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- Title
Regulation of human erythrocyte glyceraldehyde-3-phosphate dehydrogenase by ferriprotoporphyrin IX
- Authors
Omodeo Salè, Fausta; Vanzulli, Elisa; Caielli, Simone; Taramelli, Donatella
- Abstract
Abstract: Erythrocyte glyceraldehyde-3-phosphate dehydrogenase (G3PD) is a glycolytic enzyme containing critical thiol groups and whose activity is reversibly inhibited by binding to the cell membrane. Here, we demonstrate that the insertion of ferriprotoporphyrin IX (FP) into the red cell membranes exerts two opposite effects on membrane bound G3PD. First, the enzyme is partially inactivated through oxidation of critical thiols. Dithiothreitol restores part of the activity, but some critical thiols are irreversibly oxidized or crosslinked to products of FP-induced lipid peroxidation. Second, G3PD binding to the membrane is modified and the enzyme is activated through displacement into the cytosol and/or release from its binding site.
- Subjects
DEHYDROGENASES; ENZYMES; BLOOD cells; CELL membranes; OXIDATION
- Publication
FEBS Letters, 2005, Vol 579, Issue 22, p5095
- ISSN
0014-5793
- Publication type
Article
- DOI
10.1016/j.febslet.2005.07.081