Cell adhesion and integrin binding to recombinant human fibrillin‐1

FEBS Letters

Reinhardt, Dieter P.²  Timpl, Rupert¹  Sakai, Lynn Y.²  Pfaff, Martin¹ 

[1] Max Planck Institut für Biochemie, D-82152 Martinsried, Germany;Shriners Hospital for Crippled Children, Research Department, Portland, OR 97201, USA

关键词: Fibrillin-1;    Integrin;    RGD;    Cell adhesion;   

DOI  :  10.1016/0014-5793(96)00325-0

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 αVβ3. Integrins αIIbβ3, α5β1, α2β1 and α1β1 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 αVβ3.

【 授权许可】

Unknown