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Cell adhesion and integrin binding to recombinant human fibrillin-1
M Pfaff1, D P Reinhardt, L Y Sakai
1Max Planck Institut für Biochemie, Martinsried, Germany.
FEBS Letters
|April 22, 1996
Summary
Fibrillin-1, a key protein in connective tissues, promotes cell adhesion through a specific RGD sequence. This sequence binds to integrin alphaVbeta3, revealing a new function for fibrillin-1 in cell interactions.
Area of Science:
- Biochemistry
- Cell Biology
- Connective Tissue Research
Background:
- Fibrillin-1 is a major component of extracellular microfibrils found in connective tissues.
- Its role in cell adhesion has not been fully elucidated.
Purpose of the Study:
- To investigate the potential cell-adhesive functions of fibrillin-1.
- To identify specific interactions between fibrillin-1 and cell surface receptors.
Main Methods:
- Recombinant human fibrillin-1 polypeptides were produced using a mammalian expression system.
- Cell attachment assays and solid-phase integrin binding assays were performed.
Main Results:
- Fibrillin-1 polypeptides containing an RGD sequence in the fourth 8-cysteine domain mediated cell adhesion.
- These polypeptides specifically bound to purified integrin alphaVbeta3.
- No interaction was observed with integrins alphaIIbbeta3, alpha5beta1, alpha2beta1, or alpha1beta1.
Conclusions:
- Fibrillin-1 plays a novel role in mediating cellular interactions.
- This interaction is facilitated by an exposed RGD motif recognized by integrin alphaVbeta3.