Phone (317) 274-0115
Fax (317) 248-1411
Indiana University School of Dentistry
Department of Oral Biology
1121 W. Michigan Street, Room 243
Indianapolis, IN 46202-5186
Publications
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Gregson KS, Platt JA, Windsor LJ. Glutathione affects gingival and pulp fibroblast hydrolases after TEGDMA exposure. J. Dent. Res. 2009(89). Abs 2932. |
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Gregson KS, Windsor LJ, Platt JA. Biodegradation of a dental resin material by fibroblast conditioned media. Dent. Mater. 2009 25(11);1358-62. Gregson KS, Beiswanger AJ, Platt JA. The impact of sorption, buffering and proteins on leaching of organic and inorganic substances from dental resin core material. J. Biomed. Mater. Res. 2008 84(1);256-64. Gregson KS, O'Neill JT, Platt JA, Windsor LJ. In vitro induction of hydrolytic activity in human gingival and pulp fibroblasts by trietheylene glycol demethacrylate and monocyte chemotatic protein-1. Dent. Mater. 2008 24(11);1461-67. |
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Gregson KS, |
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Windsor LJ. Monocyte chemotatic protein increases hydrolase activity in human pulp. J. Dent. Res. 2008 (88). Abs. 2435. Gregson KS, Romito LM, Garetto LP. Students' attitudes toward integrating problem-based learning into DDS pharmacology curriculum. J. Dent. Ed. Accepted. Gregson KS, Bennett JD. "Drugs acting on the respiratory system" in Pharmacology and Therapeutics |
Research Interest
Dental resin materials are composed of methacrylates that are linked through ester bonds. They are polymerized with visible light. Small molecules leach out of the materials and can come into contact with the tissues of the oral cavity. We found that triethylene glycol demethacrylate (TEGDMA) leaches out of the resin materials. Pulp and gingival fibroblasts respond to sub-lethal concentrations of TEGDMA by secreting a hydrolase enzyme into the media. This enzyme has the ability to hydrolyze the dental resin materials. We believe that this is one of the reasons that resin materials are more unstable than dental amalgam. We are currently looking at the signal transduction pathways through which the enzyme might be activated and secreted and investigating the identity of the enzyme.
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Education
B.S., 1989: Pharmacy, Purdue University, West Lafayette
Ph.D., 2001: Medicinal Chemistry, University of Michigan, Ann Arbor


