Cell-type specific recognition of RGD- and non-RGD-containing cell binding domains in fibrillin-1

Hiroshi Sakamoto, Thomas Broekelmann, David A. Cheresh, Francesco Ramirez, Joel Rosenbloom, Robert P. Mecham

Research output: Contribution to journalArticlepeer-review

142 Scopus citations

Abstract

The fibrillins are large glycoprotein components of 10-nm microfibrils found in the extracellular matrix of most tissues. Microfibrils play a role in elastic fiber assembly and serve to link cells to elastic fibers in the extracellular matrix. To determine whether fibrillin-1 specifically interacts with receptors on cells from fibrillin-rich tissues, we evaluated whether two cell types that produce different types of fibrillin can adhere to purified fibrillin-1 in cell adhesion assays. Our results indicate that both cell types attach and spread on fibrillin-1 and that the RGD sequence in the fourth 8-cysteine motif mediates this interaction. Fibroblast attachment to fibrillin-1 was sensitive to inhibition by antibodies to the αvβ3 receptor and by peptides encoding the RGD sequence in fibrillin-1 and the second RGD sequence in fibrillin-2. In contrast, adhesion of auricular chondroblasts to fibrillin-1 was only partially inhibited by these reagents, suggesting that some cell types recognize a second, non-RGD binding site within the fibrillin molecule. These findings confirm and extend ultrastructural studies that suggest a direct interaction between microfibrils and the cell surface and provide a functional explanation for how this association occurs.

Original languageEnglish
Pages (from-to)4916-4922
Number of pages7
JournalJournal of Biological Chemistry
Volume271
Issue number9
DOIs
StatePublished - Mar 1 1996

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