Erythrocyte membrane protein changes in glucose-6-phosphate dehydrogenase mutants with chronic hemolytic disease: an example of postsynthetic modification of membrane proteins.

D. W. Allen; T. P. Flynn; G. J. Johnson

Erythrocyte membrane protein changes in glucose-6-phosphate dehydrogenase mutants with chronic hemolytic disease: an example of postsynthetic modification of membrane proteins.

D. W. Allen, T. P. Flynn, G. J. Johnson

Research output: Contribution to journal › Article › peer-review

Abstract

1. G6PD mutants with CHD have decreased GSH, despite reticulocytosis, and increased membrane polypeptide aggregates. Aggregates increase logarithmically with decrease in RBC GSH. 2. These aggregates contain spectrin and can be depolymerized by disulfide reducing agents. Disulfide bonds between spectrin molecules and between the cytoskeleton and the cytoplasmic protein rigidify the red cell membrane and decrease RBC survival. 3. Direct oxidative damage of the RBC membrane, not Heinz body formation, explains the hemolytic anemia of G6PD mutants with CHD. This membrane damage may constitute a useful model system of oxidant-induced injury of other cells, and is an example of postsynthetic modification of membrane proteins by a nonmembrane gene.

Original language	English (US)
Pages (from-to)	33-43
Number of pages	11
Journal	Progress in clinical and biological research
Volume	97
State	Published - 1982
Externally published	Yes

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title = "Erythrocyte membrane protein changes in glucose-6-phosphate dehydrogenase mutants with chronic hemolytic disease: an example of postsynthetic modification of membrane proteins.",

abstract = "1. G6PD mutants with CHD have decreased GSH, despite reticulocytosis, and increased membrane polypeptide aggregates. Aggregates increase logarithmically with decrease in RBC GSH. 2. These aggregates contain spectrin and can be depolymerized by disulfide reducing agents. Disulfide bonds between spectrin molecules and between the cytoskeleton and the cytoplasmic protein rigidify the red cell membrane and decrease RBC survival. 3. Direct oxidative damage of the RBC membrane, not Heinz body formation, explains the hemolytic anemia of G6PD mutants with CHD. This membrane damage may constitute a useful model system of oxidant-induced injury of other cells, and is an example of postsynthetic modification of membrane proteins by a nonmembrane gene.",

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year = "1982",

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pages = "33--43",

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AU - Flynn, T. P.

AU - Johnson, G. J.

PY - 1982

Y1 - 1982

N2 - 1. G6PD mutants with CHD have decreased GSH, despite reticulocytosis, and increased membrane polypeptide aggregates. Aggregates increase logarithmically with decrease in RBC GSH. 2. These aggregates contain spectrin and can be depolymerized by disulfide reducing agents. Disulfide bonds between spectrin molecules and between the cytoskeleton and the cytoplasmic protein rigidify the red cell membrane and decrease RBC survival. 3. Direct oxidative damage of the RBC membrane, not Heinz body formation, explains the hemolytic anemia of G6PD mutants with CHD. This membrane damage may constitute a useful model system of oxidant-induced injury of other cells, and is an example of postsynthetic modification of membrane proteins by a nonmembrane gene.

AB - 1. G6PD mutants with CHD have decreased GSH, despite reticulocytosis, and increased membrane polypeptide aggregates. Aggregates increase logarithmically with decrease in RBC GSH. 2. These aggregates contain spectrin and can be depolymerized by disulfide reducing agents. Disulfide bonds between spectrin molecules and between the cytoskeleton and the cytoplasmic protein rigidify the red cell membrane and decrease RBC survival. 3. Direct oxidative damage of the RBC membrane, not Heinz body formation, explains the hemolytic anemia of G6PD mutants with CHD. This membrane damage may constitute a useful model system of oxidant-induced injury of other cells, and is an example of postsynthetic modification of membrane proteins by a nonmembrane gene.

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Erythrocyte membrane protein changes in glucose-6-phosphate dehydrogenase mutants with chronic hemolytic disease: an example of postsynthetic modification of membrane proteins.

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