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The Kemp Lab

Redox Systems Biology at Georgia Tech

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Aberrations in redox potential are associated with cancerous phenotypes, resulting in a resistance towards chemotherapeutic drugs. Reactive oxygen species (ROS) such as hydrogen peroxide and superoxide that are generated by ligation events across a diverse range of receptor families and redox couples provide a means of translating the presence of ROS into useful signals in the cell. Thioredoxin and glutathione-mediated post-translational modifications of proteins (thiolation and glutathiolation, respectively) have been shown to functionally alter the activity of certain proteins. However, few proteins have been investigated in depth to understand this relationship. More broadly, an in-depth quantitative analysis of how redox-related effects systemically influence the regulation of a receptor signaling pathway has never been undertaken. Challenges in quantificatifying post-translational events and discerning the effects of one redox couple from another have compounded the difficulties in understanding the role of redox-potential in cellular signaling, mandating a modeling-based approach for gaining insight into these biological processes.

The Kemp lab uses computational modeling and wet-lab experimentation to investigate how thiolation/glutathiolation of proteins influences the information flow from receptors to the nucleus. We study these effects in the context of T cell activation and cytokine response through TCR ligation. Research projects include:

  • modeling of NF-kB regulation through thioredoxin
  • development of new techniques to monitor glutathiolation of proteins
  • systemic influences of ROS on cellular phosphorylation levels