Production of recombinant human tropoelastin: Characterization and demonstration of immunologic and chemotactic activity

Zena Indik, William R. Abrams, Umberto Kucich, Carolyn W. Gibson, Robert P. Mecham, Joel Rosenbloom

Research output: Contribution to journalArticle

66 Scopus citations

Abstract

Tropoelastin cannot readily be prepared in quantity from natural sources and this has limited research in several important areas including structure/function relationships and fiber assembly. In order to eliminate this limitation, human tropoelastin has been expressed in a recombinant bacterial system and the protein has been highly purified. The size, amino acid composition, and sequence of the amino terminus of the recombinant tropoelastin (rTE) all agree with values predicted by the nucleotide sequence of the cDNA used in the expression vector. The rTE exhibits cross-reactivity with antibodies directed against a mixture of peptides derived from human elastin as well as antibody against a defined peptide located at the carboxy terminus of the protein. In addition, the rTE is chemotactic for fetal calf ligament fibroblasts. These results suggest that rTE could be a useful reagent for many types of studies.

Original languageEnglish
Pages (from-to)80-86
Number of pages7
JournalArchives of Biochemistry and Biophysics
Volume280
Issue number1
DOIs
StatePublished - Jul 1990
Externally publishedYes

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