Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias

  • H W Lehmann
  • E Wolf
  • K Röser
  • M Bodo
  • G Delling
  • P K Müller

Abstract

The composition of collagen was analyzed and the degree of lysyl hydroxylation of individual collagen chains was determined in four osteosarcomas and two osteofibrous dysplasias. In addition, the tumor proliferation (number of mitoses, proliferating-nuclear-antigen-positive cells, MIB) as well as the response to chemotherapy (morphological regression grade) were checked. All tumors contained a high proportion of collagen III and, in all but one osteosarcoma, pepsin-extracted collagens I and III were overmodified. Furthermore, the proportion of diglycosides in collagen I was about four times higher than in controls. The collagen composition and modification resembled those of bones at early stages of human development. One osteosarcoma and both osteofibrous dysplasias were in the normal range of lysyl hydroxylation. There was no correlation between the collagen properties and the histopathological marker of tumor proliferation.

Bibliographical data

Original languageEnglish
ISSN0171-5216
Publication statusPublished - 1995
PubMed 7635871