Synthesis of elastin and procallagen by cells from embryonic aorta. Differences in the role of hydroxyproline and the effects of proline analogs on the secretion of the two proteins. Academic Article uri icon

abstract

  • Cells free of extracellular matrix were prepared by controlled enzymic digestion of aortas and associated large blood vessels of chick embryos. When the isolated cells were incubated in suspension, they synthesized and secreted both procollagen and an elastin component. The procollagen was shown to be predominantly of the Type I variety. The elastin component contained hydroxyproline, and hydroxyproline accounted for about one-third of the total imino acid content of the protein. The presence of hydroxyproline in the elastin component, however, was shown to be a coincidental feature in terms of the synthesis and secretion of the molecule. When the cells were incubated with the chelator α,α′-dipyridyl so as to inhibit prolyl hydroxylase, intact procollagen was no longer recovered from the medium, but the unhydroxylated elastin component was synthesized and secreted at a normal rate. When the cells were incubated with several proline analogs which have been previously shown to be incorporated into protein, intact procollagen no longer appeared in the medium. However, the elastin component was synthesized and secreted at a normal rate, an observation supporting previous suggestions that proline analogs may function as specific inhibitors of procollagen synthesis. Incubation of the cells with colchicine slowed the secretion of both the procollagen and the elastin components. The results suggested, therefore, that elastin may be secreted by the same system of vacuoles that is involved in the secretion of procollagen. © 1976.

published proceedings

  • Arch Biochem Biophys

author list (cited authors)

  • Uitto, J., Hoffmann H-P, .., & Prockop, D. J

citation count

  • 106

complete list of authors

  • Uitto, J||Prockop, DJ
  • Uitto, J||||Prockop, DJ

publication date

  • March 1976