The focus of our research group is to understand the key protein phosphorylation steps of apoptotic cell death. We use phosphatase inhibiting algal toxins to induce apoptosis. These toxins are extremely efficient apoptosis-inducers. Proteomic tools are used to identify and analyse phosphoproteins in the apoptotic cells.

Protein Phosphorylation

Protein phosphorylation is the one most important way of intracellular signaling. A protein is phosphorylated when a phosphate group is added to it. The phosphate group can rapidly be taken off. One believes that more than 50% of all proteins can be phosphorylated. This reversible modification controls almost all cellular functions, including cell proliferation, cellular movement, cell adhesion, and apoptotic cell death. A large number of natural occurring toxins act through targeting protein phosphorylation.

Apoptotic Cell Death

Each day billions of cells in the human body kill themselves. This suicide process is called apoptosis and is fundamental for our wellbeing. Failure in the cellular apoptosis signaling pathways may lead to diseases such as cancer, AIDS and neurodegenerative disorders. Protein phosphorylation is believed to control the early phase of apoptotic cell death due to its reversible nature and widespread occurrence.

Proteomics

Proteomic research involves separation of proteins followed by identification and characterization using mass spectrometry. Tremendous achievements in proteomics have been done the last years and proteomics is believed to resolve demanding biomedical and biochemical tasks. Even though phosphorylation is the most studied and best understood type of protein modification, the analysis of phosphoproteins is still one most challenging tasks in proteomic research.