Migration of keratinocytes is impaired on glycated collagen I
Migration of keratinocytes is impaired on glycated collagen I
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DOI：
10.1111/j.1067-1927.2005.130112.x
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发表时间：
2005-01-01
影响因子：
2.9
通讯作者：
Furue, M
中科院分区：
文献类型：
--
作者：
Morita, K;Urabe, K;Furue, M
晚期糖基化终末产物是糖在高血糖条件下对蛋白质的化学修饰，细胞外基质蛋白由于其缓慢的周转速度而成为非酶糖基化的重要靶点。本研究旨在探讨I型胶原非酶糖化对角质形成细胞迁移的影响。与未涂层的培养皿相比，国产I型胶原涂层培养皿中角质形成细胞的迁移明显增强。当I型胶原用乙醇醛糖化时，会产生大量的晚期糖基化终产物；糖化的I型胶原包衣培养皿不能促进角质形成细胞的迁移。糖化I型胶原不影响角质形成细胞的增殖能力。然而，角质形成细胞对糖化的I型胶原的粘附力以糖化强度依赖的方式显著降低。α2β1整合素负责角质形成细胞与I型胶原的迁移和黏附。糖基化的I型胶原不影响角质形成细胞α2β1整合素的表达水平和功能活性。这些发现表明，在糖化的胶原1存在的情况下，角质形成细胞失去了它们的黏附和迁移能力。由于糖基化不改变角质形成细胞上的α2β1整合素，提示糖基化可能会削弱I型胶原的结合能力。
Advanced glycation end products are the chemical modification of proteins induced by sugars in a hyperglycemic condition, Extracellular matrix proteins are prominent targets of nonenzymatic glycation because of their slow turnover rates. The aim of this study was to investigate the influence of nonenzymatic glycation of type I collagen on the migration of keratinocytes. The migration of keratinocytes was dramatically promoted on native type I collagen-coated dishes compared with that on uncoated dishes. When type I collagen was glycated with glycolaldehyde, large amounts of advanced glycation end products were produced; the glycated collagen 1-coated dishes did not promote the migration of keratinocytes. Glycated collagen I did not affect the proliferative capacity of keratinocytes. However, the adhesion of keratinocytes to glycated collagen I was profoundly diminished in a glycation intensity-dependent manner. alpha2beta1 integrin is responsible for the migration and adhesion of keratinocytes to type I collagen. Pretreatment with glycated collagen I did not affect the expression level or functional activity of alpha2beta1 integrin on keratinocytes. These findings suggest that in the presence of glycated collagen 1, keratinocytes lose their adhesive and migratory abilities. As the glycation did not modify the alpha2beta1 integrin on keratinocytes, it is suggested that glycation may diminish the binding capacity of type I collagen.