硫酸乙酰肝素
细胞外基质
化学
糖胺聚糖
蛋白多糖
硫酸化
佩莱肯
细胞生物学
细胞粘附
细胞迁移
癌细胞
生物化学
细胞
癌症
生物
遗传学
作者
Lorenzo Depau,Jlenia Brunetti,Chiara Falciani,Elisabetta Mandarini,Giulia Riolo,Marta Zanchi,Evgenia Karousou,Alberto Passi,Alessandro Pini,Luisa Bracci
标识
DOI:10.1021/acs.jmedchem.0c01848
摘要
Heparan sulfate proteoglycans take part in crucial events of cancer progression, such as epithelial–mesenchymal transition, cell migration, and cell invasion. Through sulfated groups on their glycosaminoglycan chains, heparan sulfate proteoglycans interact with growth factors, morphogens, chemokines, and extracellular matrix (ECM) proteins. The amount and position of sulfated groups are highly variable, thus allowing differentiated ligand binding and activity of heparan sulfate proteoglycans. This variability and the lack of specific ligands have delayed comprehension of the molecular basis of heparan sulfate proteoglycan functions. Exploiting a tumor-targeting peptide tool that specifically recognizes sulfated glycosaminoglycans, we analyzed the role of membrane heparan sulfate proteoglycans in the adhesion and migration of cancer cell lines. Starting from the observation that the sulfated glycosaminoglycan-specific peptide exerts a different effect on adhesion, migration, and invasiveness of different cancer cell lines, we identified and characterized three cell migration phenotypes, where different syndecans are associated with alternative signaling for directional cell migration.
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