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Edward J. Benz Jr., MD

Medical Oncology

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  • President and CEO Emeritus, Dana-Farber Cancer Institute
  • Richard and Susan Smith Distinguished Professor of Medicine, Professor of Pediatrics, Professor of Genetics, Harvard Medical School

Contact Information

  • Office Phone Number617-632-2015
  • Fax617-632-2161


Dr. Benz graduated from Harvard Medical School in 1973 and received his training at Brigham and Women's Hospital and the National Institutes of Health. He is president and CEO emeritus of Dana-Farber Cancer Institute, director emeritus and principal investigator of Dana-Farber/Harvard Cancer Center, and a member of the Governing Board of Dana-Farber/Children's Cancer Center. He is also a clinical hematologist and an active NIH-funded investigator.

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Board Certification:

  • Hematology
  • Internal Medicine


  • Yale University, Hematology


  • Brigham and Women's Hospital, Internal Medicine

Medical School:

  • Harvard Medical School

Recent Awards:

  • President, American Association of Cancer Institutes 2005
  • Elected Fellow, American Association for the Advancement of Science 2004
  • Member, American Academy of Arts and Sciences 2004
  • Member, Institute of Medicine 2004


The Molecular Pathology of Hemolytic Anemias

Our laboratory continues to focus on the molecular pathology and physiology of red cell development, the molecular basis of inherited hemolytic anemias, and the use of the red cell homeostatic system as a model to study gene regulation and growth control in other tissues. During the past five years, we have focused on the structure, function, gene regulation, and molecular pathology of protein 4.1. This cytoskeletal protein, originally described in the red cell, forms a ternary complex with spectrin-actin, and attaches the spectrin latticework to membranes by binding to the cytoplasmic domains of key transmembrane proteins. Defects in this protein are associated with hereditary erythrocytosis. Our laboratory has shown that many isoforms of protein 4.1 arise from a single protein 4.1R gene by tissue-specific alternative mRNA splicing pathways, a number of which we have characterized. Our group has identified at least three target sequence areas and one putative splicing factor involved in tissue-specific regulation of red cell isoforms during erythroid differentiation. Isoforms of protein 4.1R are expressed in many tissues and exhibit complex patterns of intracellular localization. We have shown that some forms associate with NuMa, a key mitotic protein, and are components of the mitotic apparatus. Other domains of protein 4.1R participate in tight junction formation by binding the proteins ZO-2. Moreover, as cells approach the state of terminal differentiation, there is a clear shift from the intranuclear localization of protein 4.1R to peripheral localization. Current studies are pursuing the hypothesis that this complex shift in localization and association is indicative of a role for protein 4.1R in signaling terminal differentiation and initiating shutdown of cell proliferation and division.


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