Fibroblast adhesion to recombinant tropoelastin expressed as a Protein A-fusion protein

L. E. Grosso, W. C. Parks, L. Wu, R. P. Mecham

Research output: Contribution to journalArticlepeer-review

16 Scopus citations

Abstract

A bovine tropoelastin cDNA encoding exons 15-36 that includes the elastin-receptor binding site was expressed in Escherichia coli as a fusion protein with Protein A from Staphylococcus aureus. After isolation of the fusion protein by affinity chromatography on Ig-Sepharose, the tropoelastin domain was separated from plasmid-pR1T2T-encoded Protein A (Protein A') by CNBr cleavage. Cell-adhesion assays demonstrated specific adhesion to the recombinant tropoelastin. Furthermore, the data indicate that interactions involving the bovine elastin receptor mediate nuchal-ligament fibroblast adhesion to the recombinant protein. In agreement with earlier studies of fibroblast chemotaxis to bovine tropoelastin, nuchal-ligament fibroblast adhesion demonstrated developmental regulation of the elastin receptor.

Original languageEnglish
Pages (from-to)517-522
Number of pages6
JournalBiochemical Journal
Volume273
Issue number3
DOIs
StatePublished - 1991

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