Cell adhesion and integrin binding to recombinant human fibrillin-1

• Published in: FEBS letters Vol. 384; no. 3; pp. 247 - 250
• Main Authors: Pfaff, Martin, Reinhardt, Dieter P., Sakai, Lynn Y., Timpl, Rupert
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 22-04-1996
• Subjects: Amino Acid Sequence; Binding Sites; Cell Adhesion; Cell Line; Fibrillin-1; Fibrillins; Fibrinogen - metabolism; Fibroblasts - cytology; Humans; Integrin; Integrins - metabolism; Microfilament Proteins - chemistry; Microfilament Proteins - isolation & purification; Microfilament Proteins - metabolism; Molecular Sequence Data; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Recombinant Proteins - chemistry; Recombinant Proteins - isolation & purification; Recombinant Proteins - metabolism; RGD; Sensitivity and Specificity; Tumor Cells, Cultured; Vitronectin - metabolism; Fibrillin-1; Integrin; RGD; Cell adhesion
• ISSN: 0014-5793; 1873-3468
• 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 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.