Center for Biochemistry, Medical Faculty, University of Cologne, D-50931 Cologne, Germany.
J Biol Chem. 2011 Aug 5;286(31):27804-13. doi: 10.1074/jbc.M111.220046. Epub 2011 Jun 7.
Cellular receptors for collagens belong to the family of β(1) integrins. In the epidermis, integrin α(2)β(1) is the only collagen-binding integrin present. Its expression is restricted to basal keratinocytes with uniform distribution on the cell surface of those cells. Although α(2)β(1) receptors localized at the basal surface interact with basement membrane proteins collagen IV and laminin 111 and 332, no interaction partners have been reported for these integrin molecules at the lateral and apical membranes of basal keratinocytes. Solid phase binding and surface plasmon resonance spectroscopy demonstrate that collagen XXIII, a member of the transmembrane collagens, directly interacts with integrin α(2)β(1) in an ion- and conformation-dependent manner. The two proteins co-localize on the surface of basal keratinocytes. Furthermore, collagen XXIII is sufficient to induce adhesion and spreading of keratinocytes, a process that is significantly reduced in the absence of functional integrin α(2)β(1).
细胞胶原受体属于β(1)整合素家族。在表皮中,整合素α(2)β(1)是唯一存在的胶原结合整合素。它的表达局限于基底角质形成细胞,在这些细胞的细胞表面均匀分布。尽管定位于基底表面的α(2)β(1)受体与基底膜蛋白Ⅳ型胶原和层粘连蛋白 111 和 332 相互作用,但尚未报道基底角质形成细胞的侧向和顶端膜上这些整合素分子的相互作用伙伴。固相结合和表面等离子体共振光谱分析表明,跨膜胶原成员 XXIII 以离子和构象依赖的方式直接与整合素α(2)β(1)相互作用。这两种蛋白质在基底角质形成细胞的表面共定位。此外,胶原 XXIII 足以诱导角质形成细胞的黏附和铺展,在缺乏功能性整合素α(2)β(1)的情况下,该过程显著减少。