Evidence map›Paper›PMID 27034738›Full record

ArticleOxidative medicine and cellular longevity2016

Band 3 Erythrocyte Membrane Protein Acts as Redox Stress Sensor Leading to Its Phosphorylation by p (72) Syk.

Antonella Pantaleo, Emanuela Ferru, Maria Carmina Pau, Amina Khadjavi, Giorgia Mandili, Alessandro Mattè, Alessandra Spano, Lucia De Franceschi, Proto Pippia, Francesco Turrini

Open access · hybridAbstract read
In one paragraph

Article in Oxidative medicine and cellular longevity, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
2.3field-weighted citation impact, top 12% 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

55 citing papers in PubMed, 80 citations in OpenAlex.

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  16. APPCNS neuroscience & therapeutics · 2023
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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 at 3 institutions in 1 country.

Antonella PantaleoDepartment of Biomedical Sciences, University of Sassari, 07100 Sassari, Italy.
Emanuela FerruDepartment of Oncology, University of Turin, 10126 Turin, Italy.
Maria Carmina PauDepartment of Medicine, Section of Internal Medicine, University of Verona, 37134 Verona, Italy.
Amina KhadjaviDepartment of Oncology, University of Turin, 10126 Turin, Italy.
Giorgia MandiliDepartment of Molecular Biotechnology and Life Sciences, University of Torino, 10126 Turin, Italy.
Alessandro MattèDepartment of Medicine, Section of Internal Medicine, University of Verona, 37134 Verona, Italy.
Alessandra SpanoDepartment of Biomedical Sciences, University of Sassari, 07100 Sassari, Italy.
Lucia De FranceschiDepartment of Medicine, Section of Internal Medicine, University of Verona, 37134 Verona, Italy.
Proto PippiaDepartment of Biomedical Sciences, University of Sassari, 07100 Sassari, Italy.
Francesco TurriniDepartment of Oncology, University of Turin, 10126 Turin, Italy.
University of Turin · ITUniversity of Sassari · ITUniversity of Verona · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In erythrocytes, the regulation of the redox sensitive Tyr phosphorylation of band 3 and its functions are still partially defined. A role of band 3 oxidation in regulating its own phosphorylation has been previously suggested. The current study provides evidences to support this hypothesis: (i) in intact erythrocytes, at 2 mM concentration of GSH, band 3 oxidation, and phosphorylation, Syk translocation to the membrane and Syk phosphorylation responded to the same micromolar concentrations of oxidants showing identical temporal variations; (ii) the Cys residues located in the band 3 cytoplasmic domain are 20-fold more reactive than GSH; (iii) disulfide linked band 3 cytoplasmic domain docks Syk kinase; (iv) protein Tyr phosphatases are poorly inhibited at oxidant concentrations leading to massive band 3 oxidation and phosphorylation. We also observed that hemichromes binding to band 3 determined its irreversible oxidation and phosphorylation, progressive hemolysis, and serine hyperphosphorylation of different cytoskeleton proteins. Syk inhibitor suppressed the phosphorylation of band 3 also preventing serine phosphorylation changes and hemolysis. Our data suggest that band 3 acts as redox sensor regulating its own phosphorylation and that hemichromes leading to the protracted phosphorylation of band 3 may trigger a cascade of events finally leading to hemolysis.

Indexed as

Signal TransductionAnion Exchange Protein 1, ErythrocyteErythrocyte MembraneFemaleHumansMaleOxidation-ReductionPhosphorylationProtein Kinase InhibitorsSyk KinaseAnion Exchange Protein 1, ErythrocyteProtein Kinase InhibitorsSLC4A1 protein, humanSyk KinaseSYK protein, human

Identifiers

PMID27034738
PMCPMC4806680
OpenAlexW2208743315

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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.