991 Moscow, Russia.
Tatiana FeldmanEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.ORCID 0000-0003-2613-056X
Mikhail OstrovskyEmanuel Institute of Biochemical Physics, Russian Academy of Sciences, 119334 Moscow, Russia.

Funding

Ministry of Science and Higher Education of Russia 075-15-2020-795 (local identifier 13.1902.21.0027
6 · The paper itself

Abstract

Aging of the retina is accompanied by a sharp increase in the content of lipofuscin granules and bisretinoid A2E in the cells of the retinal pigment epithelium (RPE) of the human eye. It is known that A2E can have a toxic effect on RPE cells. However, the specific mechanisms of the toxic effect of A2E are poorly understood. We investigated the effect of the products of photooxidative destruction of A2E on the modification of bovine serum albumin (BSA) and hemoglobin from bovine erythrocytes. A2E was irradiated with a blue light-emitting diode (LED) source (450 nm) or full visible light (400-700 nm) of a halogen lamp, and the resulting water-soluble products of photooxidative destruction were investigated for the content of carbonyl compounds by mass spectrometry and reaction with thiobarbituric acid. It has been shown that water-soluble products formed during A2E photooxidation and containing carbonyl compounds cause modification of serum albumin and hemoglobin, measured by an increase in fluorescence intensity at 440-455 nm. The antiglycation agent aminoguanidine inhibited the process of modification of proteins. It is assumed that water-soluble carbonyl products formed as a result of A2E photodestruction led to the formation of modified proteins, activation of the inflammation process, and, as a consequence, to the progression of various senile eye pathologies.

Indexed as

AnimalsCattleGuanidinesHemoglobinsLightMass SpectrometryRetinoidsSerum Albumin, BovineThiobarbituratesWaterA2-E (N-retinylidene-N-retinylethanolamine)GuanidinesHemoglobinspimagedineRetinoidsSerum Albumin, BovineThiobarbituratesthiobarbituric acidWaterA2Eadvanced glycation end productscarbonylsfluorophoreslipofuscin granulesphotooxidationretinal pigment epithelium

Identifiers

PMID35163454
PMCPMC8836230

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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.