Faculty & Staff Directory
Department of Biology
University of South Carolina
|Office:||PSC 623||Phone Number:||803-777-1551||Email:||email@example.com|
There are two isoforms of cyclooxygenase: COX-1 and COX-2. Although these enzymes catalyze a nearly identical reaction, their expression pattern is distinctly different. COX-1 is constitutively expressed in many tissues and is thought to play roles in tissue homeostasis. In contrast, COX-2 has a low or undetectable level of basal expression in most normal tissues and cell types. However, its expression is highly induced during infection or inflammation, suggesting that COX-2 plays a role in inflammatory responses. In addition, COX-2 expression is highly induced by various environmental insults such as UV, hypoxia, heat shock, and xenobiotics. Therefore, increased expression of COX-2 may be an indicator of cellular and environmental stresses. Consistent with this notion, aberrant COX-2 expression is frequently observed in many types of human diseases such as inflammation, cancer, cardiovascular diseases, and neurodegenerative diseases.
Our laboratory is interested in understanding the pathophysiological roles of COX-2 in human diseases such as cancer and arthritis. We have developed a COX-2 transgenic mouse model in which COX-2 expression can be achieved in any cell types by a targeted Cre recombinase activity. Using this model, we have shown that aberrant expression of COX-2 induces cell death and p53 expression, resulting in skeletal malformation. We are now in the process of developing chondrocyte-specific, inducible COX-2 transgenic mouse model to study the role of increased COX-2 expression in osteoarthritis. Additionally, we study the association of COX-2 signaling with p53 pathway using cellular and molecular tools, and knockout mouse models
Vaish V., Kim J., and Shim M. “Lentivirus-mediated Somatic Recombination and Development of a Novel Mouse Model for Sporadic Colorectal Cancer” Genes, Chromosomes and Cancer (In press) 2016
Kim J. and Shim M. “COX-2 inhibitor NS-398 suppresses doxorubicin-induced p53 accumulation through inhibition of ROS-mediated Jnk activation” Molecular Carcinogenesis (In press) 2016
Chun K. and Shim M. “EP2 Induces p38 Phosphorylation via the Activation of Src in HEK 293 Cells.” Biomol Ther. 23:539-48, 2015
Kim J. and Shim M. “Prostaglandin F2α receptor (FP) signaling regulates Bmp signaling and promotes chondrocyte differentiation.” Biochim Biophys Acta. 1853:500-12, 2015
Wang X, Chrysovergis K, Bienstock RJ, Shim M, Eling TE. 2012. The H6D variant of NAG-1/GDF15 inhibits prostate xenograft growth in vivo. Prostate.
Shim M, Foley J, Anna C, Mishina Y, Eling T. 2010. Embryonic expression of cyclooxygenase-2 causes malformations in axial skeleton. J Biol Chem. 16206-17.
Shim M., Eling T.E. 2008. Vitamin E Succinate (VES) induces NAG-1 expression in a p38 kinase dependent mechanism. Mol Cancer Ther. 961-71.
Shim M., Eling T.E. 2005. PKC-dependent regulation of NAG-1/PLAB/MIC-1 expression in LNCaP prostate carcinoma cells. J Biol Chem. 18636-18642.