scholarly journals Glutathione-dependent protection against oxidative damage of the human red cell membrane

Blood ◽  
1984 ◽  
Vol 63 (5) ◽  
pp. 1096-1101
Author(s):  
S Fujii ◽  
GL Dale ◽  
E Beutler
Keyword(s):  
Lipid Peroxidation ◽  
Cell Membrane ◽  
Oxidative Damage ◽  
The Other ◽  
Red Cell ◽  
Artificial System ◽  
Red Cell Membrane ◽  
Dependent Inhibition ◽  
Chloroform Methanol ◽  
Human Red Cell Membrane

Glutathione (GSH) dependent protection against oxidative damage of human red cell membrane was examined. An artificial system was used in which chloroform/methanol-extracted red cell lipids, in the form of liposomes, were subjected to attack by a peroxidation system consisting of ascorbate-Fe3+. Human erythrocytes contained a nondialyzable factor, completely inactivated by heating in a boiling water bath for 3 min, which showed GSH-dependent inhibition against lipid peroxidation and was devoid of GSH peroxidase activity. On the other hand, GSH-S transferase, highly purified by affinity chromatography, had no inhibitory activity. These findings strongly indicate that the GSH- dependent protection against lipid peroxidation of human red cell membrane is mediated by one or more proteins other than GSH peroxidase and GSH-S transferase.

scholarly journals Glutathione-dependent protection against oxidative damage of the human red cell membrane

Blood ◽  
1984 ◽  
Vol 63 (5) ◽  
pp. 1096-1101 ◽  
Author(s):  
S Fujii ◽  
GL Dale ◽  
E Beutler
Keyword(s):  
Lipid Peroxidation ◽  
Cell Membrane ◽  
Oxidative Damage ◽  
The Other ◽  
Red Cell ◽  
Artificial System ◽  
Red Cell Membrane ◽  
Dependent Inhibition ◽  
Chloroform Methanol ◽  
Human Red Cell Membrane

Abstract Glutathione (GSH) dependent protection against oxidative damage of human red cell membrane was examined. An artificial system was used in which chloroform/methanol-extracted red cell lipids, in the form of liposomes, were subjected to attack by a peroxidation system consisting of ascorbate-Fe3+. Human erythrocytes contained a nondialyzable factor, completely inactivated by heating in a boiling water bath for 3 min, which showed GSH-dependent inhibition against lipid peroxidation and was devoid of GSH peroxidase activity. On the other hand, GSH-S transferase, highly purified by affinity chromatography, had no inhibitory activity. These findings strongly indicate that the GSH- dependent protection against lipid peroxidation of human red cell membrane is mediated by one or more proteins other than GSH peroxidase and GSH-S transferase.

scholarly journals Genetic variants of human red-cell membrane sialoglycoprotein β. Study of the alterations occurring in the sialoglycoprotein-β gene

1988 ◽  
Vol 250 (2) ◽  
pp. 407-414 ◽  
Author(s):  
M J Tanner ◽  
S High ◽  
P G Martin ◽  
D J Anstee ◽  
P A Judson ◽  
...  
Keyword(s):  
Genetic Variants ◽  
Southern Blotting ◽  
Protein Product ◽  
Red Cells ◽  
The Other ◽  
Red Cell ◽  
Red Cell Membrane ◽  
Initiation Of Translation ◽  
Beta Gene ◽  
Human Red Cell Membrane

We have studied the DNA of individuals who express an altered sialoglycoprotein beta on their red cells by using Southern blotting with sialoglycoprotein-beta cDNA probes. Individuals of the Leach phenotype do not express any beta (sialoglycoprotein beta) or gamma (sialoglycoprotein gamma) on their red cells, and we show that about 7 kb of DNA, including the 3′ end of the beta gene, is deleted in this DNA. Any protein product of this gene is likely to lack the membrane-associating domain of beta. We have also examined the DNA of two types of other individuals (Yus-type and Gerbich-type) who have red cells that lack beta and gamma, but contain abnormal sialoglycoproteins related to beta. These two types of DNA contain different internal deletions of about 6 kb in the beta gene. We suggest that these deletions result from the presence of two different sets of internal homology in the beta gene, and on this basis we propose structures for the abnormal Yus-type and Gerbich-type sialoglycoproteins which are consistent with the other evidence that is available. We provide evidence that beta and gamma are products of the same gene and suggest a possible mechanism for the origin of gamma based on leaky initiation of translation of beta mRNA.

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