Laboratory for Redox Regulation


The Laboratory for Redox Regulation was established primo 2010. The research within the laboratory is focused on the functional consequences of oxidative stress and reactive oxygen species (ROS) on biological systems. The role of oxidative stress in disease became apparent in the mid 50's and it is now well recognized that a number of diseases are associated with an increased level of ROS. However, research within the last decades has shown that ROS - maintained at a normal physiological level - regulates diverse physiological processes including signaling, transcription, translation and protein folding. This type of regulation is referred to as redox regulation.

The aim of our research is to gain further insight into the mechanistic roles of ROS in biological systems in order to understand how redox homeostasis is maintained in the body. This knowledge may support the further understanding of the potential roles the ROS play in disease.

Research interests

EC-SOD: Extracellular superoxide dismutase (EC-SOD) is a tetrameric glycoprotein present in the extracellular matrix. EC-SOD is an antioxidant and responsible for the removal of superoxide radicals generated in the extracellular space and plays an important role in maintaining redox homeostasis. Hence, a natural occurring variant of the protein with compromised biological activity has been found associated with heart disease and chronic obstructive pulmonary disease (COPD).

Our research within this field is focused on how the biological activity of this protein is modulated and potentially regulated. This information is important to further understand how redox homeostasis is maintained in the extracellular space.

Reactive oxygen species and protein activity:  ROS has the capacity to introduce reversible modifications in proteins based on the oxidation/reduction of cysteine residues. This process will potentially induce structural and/or functional alterations of the protein and in turn regulate biological function. Of potential interest are proteins with un-paired cysteine residues which have the capacity to participate in redox cycling.

The activity of reactive oxygen species in intracellular compartments: Several biological systems are known to regulate the redox potential, including gluthatione (GSH/GSSG), cysteine (Cys/CySS) and a number of oxidoreductases. In concert, these elements allow for the establishment of different redox potentials in diverse intracellular compartments. This type of redox compartmentalization is likely to be a key concept in the redox regulation of protein activity, allowing for protein activity in specific compartments only.

We are interested in adding new knowledge to this field of research, which is now evolving as a field of significant importance both in basic and clinical research areas.


The laboratory has a strong profile in protein purification and characterization and use large number of standard and advanced technologies within protein chemistry. Moreover, we use a number of cell based technologies.

Mass spectrometry: The laboratory uses both MALDI- and ESI-based mass spectrometry to support the identification of proteins in simple or complex mixtures as cell homogenates. Moreover, we use this technology to characterize protein post-translational modifications including, e.g., phosphorylations and oxidations. The application of both MALDI and ESI technologies allows us to utilize a large number of protein/peptide preparations technologies to obtain the desired information.

Protein/peptide purification: We use state-off-the-art equipment to facilitate the purification and separation of both proteins and peptides. In this context we use a large number of supports and protein methodologies to facilitate the optimal resolution and separation of protein and peptides. This capacity is essential for the further characterization using mass spectrometry.

Cell biology: We use a number of cell lines to evaluate the impact of oxidative stress on cellular biology and also to support the expression of recombinant protein. Moreover, we use confocal microscopy to evaluate the localization of proteins within the cell and the potential co-localization with interaction partners.

Collaborators and centres

  • Associate professor Russell P. Bowler, National Jewish Health, CO, USA
  • Professor Poul Henning Jensen, Department of Biomedicine, AU
  • Associate professor Morten S. Nielsen, Department of Biomedicine, AU
  • Professor Henrik Birn, Department of Biomedicine, AU
  • Professor Jan J. Enghild, Department of Molecular Biology and Genetics, AU
  • Associate professor Gregers R. Andersen, Department of Molecular Biology and Genetics, AU

Research group members

  • Randi Heidemann Gottfredsen, PhD student
  • Technician Ulrike Gabriele Larsen  

Group leader

Steen Vang Petersen

Associate professor
H bldg. 1242, 451
P +4587167823
P +4560202638


Sort by: Date | Author | Title