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Structural Studies on Cross-Linked Regions of Elastin

From the ¹ From the Department of Biochemistry, University of Toronto, Toronto, M5S 1A8, Canada

A novel use of Edman degradation was made in the study of desmosine- and isodesmosine-containing elastolytic peptides of bovine ligamentum nuchae elastin. The elastolysis of elastin produced peptides with the cleavage at or near the NH₂-terminals of desmosine and isodesmosine cross-links. Therefore, it became possible to release single chain peptides from the carboxyl groups of these cross-links with the use of Edman degradation. This approach permitted the isolation and sequencing of seven unique peptides from bovine ligamentum nuchae elastin; the sequences of five such peptides from porcine aortic elastin were also determined. The comparison of the sequences of these peptides with the NH₂-terminal sequences of porcine tropoelastin tryptic peptides (Foster, J. A., Bruenger, E., Gray, W. R., and Sandberg, L. B. (1973) J. Biol. Chem. 248, 2876–2879) permitted the identification of 12 possible lysine sequences which may be involved in cross-link formation. On the basis of the available data on elastin and tropoelastin, it is proposed that the tropoelastin molecule contains six pairs of lysines in the sequence -Lys-Ala-Ala-Lys- and six additional pairs of lysines in the sequence -Lys-Ala-Ala-Ala-Lys- and that two such pairs meet to form desmosine or isodesmosine cross-links.

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				P. Brown-Augsburger, C. Tisdale, T. Broekelmann, C. Sloan, and R. P. Mecham Identification of an Elastin Cross-linking Domain That Joins Three Peptide Chains J. Biol. Chem., July 28, 1995; 270(30): 17778 - 17783. [Abstract] [Full Text] [PDF]