Roles of Integrin α6β4 Glycosylation in Cancer.

Roles of Integrin α6β4 Glycosylation in Cancer.
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DOI:
10.3390/cancers9070079
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发表时间:
2017-07-05
期刊:
影响因子:
5.2
通讯作者:
Gu J
Gu J
中科院分区:
医学2区
文献类型:
--
作者:
Kariya Y;Kariya Y;Gu J

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恶性转化伴随着蛋白质的异常糖基化。这种糖链结构的变化也发生在整合素中,整合素是细胞外基质的一个细胞表面受体大家族,在肿瘤进展中发挥关键作用。现在有越来越多的证据表明,整合素的糖基化影响细胞信号以及与细胞外基质、受体酪氨酸激酶和半乳糖凝集素的相互作用,从而调节细胞的黏附、运动、生长和存活。整合素α6β4是层粘连蛋白-332的受体,其表达水平的升高与各种癌症的恶性进展和预后不良有关。最近的研究表明,整合素α-6-β-4在肿瘤的发生和转移过程中起着核心作用。本文综述了目前对整合素α6β4调控肿瘤进展的分子机制的认识,并讨论了糖链对整合素β4亚单位的修饰,以阐明糖链在整合素介导的肿瘤进展中的重要作用。
Malignant transformation is accompanied with aberrant glycosylation of proteins. Such changes in glycan structure also occur in the integrins, which are a large family of cell surface receptors for the extracellular matrix and play key roles in tumor progression. There is now increasing evidence that glycosylation of integrins affects cellular signaling and interaction with the extracellular matrix, receptor tyrosine kinases, and galectins, thereby regulating cell adhesion, motility, growth, and survival. Integrin α6β4 is a receptor for laminin-332 and the increased expression level is correlated with malignant progression and poor survival in various types of cancers. Recent studies have revealed that integrin α6β4 plays central roles in tumorigenesis and the metastatic process. In this review, we summarize our current understanding of the molecular mechanisms of tumor progression driven by integrin α6β4 and also discuss the modification of glycans on integrin β4 subunit to address the important roles of glycan in integrin-mediated tumor progression.
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