Effects of physical states of phospholipids on the incorporation and cytochalasin B binding activity of human erythrocyte membrane proteins in reconstituted vesicles

Biochemistry ◽  
1983 ◽  
Vol 22 (20) ◽  
pp. 4763-4769 ◽  
Author(s):  
Jong Sik Hah ◽  
S. W. Hui ◽  
Chan Y. Jung
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Cytochalasin B ◽  
Binding Activity ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

Reaction of acetaldehyde with human erythrocyte membrane proteins

FEBS Letters ◽  
1977 ◽  
Vol 75 (1-2) ◽  
pp. 115-119 ◽  
Author(s):  
Katherine C. Gaines ◽  
J.M. Salhany ◽  
D.J. Tuma ◽  
M.F. Sorrell
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

scholarly journals Erythrocyte membrane inhibitor of reactive lysis: effects of phosphatidylinositol-specific phospholipase C on the isolated and cell- associated protein

Blood ◽  
1990 ◽  
Vol 75 (1) ◽  
pp. 284-289 ◽  
Author(s):  
MH Holguin ◽  
LA Wilcox ◽  
NJ Bernshaw ◽  
WF Rosse ◽  
CJ Parker
Keyword(s):  
Membrane Proteins ◽  
Phospholipase C ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Paroxysmal Nocturnal Hemoglobinuria ◽  
Membrane Attack Complex ◽  
Human Erythrocyte Membrane ◽  
Glycosyl Phosphatidylinositol ◽  
Normal Human ◽  
Erythrocyte Membrane Proteins

Abstract The erythrocyte membrane inhibitor of reactive lysis (MIRL) is an 18-Kd protein that controls complement-mediated hemolysis by restricting the activity of the membrane attack complex. MIRL expression on the erythrocytes of paroxysmal nocturnal hemoglobinuria (PNH) is abnormally low, and the greater susceptibility of PNH erythrocytes to complement is causally related to this deficiency. Inasmuch as other proteins that are deficient in PNH are anchored to the membrane through a glycosyl phosphatidylinositol moiety, studies were undertaken to determine if MIRL shares this structural feature. Normal human erythrocytes that had been radiolabeled with 125I were incubated with phosphatidylinositol- specific phospholipase C (PIPLC), and the supernate and the solubilized membrane proteins were immunoprecipitated using anti-MIRL antiserum. The MIRL that was specifically released into the supernate had an Mr of 19 Kd, while the MIRL that remained bound to the membrane had an Mr of 18 Kd. A quantitative assay showed that approximately 10% of erythrocyte MIRL was susceptible to PIPLC; however, treatment with PIPLC had no effect on either the electrophoretic mobility or the functional activity of purified MIRL. These studies show that the effects of PIPLC on MIRL are similar to those observed for other human erythrocyte membrane proteins that are anchored by a glycosyl phosphatidylinositol moiety.

Interaction of molybdenum with human erythrocyte membrane proteins

1980 ◽  
Vol 2 (1) ◽  
pp. 57-64 ◽  
Author(s):  
Marie Kselíková ◽  
Tomáš Mařík ◽  
Bedřich Bíbr ◽  
Jaroslav Lener
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

scholarly journals Glycation of the human erythrocyte glucose transporter in vitro and its functional consequences

1990 ◽  
Vol 268 (3) ◽  
pp. 661-667 ◽  
Author(s):  
P J Bilan ◽  
A Klip
Keyword(s):  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Glucose Transporter ◽  
Cytochalasin B ◽  
Competitive Inhibitor ◽  
Human Erythrocyte Membrane ◽  
Functional Consequences ◽  
High Concentrations ◽  
Erythrocyte Membrane Proteins

Glycation of human erythrocyte membrane proteins was induced by incubation in vitro with high concentrations (80 mM or 200 mM) of D-glucose for 3 or 6 days. The extent of glycation was quantified from the covalent incorporation of 3H by reduction of the glucose glycation products with NaB3H4. For membranes incubated for 3 days with 80 mM-D-glucose, glycation in vitro of Band 4.5 (containing the glucose transporter) was equivalent to 0.11 mol of glucose/mol of glucose transporter, compared with 3H labelling in 3-day-incubated control membranes of 0.055 mol of glucose/mol of glucose transporter. In membranes incubated for 6 days with 200 mM-D-glucose, glycation increased to 0.21 mol of glucose/mol of glucose transporter, whereas the controls without glucose had 0.11 mol of glucose/mol of glucose transporter. Glycation in vitro was accompanied by a fall in the Bmax of binding of [3H]cytochalasin B (a competitive inhibitor of glucose transport), without any change in the binding affinity. The data suggest that glycated glucose transporters have decreased ability to bind cytochalasin B. It is proposed that glycation can alter glucose transporter activity.

Changes in Human Erythrocyte Membrane Proteins During Storage

Vox Sanguinis ◽  
1971 ◽  
Vol 20 (3) ◽  
pp. 239-251
Author(s):  
G.L. Moore ◽  
D.A. Cooper ◽  
R.S. Antonoff ◽  
S.L. Robinson
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins

Changes in Human Erythrocyte Membrane Proteins During Storage

Vox Sanguinis ◽  
1971 ◽  
Vol 20 (3) ◽  
pp. 239-251 ◽  
Author(s):  
G. L. Moore ◽  
D. A. Cooper ◽  
R. S. Antonoff ◽  
S. L. Robinson
Keyword(s):  
Membrane Proteins ◽  
Erythrocyte Membrane ◽  
Human Erythrocyte ◽  
Human Erythrocyte Membrane ◽  
Erythrocyte Membrane Proteins
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