Barnes, Jill, DVM, PhD
Assistant Professor

Ph.D.: North Carolina State University
D.V.M.: North Carolina State University
Post-doctoral: North Carolina State University

Phone: (919) 513-6372
Fax: (919) 513-6465
E-mail: ja_barnes@unity.ncsu.edu

Research Area:

Research in this laboratory is focused on investigating the role of stress proteins (heat shock proteins) in cytoprotection and carcinogenesis.

Current Research:

Heat shock proteins (Hsps) belong to the highly conserved family of stress proteins, some of which are induced by a variety of cellular stresses, environmental factors and pathological conditions. The stress response, i.e. synthesis of heat shock proteins, allows cells to adapt to changes in their environment and to survive in otherwise lethal conditions. The ability of Hsps to protect a wide variety of cells and tissues from apoptosis and necrosis is well demonstrated. However, the specific mechanisms of this protection are still under investigation. In addition, Hsps are often expressed in cancer tissues and appear to be associated with increased cell proliferation and resistance to anticancer therapies.

The present studies are aimed at using a tetracycline-regulated gene expression in human MCF-7 breast cancer cells to examine the specific effects of inducible Hsp70 on cell growth and protection against the cytotoxicity of hyperthermia and various chemical agents. Using this unique cell line/expression system, we have shown that overexpression of Hsp70 stimulates MCF-7 cell proliferation and protects against the cytotoxicity of heat and DNA damage induced by exposure to sodium arsenite and vincristine. We are currently evaluating the molecular and cellular mechanisms responsible for the effects of Hsp70 on cell growth and protection from hyperthermia. In addition, we are investigating the range and type of cytoprotection provided by Hsp70 following exposure to chemotherapeutic agents with different mechanisms of action. Future research will be aimed at investigating the roles of other members of the HSP family (Hsp25, Hsp90) in cell protection and carcinogenesis. This data will permit us to gauge drug resistance with a substantial impact on selection of the most appropriate therapies for cancer treatment

Micronucleus induction (DNA damage) following exposure to vincristine. A. Normal bi-nucleated cell, B. Bi-nucleated cell with kinetochore positive mixcronucleus C. Bi-nucleated cell with multiple micronuclei.

ß-Tubulin immunostaining of MCF-7 cells following exposure to vincristine. A. Control; B. and C. Exposed to 2 ng/ml vincristine for 24 hours.

Research Methods:

Mammalian cell culture, cDNA microarray, DNA transfections, Western blotting, Apoptosis assays, Immunofluorescence, Micronucleus assay, DNA and RNA isolations, Flow cytometry.

Selected Publications:

Barnes, J.A., Dix, D.J., Collins, B.W., Luft , C and Allen J.W. (2001) Expression of inducible HSP70 enhances the proliferation of MCF-7 breast cancer cells and protects against the cytotoxic effects of hyperthermia. Cell Stress & Chaperones (in press).

Barnes, J.A., Collins, B.W. Dix, D.J. and Allen J.W.(2001) Effect of exposure protocol and Heat Shock Protein 70 (HSP70) expression on arsenite induced genotoxicity in MCF-7 cells Environmental and Molecular Mutagenesis (in preparation).

Barnes, J.A. and Smoak, I.W. (2000) Glucose-regulated protein 78 (GRP78) is elevated in embryonic mouse heart and induced following hypoglycemic stress. Anatomy and Embryology. 202 67-74.

Barnes, J.A., Smoak, I.W. and Branch, S. (1999) Expression of glucose-regulated proteins (GRP78 and GRP94) in hearts and fore-limb buds of mouse embryos exposed to hypoglycemia in vitro. Cell Stress and Chaperones. 4(4) 250-258.

Barnes, J.A. and Smoak, I.W. (1997) Immunolocalization and heart levels of GRP94 in the mouse during post-implantation development. Anatomy and Embryology.196(4) 335-341.

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