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. 2003 Oct 15;375(Pt 2):425–432. doi: 10.1042/BJ20030649

Fibrillin-1 and -2 contain heparin-binding sites important for matrix deposition and that support cell attachment.

Timothy M Ritty 1, Thomas J Broekelmann 1, Claudio C Werneck 1, Robert P Mecham 1
PMCID: PMC1223679  PMID: 12837131

Abstract

Fibrillin-1 and -2 are large modular extracellular matrix glycoproteins found in many vertebrate organ systems and are known to be key components of the elastic fibre. In the present study, we identify a new heparin-binding region in fibrillin-2 between exons 18 and 24. Additionally, we have narrowed the location of heparin-binding activity previously identified in fibrillin-1 to the last 17 residues of the mature proteolytically processed protein. This domain demonstrated higher activity as a multimer than as a monomer. The fibrillin-1 C-terminal site supported cell attachment in each of nine cell types tested. Attachment was shown to be mediated by cell-surface heparan sulphate proteoglycans. Fibrillin-1 has been shown previously to have heparin-binding activity that is important for matrix deposition of the molecule by fibroblasts. This function in deposition was confirmed in two additional fibrillin-producing cell types (osteosarcoma and epithelial cells) for the deposition of both fibrillin-1 and -2 into the extracellular matrix.

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Selected References

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