Michael Thirman
Section of Hematology / Oncology
Associate Professor of Medicine
Director, Leukemia Biology
Referring Physician Access Line: 1-877-DOM-2730

Training

DegreeYearInstitutionArea
BA1982University of MichiganBiomedical Science
MD1986University of Michigan 
Residency1989University of MinnesotaInternal Medicine
Fellowship1994The University of ChicagoHematology/Oncology

Academic Interests

Dr. Thirman’s laboratory focuses on the role of MLL and ELL in the development of acute leukemia. In MLL-ELL associated leukemia, the normal protein-protein interactions of MLL and ELL are disrupted. Dr. Thirman’s laboratory has recently identified two novel proteins, named EAF1 and EAF2, which interact specifically with ELL. Using a bone marrow immortalization assay and a mouse leukemia model, they found that the interaction of EAF1 with ELL is essential to MLL-ELL induced leukemia. Using model systems, Dr. Thirman’s laboratory plans to analyze the pathways that mediate leukemogenesis and then to translate this knowledge into the development of novel treatment strategies.


Clinical Interests

Leukemia, lymphoma, myeloproliferative disorders, myelodysplastic syndromes


Representative Publications

  1. Lavau C., Luo R.T., Du C., and Thirman, M.J. Retrovirus mediated gene transfer of MLL-ELL transforms primary myeloid progenitors and causes acute myeloid leukemias in mice. Proceedings of the National Academy of Sciences USA, 2000;97:10984-10989.
  2. Simone, F. Polak, P.E., Luo, R.T., Kaberlein, J.J., Levitan, D.A., and Thirman, M.J. EAF1, a novel ELL associated factor that is delocalized by expression of the MLL-ELL fusion protein. Blood, 2001;98:201-209.
  3. Luo, R.T., Lavau, C., Du, C., Simone, F., Polak, P.E., Kawamata, S., and Thirman, M.J. The elongation domain of ELL is dispensable but its EAF1 interaction domain is essential for MLL-ELL induced leukemogenesis. Molecular and Cellular Biology, 2001;21:5678-5687.
  4. Simone. F., Luo, R.T., Polak, P.E., Kaberlein, J.J., and Thirman, M.J. ELL-Associated Factor 2 (EAF2), a functional homolog of EAF1 with alternative ELL binding properties. Blood, 2003;101:2355-2362.
  5. Polak, P.E., Simone, F., Kaberlein, J.J., Luo, R.T., and Thirman, M.J. ELL and EAF1 are Cajal body components that are disrupted in MLL-ELL leukemia. Molecular Biology of the Cell 2003;14:1517-1528.



More Information

For more information about Dr. Michael Thirman publications and research collaborations , please click here