Cellular signaling via receptor for advanced glycation end products (RAGE) results in pro-inflammatory responses. RAGE-mediated inflammation has been implicated in inflammatory diseases including diabetes, atherosclerosis, Alzheimers disease. In the biochemistry part, we have identified critical structural elements that mediate RAGE oligomerization and regulate RAGE expression on the cell surface. We have also completed a preliminary study of RAGE cell surface complex via proteomics. In collaboration with scientists in the Department of Energy's Los Alamos National Lab, we have also developed split GFP tagging technology that can be broadly used to study oligomerization of other mammalian membrane proteins. The technology will be further developed to study RAGE signaling. We also collaborate with scientists in University of New South Wales, Australia, to study the molecular mechanism of RAGE thiol-disulfide exchanges on the cell surface.
| Peng, Yunqian; Kim, Ji-Min; Park, Hal-Sol et al. (2016) AGE-RAGE signal generates a specific NF-?B RelA ""barcode"" that directs collagen I expression. Sci Rep 6:18822 |
| Low, Daren; Subramaniam, Renuka; Lin, Li et al. (2015) Chitinase 3-like 1 induces survival and proliferation of intestinal epithelial cells during chronic inflammation and colitis-associated cancer by regulating S100A9. Oncotarget 6:36535-50 |
| Wei, Wen; Lampe, Leonie; Park, Sungha et al. (2012) Disulfide bonds within the C2 domain of RAGE play key roles in its dimerization and biogenesis. PLoS One 7:e50736 |
