ABSTRACT
Arils, juice and rinds of Punica granatum fruits and their aqueous and ethyl acetate extracts displayed good antioxidant activity.
Subject(s)
Antioxidants/chemistry , Lythraceae , Phytotherapy , Plant Extracts/chemistry , Arachidonate 5-Lipoxygenase/chemistry , Biphenyl Compounds , Fruit , Humans , Luminol/chemistry , Picrates/chemistryABSTRACT
Human erythrocytes were loaded with myo-[(3)H]-inositol in the presence or absence of cytidine trisphosphate to investigate the synthesis of membrane phosphoinositides in the intact red cell. The addition of cytidylic nucleotides to the loading mixture yielded a four-fold increase in the [(3)H]-labeling of the membranes. The [(3)H]-labeling of phosphatidylinositol, phosphatidylinositol 4-phosphate and phosphatidylinositol 4,5-bisphosphate was distinguished by two chromatographic techniques. Experiments performed on white ghosts demonstrated the presence of CDP-diacylglycerol synthase and phosphatidylinositol synthase. These results and those already reported allow to discuss a possible turnover of the inositol polar head.
Subject(s)
Erythrocytes/metabolism , Inositol/blood , Phosphatidylinositols/blood , Adult , CDP-Diacylglycerol-Inositol 3-Phosphatidyltransferase , Cytidine Triphosphate/blood , Diacylglycerol Cholinephosphotransferase/blood , Erythrocyte Membrane/metabolism , Humans , In Vitro Techniques , Membrane Proteins , Models, Biological , Transferases (Other Substituted Phosphate Groups)/bloodABSTRACT
Mammalian red blood cell alpha-spectrin is ubiquitinated in vitro and in vivo [Corsi, D., Galluzzi, L., Crinelli, R., Magnani, M. (1995) J. Biol. Chem. 270, 8928-8935]. This process shows a cell age-dependent decrease, with senescent red blood cells having approximately one third of the amount of ubiquitinated alpha-spectrin found in young cells. In-vitro ubiquitination of alpha-spectrin was dependent on the source of the red cell membranes (those from older cells are less susceptible to ubiquitination than those from younger cells), on the source of ubiquitin-conjugating enzymes (those from older cells catalyze the process at a reduced rate compared to those from younger cells) and on the ubiquitin isopeptidase activity (which decreases during red cell ageing). However, once alpha-spectrin has been extracted from the membranes of young or old red blood cells, it is susceptible to ubiquitination to a similar extent regardless of source. This suggests that it is the membrane architecture, and not spectrin itself, that is responsible for the age-dependent decline in ubiquitination. Furthermore, spectrin oligomers, tetramers and dimers are also equally susceptible to ubiquitination. As spectrin ubiquitination occurs on domains alphaIII and alphaV of alpha-spectrin, and domain alphaV contains the nucleation site for the association of the alpha- and beta-spectrin chains, alterations in ubiquitination during red cell ageing could affect the stability and deformability of the erythrocyte membrane.
Subject(s)
Cellular Senescence , Erythrocyte Membrane/metabolism , Spectrin/metabolism , Ubiquitins/metabolism , Dimerization , Endopeptidases/blood , Erythrocyte Membrane/enzymology , HumansABSTRACT
The concentration of inositol 1,4,5-trisphosphate (InsP3) in erythrocytes from volunteers has been found to modify following strenuous physical exercise. The basal value was almost regained within some 75 min after the completion of the effort. The concurrent variations of pH and blood lactate have also been evaluated. Our results represent, to our knowledge, the first evidence of in vivo induced intraerythrocyte InsP3 modification. They reinforce the idea of the participation of its precursor phosphatidylinositol 4,5-bisphosphate (PtdIns4,5-P2) in red bood cell shape regulation by contributing to the interactions between membrane and cytoskeleton components.
