Investigating the glycosylation of interleukin 13 receptor alpha 2 proteins expressed in cancerous and noncancerous human cell lines

BIOL 217

Christopher R. Pope and Jeffrey P. Thompson. Department of Biology, York College of Pennsylvania, Country Club Rd., York, PA 17405
Human interleukin 13 receptor alpha 2 (IL13Rα2) is a tumor-associated antigen, expressed in several cancers including malignant gliomas. The abundance of this protein on the surface of cancer cells compared to most other non-cancerous cells has allowed this receptor to be exploited therapeutically. The cytotoxic agents which target this receptor have been shown to preferentially kill cancer cells while sparing healthy ones. Our previous research of IL13Rα2 expressed in glioma cells has supported the computer predicted model of IL13Rα2 as an N-linked glycoprotein belonging to either the hybrid or complex oligosaccharide class. Since many cancer cells produce aberrant and unique glycosylation patterns compared to healthy cells, our current work investigates the possible differences in the glycosylation of IL13Rα2 expressed in both cancerous and non-cancerous cell lines. Any differences in the glycosylation of the receptor may provide an additional strategy to enhance the precision of therapies targeting IL13Rα2.
 

Frontiers in Chemical Biology
5:00 PM-7:00 PM, Wednesday, August 22, 2007 BCEC -- Exhibit Hall - B2, Poster

Division of Biological Chemistry

The 234th ACS National Meeting, Boston, MA, August 19-23, 2007