A defect in the structure of type I procollagen in a patient who had osteogenesis imperfecta: excess mannose in the COOH-terminal propeptide. Academic Article uri icon

abstract

  • Fibroblasts from normal human subjects and from a patient who had osteogenesis imperfecta were incubated with [3H]mannose, and types I and III procollagens were isolated from the culture medium. The type I procollagen from the patient's fibroblasts contained 2-3 time more [3H]mannose than the type I procollagen from the normal fibroblasts. In contrast, there was no difference in the [3H]mannose content of the type III procollagen simultaneously synthesized and secreted by the same cells. Isolation of a collagenase-resistant peptide fragment from the type I procollagen showed that the excess mannose was located in the COOH-terminal propeptide of the protein. Radioimmunoassays of the medium and the cell layer showed that the type I procollagen synthesized by the patient's fibroblasts was secreted into the medium more slowly than the type I procollagen synthesized by normal fibroblasts. These results appear to provide evidence for an alteration in the structure of procollagen in osteogenesis imperfecta.

published proceedings

  • Proc Natl Acad Sci U S A

author list (cited authors)

  • Peltonen, L., Palotie, A., & Prockop, D. J.

citation count

  • 70

complete list of authors

  • Peltonen, L||Palotie, A||Prockop, DJ

publication date

  • October 1980