The team analyses the view of cells with stress, when measuring all proteins in the mass spectrometer, a booster channel added to enhance the signal of synthesized proteins to enable their measurement.
Thus, acute changes in protein synthesis can now be tracked by state-of-the-art quantitative mass spectrometry.
The idea emerged because the team wanted to understand how specific stress signals influence protein synthesis. Since the amount of produced proteins within a brief time interval is rather small, the challenge was to record minute changes of very small percentages for each protein.
The developed analysis method now provides his team with detailed insight into the molecular events that ensure the survival of stressed cells.
The cellular response to stress plays an important role in the pathogenesis of many human diseases, including cancer and neurodegenerative disorders. An understanding of the underlying molecular processes opens the door for the development of new therapeutic strategies.
The method we developed enables precise time-resolved measurements. We can now analyze acute cellular stress responses, i.e, those taking place within minutes. Also, our method requires little material and is a cost-efficient researcher explains.
This helps us to quantify thousands of proteins in defined periods after specific stress treatment.
Due to the small amount of material required, measurements can also be carried out in patient tissue samples, facilitating collaborations with clinicians.
The young molecular biologist demonstrated for the first time that two of the most important cellular signaling pathways, which triggered by completely different stress stimuli, results in the same effects on protein synthesis. This discovery is a breakthrough in the field.