Alteration of Plasma Galactose/N-acetylgalactosamine Level After Irradiation
Although glycoproteins possess a variety of functional and structural roles in intracellular and intercellular activities, the effect of ionizing radiation (IR) on glycosylation is largely unknown. To explore this effect, we established a sandwich assay in which PHA-L, a phytohaemagglutinin that agglutinates leukocytes, was used as a coating layer to capture glycoproteins containing complex oligosaccharides; the bound glycoproteins were then measured. C57BL/6 mice were exposed to 0, 3, 6, or 10 Gy, and the plasma was collected at 6, 12, 18, 24, 48, 72, or 168 h and then analyzed for galactose/N-acetylgalactosamine (Gal/GalNAc) containing proteins. We found that (1) the sandwich assay accurately measured the level of glycoproteins, (2) 6–12 h after IR, the amount of glycoproteins containing GalNAc increased, and (3) at 72 and 168 h, 10 Gy was associated with a decrease in Gal/GalNAc. These IR-induced alterations might relate to the release of glycoproteins into the blood and the damage of the proteins and genes that are related to the glycosylation process.
KeywordsGalactose/N-acetylgalactosamine Glycosylation Lectins PHA-L Radiation
This project is supported in part by U19 AI067733, RC1AI078519, RC2-AI-087580, RC1-AI081274 (NIAID/NIH), and Shands Cancer Center startup funds (University of Florida). We thank Dr. Chihray Liu and his team at UF for ensuring dosimetric accuracy and Kate Casey-Sawicki for editing this manuscript.
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