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Band 3 Erythrocyte Membrane Protein Acts as Redox Stress Sensor Leading to Its Phosphorylation by p72 Syk
Joint Authors
Mandili, Giorgia
Khadjavi, Amina
Pantaleo, Antonella
Ferru, Emanuela
Pau, Maria Carmina
Spano, Alessandra
Pippia, Proto
Turrini, Francesco
Matte, Alessandro
De Franceschi, Lucia
Source
Oxidative Medicine and Cellular Longevity
Issue
Vol. 2016, Issue 2016 (31 Dec. 2016), pp.1-11, 11 p.
Publisher
Hindawi Publishing Corporation
Publication Date
2015-12-29
Country of Publication
Egypt
No. of Pages
11
Main Subjects
Abstract EN
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.
American Psychological Association (APA)
Pantaleo, Antonella& Ferru, Emanuela& Pau, Maria Carmina& Khadjavi, Amina& Mandili, Giorgia& Matte, Alessandro…[et al.]. 2015. Band 3 Erythrocyte Membrane Protein Acts as Redox Stress Sensor Leading to Its Phosphorylation by p72 Syk. Oxidative Medicine and Cellular Longevity،Vol. 2016, no. 2016, pp.1-11.
https://search.emarefa.net/detail/BIM-1114081
Modern Language Association (MLA)
Pantaleo, Antonella…[et al.]. Band 3 Erythrocyte Membrane Protein Acts as Redox Stress Sensor Leading to Its Phosphorylation by p72 Syk. Oxidative Medicine and Cellular Longevity No. 2016 (2016), pp.1-11.
https://search.emarefa.net/detail/BIM-1114081
American Medical Association (AMA)
Pantaleo, Antonella& Ferru, Emanuela& Pau, Maria Carmina& Khadjavi, Amina& Mandili, Giorgia& Matte, Alessandro…[et al.]. Band 3 Erythrocyte Membrane Protein Acts as Redox Stress Sensor Leading to Its Phosphorylation by p72 Syk. Oxidative Medicine and Cellular Longevity. 2015. Vol. 2016, no. 2016, pp.1-11.
https://search.emarefa.net/detail/BIM-1114081
Data Type
Journal Articles
Language
English
Notes
Includes bibliographical references
Record ID
BIM-1114081