par Robaye, Bernard 
;Døskeland, A P;Suarez Gonzalez, Nathalie ;Døskeland, Stein O;Dumont, Jacques Emile
Référence Electrophoresis, 15, 3-4, page (503-510)
Publication Publié, 1994
;Døskeland, A P;Suarez Gonzalez, Nathalie ;Døskeland, Stein O;Dumont, Jacques Emile Référence Electrophoresis, 15, 3-4, page (503-510)
Publication Publié, 1994
Article révisé par les pairs
| Résumé : | The pattern of protein expression and phosphorylation after an apoptotic stimulus has been studied in two systems. Bovine aortic endothelial cells were induced to undergo apoptotic cell death by a combination of a cytokine (tumor necrosis factor, TNF) and inhibitors of protein synthesis, like cycloheximide. Two-dimensional (2-DE) electrophoresis of proteins from such cells revealed specific proteolysis of distinct proteins, some at an early stage of apoptosis and some at a later stage. These proteins may have antiapoptotic properties. In rat IPC-81 promyelocytic leukemia cells, cAMP induced apoptosis. 2-DE of such cells pulse-labeled with [35S]methionine revealed two "novel" protein spots (of 30 kDa and 46 kDa, respectively), induced very rapidly by a posttranscriptional mechanism. It is proposed that "dysphosphorylation" may accompany apoptosis in general, since both endothelial cells treated with TNF/cycloheximide and IPC-81 cells treated with cAMP analog or the apoptosis-inducing phosphatase inhibitors okadaic acid or calyculin A all showed altered protein phosphorylation patterns, as revealed by 2-DE electrophoresis of proteins from cells prelabeled with 32Pi. |
