scholarly journals Cytosolic protein binding to band-3 protein inhibits endocytosis of isolated human erythrocyte membranes

1982 ◽  
Vol 207 (3) ◽  
pp. 595-598 ◽  
Author(s):  
K A Cordes ◽  
J M Salhany
Keyword(s):  
Membrane Protein ◽  
Integral Membrane Protein ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Band 3 Protein ◽  
High Affinity ◽  
Human Erythrocyte Membranes ◽  
Affinity Interaction ◽  
Cytoplasmic Side

Recent studies of haemoglobin binding to the cytoplasmic side of the erythrocyte membrane have shown that the predominant high-affinity interaction occurs with the major integral membrane protein known as band-3 protein and that this interaction may occur within the intact erythrocyte in a manner regulated by cell pH. We report here that haemoglobin and glyceraldehyde 3-phosphate dehydrogenase binding to band-3 protein in isolated membranes can inhibit endocytosis during vesiculation in vitro. The specificity of this effect was demonstrated by showing that myoglobin, which has an affinity for the membrane fully one to two orders of magnitude lower than that for haemoglobin, does not inhibit endocytosis.

Protoporphyrin-induced photodynamic effects on band 3 protein of human erythrocyte membranes

1981 ◽  
Vol 649 (2) ◽  
pp. 310-316 ◽  
Author(s):  
T.M.A.R. Dubbelman ◽  
A.F.P.M. De Goeij ◽  
K. Christianse ◽  
J. Van Steveninck
Keyword(s):  
Human Erythrocyte ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Band 3 Protein ◽  
Human Erythrocyte Membranes

scholarly journals Degradation of Band-3 Glycoprotein in vitro by a Protease Isolated from Human Erythrocyte Membranes

1982 ◽  
Vol 121 (2) ◽  
pp. 463-467 ◽  
Author(s):  
Anne Marianne GOLOVTCHENKO-MATSUMOTO ◽  
Isamu MATSUMOTO ◽  
Toshiaki OSAWA
Keyword(s):  
Human Erythrocyte ◽  
Band 3 ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

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.

scholarly journals Naturally occurring human anti-band 3 autoantibodies accelerate clearance of erythrocytes in guinea pigs

Blood ◽  
1995 ◽  
Vol 85 (7) ◽  
pp. 1920-1928 ◽  
Author(s):  
U Giger ◽  
B Sticher ◽  
R Naef ◽  
R Burger ◽  
HU Lutz
Keyword(s):  
Guinea Pigs ◽  
Band 3 ◽  
Complement C3 ◽  
Erythrocyte Membranes ◽  
Dependent Manner ◽  
Band 3 Protein ◽  
Naturally Occurring ◽  
Dose Dependent

A variety of naturally occurring autoantibodies (NOAs) have been found in sera of animals and humans. Although their specific homeostatic role in the clearance of altered or senescent cells has been proposed and in vitro studies support such functions, in vivo evidence has been lacking. We studied the effect of affinity-purified human anti-band 3 NOA on the survival of untreated and diamide-treated erythrocytes in normal and complement C3-deficient guinea pigs. In vitro exposure to diamide, an oxidative agent, severely reduced the erythrocyte deformability and increased the amount of high-molecular-weight forms of band 3 protein and band 3-hemoglobin adducts in erythrocyte membranes, thereby markedly shortening the survival of these cells in vivo. Human anti-band 3 NOA bound in a dose-dependent manner to erythrocytes, and binding increased with exposure to diamide. In normal guinea pigs anti-band 3 NOA significantly accelerated the clearance of erythrocytes that were mildly damaged by iodine surface labeling and of those that were further oxidized by diamide. However, the anti-band 3 effect was transient and small. In contrast, anti-band 3 NOA did not significantly alter erythrocyte survival in functionally C3-deficient guinea pigs, thereby supporting the C3b requirement for anti-band 3 NOA activity. On the other hand, a pretreatment of animals with purified human band 3 protein slowed down the clearance of erythrocytes incubated with IgG depleted of anti-band 3 NOA. These results provide the first in vivo evidence of a role for anti-band 3 NOA in the clearance of erythrocytes.

scholarly journals Characterization of glycolytic enzyme interactions with murine erythrocyte membranes in wild-type and membrane protein knockout mice

Blood ◽  
2008 ◽  
Vol 112 (9) ◽  
pp. 3900-3906 ◽  
Author(s):  
M. Estela Campanella ◽  
Haiyan Chu ◽  
Nancy J. Wandersee ◽  
Luanne L. Peters ◽  
Narla Mohandas ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Membrane Protein ◽  
Knockout Mice ◽  
Protein Band ◽  
Band 3 ◽  
Glycolytic Enzyme ◽  
Erythrocyte Membranes ◽  
Multienzyme Complexes ◽  
Human Erythrocyte Membranes ◽  
Ankyrin Protein

Previous research has shown that glycolytic enzymes (GEs) exist as multienzyme complexes on the inner surface of human erythrocyte membranes. Because GE binding sites have been mapped to sequences on the membrane protein, band 3, that are not conserved in other mammalian homologs, the question arose whether GEs can organize into complexes on other mammalian erythrocyte membranes. To address this, murine erythrocytes were stained with antibodies to glyceraldehyde-3-phosphate dehydrogenase, aldolase, phosphofructokinase, lactate dehydrogenase, and pyruvate kinase and analyzed by confocal microscopy. GEs were found to localize to the membrane in oxygenated erythrocytes but redistributed to the cytoplasm upon deoxygenation, as seen in human erythrocytes. To identify membrane proteins involved in GE assembly, erythrocytes from mice lacking each of the major erythrocyte membrane proteins were examined for GE localization. GEs from band 3 knockout mice were not membrane associated but distributed throughout the cytoplasm, regardless of erythrocyte oxygenation state. In contrast, erythrocytes from mice lacking α-spectrin, ankyrin, protein 4.2, protein 4.1, β-adducin, or dematin headpiece exhibited GEs bound to the membrane. These data suggest that oxygenation-dependent assembly of GEs on the membrane could be a general phenomenon of mammalian erythrocytes and that stability of these interactions depends primarily on band 3.

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