Pfaff M, Reinhardt D P, Sakai L Y, Timpl R
Max Planck Institut für Biochemie, Martinsried, Germany.
FEBS Lett. 1996 Apr 22;384(3):247-50. doi: 10.1016/0014-5793(96)00325-0.
Fibrillin-1 is a major constituent of tissue microfibrils that occur in most connective tissues, either in close association with or independent of elastin. To test possible cell-adhesive functions of this protein, we used recombinant human fibrillin-1 polypeptides produced in a mammalian expression system in cell attachment and solid-phase integrin binding assays. Fibrillin-1 polypeptides containing the single RGD sequence located in the fourth 8-cysteine domain, mediated distinct cell adhesion of a variety of cell lines and bound to purified integrin alphaVbeta3. Integrins alphaIIbbeta3, alpha5beta1, alpha2beta1 and alpha1beta1 did not interact with any of the recombinant fibrillin-1 peptides. Our results indicate a novel role for fibrillin-1 in cellular interactions mediated via an RGD motif that is appropriately exposed for recognition by integrin alphaVbeta3.
原纤蛋白-1是组织微原纤维的主要成分，存在于大多数结缔组织中，与弹性蛋白紧密相连或独立于弹性蛋白。为了测试该蛋白可能的细胞黏附功能，我们在细胞黏附及固相整合素结合试验中，使用了在哺乳动物表达系统中产生的重组人原纤蛋白-1多肽。位于第四个8-半胱氨酸结构域的含单个RGD序列的原纤蛋白-1多肽，介导了多种细胞系的明显细胞黏附，并与纯化的整合素αVβ3结合。整合素αIIbβ3、α5β1、α2β1和α1β1与任何重组原纤蛋白-1肽均无相互作用。我们的结果表明原纤蛋白-1在经由RGD基序介导的细胞相互作用中具有新作用，该基序能适当暴露以供整合素αVβ3识别。
