A High Molecular Weight Species of Soluble Elastin-Proelastin

  • Judith Ann Foster
  • Robert Mecham
  • Michael Imberman
  • Barbara Faris
  • Carl Franzblau
Part of the Advances in Experimental Medicine and Biology book series (AEMB, volume 79)


The isolation of a high molecular weight species (130–140,000 daltons) of soluble elastin from the aortae of lathyritic chicks is described. In comparison to chick tropoelastin, the higher molecular weight material possesses an increased amount of acidic and hydroxyl amino acids and in contrast to tropoelastin, contains histidine, methionine and cystine residues. This high molecular weight species of soluble elastin is susceptible to proteolytic degradation and can be shown to readily break down to lower molecular weight components including tropoelastin. Preliminary data suggest that collagen may have a protective effect on the cleavage of the high molecular weight protein pointing to a potentially significant interaction between the two main structural proteins.

Immunoelectrophoresis of the high molecular weight soluble elastin reveals that it is electrophoretically distinct from tropoelastin yet it is immunochemically related or identical.

Ion exchange chromatography of a partially degraded sample of the high molecular weight elastin allows the separation of tropoelastin (72,000 daltons) and a more acidic protein (65,000 daltons) which is distinct from tropoelastin yet contains hydroxyproline. The amino acid analysis of the two components added together yield a composition similar if not identical to proelastin.

Automated sequence analyses of the intact high molecular weight protein reveals an NH2 terminal sequence homologous to tropoelastin. These data suggest that the 65,000 molecular weight protein is attached onto the C-terminals of tropoelastin.

The new model of elastin fibrogenesis is proposed based on initial alignment of proelastin molecules on the microfibril via disulfide linkages.


High Molecular Weight Amino Acid Analysis High Molecular Weight Protein High Molecular Weight Species High Molecular Weight Component 


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.


  1. 1.
    Weissman, N., Shields, G.S. and Carnes, W.H. (1963) J. Biol. Chem. 238, 3115–3123.PubMedGoogle Scholar
  2. 2.
    Sandberg, L.B., Weissman, N. and Smith, D.W. (1969) Biochemistry 8, 2940–2945.PubMedCrossRefGoogle Scholar
  3. 3.
    Partridge, S.M., Davis, H.F. and Adair, G.S. (1955) Biochem. J. 61, 11–14.PubMedGoogle Scholar
  4. 4.
    Lansing, A.I., Rosenthal, T.B., Alex, M. and Dempsey, E.W. (1952) Anat. Record 114, 555–570.CrossRefGoogle Scholar
  5. 5.
    Richmond, V., Biochim. Biophys. Acta 351, 173–177.Google Scholar
  6. 6.
    Serafini-Fracassini, A., Field, J.M., Rodger, G.W. and Spina, M. (1976) Biochem. Biophys. Acta 386, 73–77.Google Scholar
  7. 7.
    Rasmussen, B.L., Bruenger, E.L. and Sandberg, L.B. (1975) Anal. Biochem. 64, 255–259.PubMedCrossRefGoogle Scholar
  8. 8.
    Faris, B., Salcedo, L.L., Cook, V., Johnson, L., Foster, J.A. and Franzblau, C. (1976) Biochim. Biophys. Acta 427, 302–314.PubMedCrossRefGoogle Scholar
  9. 9.
    Mecham, R., Foster, J.A. and Franzblau, C. (1976) Biochim. Biophys. Acta, In Press.Google Scholar
  10. 10.
    Foster, J.A., Shapiro, R., Voynow, P., Crombie, G. Faris, B. and Franzblau, C. (1975) Biochemistry 14, 5343–5347.PubMedCrossRefGoogle Scholar
  11. 11.
    Foster, J.A., Knaack, D., Faris, B., Moscaritolo, R., Salcedo, L., Skinner, M. and Franzblau, C. (1976a) Biochim. Biophys. Acta, In Press.Google Scholar
  12. 12.
    Foster, J.A., Mecham, R. and Franzblau C. (1976b) Biochem. Biophys. Res. Commun. In Press.Google Scholar

Copyright information

© Plenum Press, New York 1977

Authors and Affiliations

  • Judith Ann Foster
    • 1
  • Robert Mecham
    • 1
  • Michael Imberman
    • 1
  • Barbara Faris
    • 1
  • Carl Franzblau
    • 1
  1. 1.Department of BiochemistryBoston University School of MedicineBostonUSA

Personalised recommendations