Efforts to characterize the process of apoptosis, or programmed cell death, are probably one of the clearest examples to represent the inherent complexity of regulatory mechanisms and interactions between enzymes, signals and various growth factors in a cell. Among these mechanisms, the role played by the kinase p38aMAP object of interest is the group of the Faculty of Pharmacy of the Universidad Complutense de Madrid, coordinated by Almudena Porras. In a paper published in the online edition of Cell Signal, this team has characterized cell lines derived from cardiomyocytes and mouse embryonic fibroblasts deficient in p38aMAP normal, with the aim to detect different responses to the process of apoptosis.

It is clear from the comments, p38aMAP deficient cells are more resistant to enter apoptosis, by reducing the expression of proapoptotic proteins Bax and Fas, and enhancing the expression of a specific pattern of survival. The results also show an increased Akt activity in these cells leads to increased survival time of p38aMAP deficient cardiomyocytes. Akt is a key protein complex in the path of cell survival by inhibiting apoptotic signals, with a clear implication in cancer and other diseases. The conclusions of the study postulated a possible modulator of Akt activity mediated by the kinase negatively p38αMAP through regulating the interaction between caveolin-1 and protein phosphatase PP2A that requires a binding mechanism in the cell membrane. One more example of the different and complex levels of interaction that control cell signaling patterns determination and fate of animal cells.