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Name:
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Takita Sumter
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Title:
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Associate Professor of Chemistry
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Education:
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Postdoctoral Fellowship, Pediatric Oncology, John Hopkins University School of Medicine
Ph.D., Biochemistry, University of South Carolina
B.S., Chemistry, University of South Carolina
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Office:
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314A Sims Science Building
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Phone:
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803/323-4991
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E-mail:
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sumtert@winthrop.edu
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Web:
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Area(s):
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Biochemistry, Cancer Biochemistry, Molecular Biology, Enzymology
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The Sumter group is interested in understanding the genetic properties of cancer cells with the aim of broadening the array of chemotherapeutic options that exist. Of particular interest is the High Mobility Group A1 (HMGA1) gene. Deregulation of this gene is a hallmark of most cancers and its overexpression leads to tumorigenesis in experimental models. The HMGA1 gene encodes two chromosome-binding proteins (HMGA1a and HMGA1b) which are both known to coordinate various biological processes that underpin cancer initiation and progression pathways. Inhibiting HMGA1 expression may be an effective cancer treatment approach. To effectively target pathways regulating HMGA1 expression, we are working to understand the role played by HMGA1 in cancer initiation and progression.
SC-INBRE Research
In addition to their roles in transcription, growth and proliferation, and retroviral integration, emerging evidence implicates the High Mobility Group A1 (HMGA1) proteins as important mediators in oncogenic transformation. Enforced expression of HMGA1 leads to neoplastic transformation in vitro and in vitro, potentially explaining the worsened outcomes observed in patients expressing the proteins. Although several putative target genes of HMGA1 have been identified, the exact pathways for malignant transformation by HMGA1 are not clearly understood.
We are working to elucidate these mechanisms with the following specific objectives in mind:
1. Structure-Function Studies of the Regions of HMGA1 Required for Cellular Transformation
The lab group is currently conducting a detailed and systematic structure-function study of transformation induced by HMGA1. We have obtained data that indicates that the understudied third A/T hook (AT hook III) domain of the protein contributes to the protein's oncogenic activity. We are also using genetic and biochemical methods to evaluate other regions that are required for the protein's oncogenic potential.
2. Identifying pathways that ultimately deregulate HMGA1 expression
Gene expression profiling and proteomic studies suggest that the proteins acts by 1) activating inflammatory pathways, 2) inhibiting tumor suppressor function, and 3) driving the expression of cellular oncogenes. A few genes have been identified as HMGA1 deregulators and we are working to identify additional activators.