Analysis of a lectin microarray identifies altered sialylation of mouse serum glycoproteins induced by whole-body radiation exposure

• Published in: Journal of radiation research Vol. 60; no. 2; pp. 189 - 196
• Main Authors: Iizuka, Daisuke, Izumi, Shunsuke, Suzuki, Fumio, Kamiya, Kenji
• Format: Journal Article
• Language: English
• Published: England Oxford University Press 01.03.2019
• Subjects: Animals; DNA microarrays; EDTA; Gene Expression Regulation; Genes; Genetic research; Glycoproteins; Glycoproteins - blood; Glycosylation; Health aspects; House mouse; Lectins; Lectins - metabolism; Liver; Liver - metabolism; Liver - radiation effects; Male; Mice; N-Acetylneuraminic Acid - metabolism; Organic acids; Protein Array Analysis; Protein Binding; Proteins; Radiation (Physics); Radiation exposure; Regular Paper; RNA, Messenger - genetics; RNA, Messenger - metabolism; Testing; Whole-Body Irradiation; Japan; glycosylation; adipsin; sialic acid; lectin array; sialyltransferase
• ISSN: 0449-3060; 1349-9157
• DOI: 10.1093/jrr/rry100

Abstract Microarrays containing 45 different lectins were analyzed to identify global changes in the glycosylation of serum glycoproteins from mice exposed to whole-body γ-radiation. The results showed that radiation exposure increased and decreased the relative amounts of α-2,3- and α-2,6-sialic acids, respectively. The expression of α-2,3- and α-2,6-sialyltransferase genes in the liver was analyzed to determine whether changes in their expression were responsible for the sialic acid changes. The increase in α-2,3-sialic acid correlated with St3gal5 upregulation after radiation exposure; however, a decrease in St6gal1 expression was not observed. Analysis of a PCR array of genes expressed in irradiated mouse livers revealed that irradiation did not alter the expression of most of the included genes. These results suggest that glycomic screening of serum glycoproteins using lectin microarrays can be a powerful tool for identifying radiation-induced changes in the post-translational addition of sugar moieties to proteins. In addition, the results indicate that altered sialylation of glycoproteins may be an initial response to acute radiation exposure.