Open AccessThermal stability of type I and type III procollagens from normal human fibroblasts and from a patient with osteogenesis imperfecta.
Author(s) -
Leena Peltonen,
Aarno Palotie,
Toshihiko Hayashi,
Darwin J. Prockop
Publication year - 1980
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.77.1.162
Subject(s) - osteogenesis imperfecta , procollagen peptidase , fibroblast , chemistry , type i collagen , microbiology and biotechnology , biochemistry , biology , anatomy , endocrinology , in vitro
Type I and type III procollagens were isolated from the medium of human fibroblast cultures in amounts adequate for examination by circular dichroism. Type I procollagen had a spectrum similar to that of type I procollagen and collagen from chicken embryos. The human type III procollagen showed a red shift not seen in type III collagen from calf skin. The midpoint (tm) for the helix-to-coil transition for both human procollagens was 40 degrees C. the same tm values were obtained with type I and type III procollagens synthesized by fibroblasts from a patient with osteogenesis imperfecta. Type I procollagen synthesized by the patient's fibroblasts, however, tended to aggregate more readily than type I procollagen from normal human fibroblasts, apparently because of a structural alteration of the protein.