Characterisation of α₃β₁ and α_vβ₃ integrin N

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• 作者：Marcelina E. Kremser ; Mał ; gorzata Przybył ; o ; Dorota Hoja-Ł ; ukowicz ; Ewa Pocheć ; Angela Amoresano ; Andrea Carpentieri ; Monika Bubka ; Anna Lityń ; ska
• 关键词：α ; ₃β ; ₁ integrin ; α ; _Vβ ; ₃ integrin ; N-oligosaccharide ; MALDI MS ; Lectin
• 刊名：Biochimica et Biophysica Acta (BBA)/General Subjects
• 出版年：2008
• 出版时间：December 2008
• 年：2008
• 卷：1780
• 期：12
• 页码：1421-1431
• 全文大小：1253 K

文摘

It is well documented that glycan synthesis is altered in some pathological processes, including cancer. The most frequently observed alterations during tumourigenesis are extensive expression of β1,6-branched complex type N-glycans, the presence of poly-N-acetyllactosamine structures, and high sialylation of cell surface glycoproteins. This study investigated two integrins, α₃β₁ and α_vβ₃, whose expression is closely related to cancer progression. Their oligosaccharide structures in two metastatic melanoma cell lines (WM9, WM239) were analysed with the use of matrix-assisted laser desorption ionisation mass spectrometry. Both examined integrins possessed heavily sialylated and fucosylated glycans, with β1,6-branches and short polylactosamine chains. In WM9 cells, α₃β₁ integrin was more variously glycosylated than α_vβ₃; in WM239 cells the situation was the reverse. Functional studies (wound healing and ELISA integrin binding assays) revealed that the N-oligosaccharide component of the tested integrins influenced melanoma cell migration on vitronectin and α₃β₁ integrin binding to laminin-5. Additionally, more variously glycosylated integrins exerted a stronger influence on these parameters. To the best of our knowledge, this is the first report concerning structural characterisation of α_vβ₃ integrin glycans in melanoma or in any cancer cells.