scholarly journals d ‐Galactose induced early aging in human erythrocytes: Role of band 3 protein

2021 ◽  
Author(s):  
Alessia Remigante ◽  
Sara Spinelli ◽  
Vincenzo Trichilo ◽  
Saverio Loddo ◽  
Antonio Sarikas ◽  
...  
Keyword(s):  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein ◽  
Early Aging

scholarly journals D‐Galactose‐induced accelerated aging model on human erythrocytes and role of Band 3 protein

2021 ◽  
Vol 35 (S1) ◽  
Author(s):  
Sara Spinelli ◽  
Alessia Remigante ◽  
Silvia Dossena ◽  
Michael Pusch ◽  
Angela Marino ◽  
...  
Keyword(s):  
Accelerated Aging ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein ◽  
Aging Model

Impact of acute inflammation on Band 3 protein anion exchange capability in human erythrocytes

2020 ◽  
pp. 1-7 ◽  
Author(s):  
Rossana Morabito ◽  
Alessia Remigante ◽  
Marika Cordaro ◽  
Vincenzo Trichilo ◽  
Saverio Loddo ◽  
...  
Keyword(s):  
Anion Exchange ◽  
Acute Inflammation ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein

scholarly journals Proteolysis of ankyrin and of band 3 protein in chemically induced cell fusion. Ca2+ is not mandatory for fusion

1984 ◽  
Vol 218 (2) ◽  
pp. 295-305 ◽  
Author(s):  
R D A Lang ◽  
C Wickenden ◽  
J Wynne ◽  
J A Lucy
Keyword(s):  
Membrane Proteins ◽  
Lipid Bilayers ◽  
Cysteine Proteinase ◽  
Serine Proteinase ◽  
Band 3 ◽  
Human Erythrocytes ◽  
General Mechanism ◽  
Band 3 Protein ◽  
Fusion Reactions ◽  
Chlorpromazine Hydrochloride

Human erythrocytes were fused by incubation with 0.5-2 mM-chlorpromazine hydrochloride at pH 6.8-7.6. Fusogenic preparations of chlorpromazine were cloudy suspensions of microdroplets, and below pH 6.8 chlorpromazine gave clear solutions that were inactive. Unlike control cells, the lateral mobility of the intramembranous particles of the PF-fracture face of chlorpromazine-treated cells was relatively unrestricted, since the particles were partly clustered at 37 degrees C and they exhibited extensive cold-induced clustering. Ca2+ stimulated fusion, but fusion was only very weakly inhibited by EGTA (10 mM) and by N-ethylmaleimide (50 mM); pretreatment of the cells with Tos-Lys-CH2Cl (7-amino-1-chloro-3-L-tosylamidoheptan-2-one) (7.5 mM) markedly inhibited fusion. Changes in the membrane proteins of erythrocytes fused by chlorpromazine, before and after treatment with chymotrypsin to remove band 3 protein, were investigated. The several observations made indicate that the Ca2+-insensitive component of fusion is associated with degradation of ankyrin (band 2.1 protein) to band 2.3-2.6 proteins and to smaller polypeptides by a serine proteinase that is inhibited by Tos-Lys-CH2Cl, and that the component of fusion inhibited by EGTA and N-ethylmaleimide is associated with degradation of band 3 protein to band 4.5 protein by a Ca2+-activated cysteine proteinase. Proteolysis of ankyrin appeared to be sufficient to permit the chlorpromazine-induced fusion of human erythrocytes, but fusion occurred more rapidly when band 3 protein was also degraded in the presence of Ca2+. Since other cells have structures comparable with the spectrin-actin skeleton of the erythrocyte membrane, the observations reported may be relevant to the initiation of naturally occurring fusion reactions in biomembranes. It is also suggested that, should polypeptides with fusogenic properties be produced from integral and skeletal membrane proteins by endogenous proteolysis, their formation would provide a general mechanism for the fusion of lipid bilayers in biomembrane fusion reactions.

scholarly journals The Lyn-Catalyzed Tyr Phosphorylation of the Transmembrane Band-3 Protein of Human Erythrocytes

1996 ◽  
Vol 240 (2) ◽  
pp. 394-399 ◽  
Author(s):  
Anna Maria Brunati ◽  
Luciana Bordin ◽  
Giulio Clari ◽  
Vittorio Moret
Keyword(s):  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein

scholarly journals Natural Antioxidants Beneficial Effects on Anion Exchange through Band 3 Protein in Human Erythrocytes

Antioxidants ◽  
2019 ◽  
Vol 9 (1) ◽  
pp. 25 ◽  
Author(s):  
Alessia Remigante ◽  
Rossana Morabito ◽  
Angela Marino
Keyword(s):  
Anion Exchange ◽  
Natural Antioxidants ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Band 3 Protein ◽  
Ion Distribution ◽  
Beneficial Effects ◽  
Cross Links

Band 3 protein (B3p) exchanging Cl− and HCO3− through erythrocyte membranes is responsible for acid balance, ion distribution and gas exchange, thus accounting for homeostasis of both erythrocytes and entire organisms. Moreover, since B3p cross links with the cytoskeleton and the proteins underlying the erythrocyte membrane, its function also impacts cell shape and deformability, essential to adaptation of erythrocyte size to capillaries for pulmonary circulation. As growing attention has been directed toward this protein in recent years, the present review was conceived to report the most recent knowledge regarding B3p, with specific regard to its anion exchange capability under in vitro oxidative conditions. Most importantly, the role of natural antioxidants, i.e., curcumin, melatonin and Mg2+, in preventing detrimental oxidant effects on B3p is considered.

Hypobaric hypoxia-reoxygenation diminishes band 3 protein functions in human erythrocytes

2002 ◽  
Vol 445 (3) ◽  
pp. 337-341 ◽  
Author(s):  
Gustavo González ◽  
Gloria Celedón ◽  
Mario Sandoval ◽  
Gabriela González ◽  
Verónica Ferrer ◽  
...  
Keyword(s):  
Hypobaric Hypoxia ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein ◽  
Protein Functions ◽  
Hypoxia Reoxygenation

scholarly journals Band-3 protein function in human erythrocytes: effect of oxygenation–deoxygenation

2002 ◽  
Vol 1564 (1) ◽  
pp. 214-218 ◽  
Author(s):  
Antonio Galtieri ◽  
Ester Tellone ◽  
Leonardo Romano ◽  
Francesco Misiti ◽  
Ersilia Bellocco ◽  
...  
Keyword(s):  
Protein Function ◽  
Band 3 ◽  
Human Erythrocytes ◽  
Band 3 Protein
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