Analysis of molecular mechanism of tumor progression induced by an alpha6beta4 integrin

在本研究中，为了阐明n-糖基化对β4整合素的作用，我们在β4整合素缺失的角质形成细胞中建立了再表达野生型或n-糖基化缺陷型β4整合素的角质形成细胞。角质形成细胞的分析表明，n-糖基化在整合素介导的细胞粘附和迁移中起重要作用。此外，我们发现β4整合素通过与半乳糖凝集素-3介导的n-聚糖交联，与EGFR形成超分子复合物，从而促进细胞信号传导和随后的细胞功能。

In this study, to elucidate the role of N-glycosylation on β4 integrin, we established the keratinocytes re-expressing wild-type or N-glycosylation-defective β4 integrin in β4 integrin null keratinocytes. The analysis using the keratinocytes indicated that N-glycosylation plays important roles for integrin-mediated cell adhesion and migration. In addition, we found that β4 integrin forms supramolecular complex with EGFR through cross-linking with galectin-3-mediated N-glycans, thereby promoting cellular signaling and the following cellular function.