Sorafenib induced alteration of protein glycosylation in hepatocellular carcinoma cells
| Autor: | Wei Li, Shu Zhang, Yinkun Liu, Kun Guo, Riqiang Liu, Tianhua Liu, Qinle Zhang |
|---|---|
| Rok vydání: | 2017 |
| Předmět: |
0301 basic medicine
Sorafenib MAPK/ERK pathway Cancer Research Glycosylation glycosylation erythroblastosis 26-1 03 medical and health sciences chemistry.chemical_compound lectin microarray 0302 clinical medicine medicine chemistry.chemical_classification biology Glycoprotein binding Kinase Lectin Articles hepatocellular carcinoma Molecular biology digestive system diseases 030104 developmental biology Oncology chemistry 030220 oncology & carcinogenesis Jacalin biology.protein Cancer research sorafenib Glycoprotein medicine.drug |
| Zdroj: | Oncology Letters |
| ISSN: | 1792-1082 1792-1074 |
| Popis: | Sorafenib is a multikinase inhibitor and is effective in treating hepatocellular carcinoma (HCC). However, it remains unknown whether sorafenib induces the alteration of protein glycosylation. The present study treated HCC MHCC97L and MHCC97H cells with a 50% inhibitory concentration of sorafenib. Following this treatment, alteration of protein glycosylation was detected using a lectin microarray. Compared with the controls, the binding capacity of glycoproteins extracted from sorafenib-treated HCC cells to the lectins Bauhinia purpurea lectin, Dolichos biflorus agglutinin, Euonymus europaeus lectin, Helix aspersa lectin, Helix pomatia lectin, Jacalin, Maclura pomifera lectin and Vicia villosa lectin were enhanced; while, the binding capacities to the lectins Caragana arborescens lectin, Lycopersicon esculentum lectin, Limulus polyphemus lectin, Maackia amurensis lecin I, Phaseolus vulgaris leucoagglutinin, Ricinus communis agglutinin 60, Sambucus nigra lectin and Solanum tuberosum lectin were reduced (spot intensity median/background intensity median ≥2, P |
| Databáze: | OpenAIRE |
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