Regulation of human erythrocyte glyceraldehyde-3-phosphate dehydrogenase by ferriprotoporphyrin IX
Articolo
Data di Pubblicazione:
2005
Citazione:
Regulation of human erythrocyte glyceraldehyde-3-phosphate dehydrogenase by ferriprotoporphyrin IX / M.F. Omodeo Salè, E. Vanzulli, S. Caielli, D. Taramelli. - In: FEBS LETTERS. - ISSN 0014-5793. - 579:22(2005), pp. 5095-5099.
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.
Tipologia IRIS:
01 - Articolo su periodico
Keywords:
glyceraldehyde 3 phosphate dehydrogenase; heme; erythrocyte; ferriprotoporphyrin IX
Elenco autori:
M.F. Omodeo Salè, E. Vanzulli, S. Caielli, D. Taramelli
Link alla scheda completa: