Modulation of ATPase activities of human erythrocyte membranes by free fatty acids or phospholipase A2

1982 ◽  
Vol 69 (1) ◽  
pp. 65-76 ◽  
Author(s):  
Günther Schmalzing ◽  
Petra Kutschera
Keyword(s):  
Fatty Acids ◽  
Phospholipase A2 ◽  
Free Fatty Acids ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes

scholarly journals Preferential incorporation of fatty acids at the inside of human erythrocyte membranes

1974 ◽  
Vol 363 (2) ◽  
pp. 287-292 ◽  
Author(s):  
W. Renooij ◽  
L.M.G. Van Golde ◽  
R.F.A. Zwaal ◽  
B. Roelofsen ◽  
L.L.M. Van Deenen
Keyword(s):  
Fatty Acids ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Human Erythrocyte Membranes ◽  
Preferential Incorporation

scholarly journals Effects of Cholesterol on Physical Properties of Human Erythrocyte Membranes: Impact on Susceptibility to Hydrolysis by Secretory Phospholipase A2

2008 ◽  
Vol 94 (8) ◽  
pp. 3084-3093 ◽  
Author(s):  
Anne L. Heiner ◽  
Elizabeth Gibbons ◽  
Jeremy L. Fairbourn ◽  
Laurie J. Gonzalez ◽  
Chisako O. McLemore ◽  
...  
Keyword(s):  
Physical Properties ◽  
Phospholipase A2 ◽  
Human Erythrocyte ◽  
Erythrocyte Membranes ◽  
Secretory Phospholipase A2 ◽  
Secretory Phospholipase ◽  
Human Erythrocyte Membranes

scholarly journals Interaction of platelet plasma membranes with thrombin-activated platelets

Blood ◽  
1981 ◽  
Vol 57 (2) ◽  
pp. 305-312 ◽  
Author(s):  
HR Prasanna ◽  
HH Edwards ◽  
DR Phillips
Keyword(s):  
Human Erythrocyte ◽  
Plasma Membranes ◽  
Membrane Binding ◽  
Human Platelets ◽  
Platelet Membrane ◽  
Erythrocyte Membranes ◽  
Functional Sites ◽  
Activated Platelets ◽  
Platelet Membranes ◽  
Human Erythrocyte Membranes

Abstract This study described the binding of platelet plasma membranes to either control or thrombin-activated platelets. Glycoproteins in plasma membranes isolated from human platelets were labeled by oxidation with periodate followed by reduction with [3H]NaBH4. Labeled membranes were incubated with either control or thrombin-activated platelets. The amount of membranes bound was measured by separating platelets with bound membranes from solution by rapid centrifugation through 27% sucrose and determining the amount of radioactivity associated with platelets. Five- to sevenfold more membranes bound to thrombin- activated platelets than to control platelets. This enhanced binding of labeled membranes was completely inhibited by an excess of unlabeled platelet membranes. Human erythrocyte membranes had little affinity for either washed or thrombin-activated platelets and therefore did not compete for platelet-membrane binding. Binding of platelet membranes to thrombin-treated platelets was inhibited by prior incubation of the platelets with PGI2 suggesting that the enhanced binding of membranes was to activated platelets. This study demonstrates that the purified platelet membranes have functional sites that can mediate membrane binding to platelets and that quantitation of membrane binding appears to reflect the increased aggregation capability of activated platelets.

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