Lectin-based protein microarray analysis of differences in serum alpha-2-macroglobulin glycosylation between patients with colorectal cancer and persons without cancer
| Autor: | Miloš Šunderić, Dragana Robajac, Jaroslav Katrlík, Peter Gemeiner, Alena Šedivá, Goran Miljuš, Olgica Nedić |
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| Rok vydání: | 2015 |
| Předmět: |
0301 basic medicine
Glycosylation Antibody microarray Immunoprecipitation Biomedical Engineering Mannose Bioengineering Biology Applied Microbiology and Biotechnology 03 medical and health sciences chemistry.chemical_compound Drug Discovery Process Chemistry and Technology Lectin General Medicine Molecular biology 3. Good health Sialic acid 030104 developmental biology chemistry Biochemistry Biotinylation biology.protein Protein microarray Molecular Medicine Biotechnology |
| Zdroj: | Biotechnology and Applied Biochemistry. 63:457-464 |
| ISSN: | 0885-4513 |
| DOI: | 10.1002/bab.1407 |
| Popis: | Glycosylation is co- and posttranslational modifications affecting proteins. The glycopattern changes are associated with changes in biological function and are involved in many diseases including cancer. We present the lectin-based protein microarray method enabling determination of differences in protein glycosylation. The method involves isolation of targeted protein from samples by immunoprecipitation, spotting of protein from multiple samples into arrays on a microarray slide, incubation with set of biotinylated lectins, the reaction with fluorescent conjugate of streptavidin, and detection of fluorescent intensities by microarray scanner. Lectin-based protein microarray was applied in investigation of differences in alpha-2-macroglobulin (α2M) glycosylation isolated from sera samples of healthy persons and patients with colorectal cancer (CC). From 14 lectins used in analysis, statistically significant differences (Student's t-test, P < 0.05) between two groups of samples (persons without cancer and CC patients) were found for 5 of them. α2M molecules isolated from sera of CC patients have higher content of α2,6 sialic acid, N-acetylglucosamine and mannose residues, and tri-/tetraantennary complex type high-mannose N-glycans. A novel lectin-based protein microarray developed and described can serve as a suitable analytical technique for sensitive, simple, fast, and high-throughput determination of differences in protein glycosylation isolated from serum or other samples. |
| Databáze: | OpenAIRE |
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