Hw. Lehmann et al., COMPOSITION AND POSTTRANSLATIONAL MODIFICATION OF INDIVIDUAL COLLAGENCHAINS FROM OSTEOSARCOMAS AND OSTEOFIBROUS DYSPLASIAS, Journal of cancer research and clinical oncology, 121(7), 1995, pp. 413-418
The composition of collagen was analyzed and the degree of lysyl hydro
xylation of individual collagen chains was determined in four osteosar
comas and two osteofibrous dysplasias. In addition, the tumor prolifer
ation (number of mitoses, proliferating-nuclear-antigen-positive cells
, MIB) as well as the response to chemotherapy (morphological regressi
on grade) were checked. All tumors contained a high proportion of coll
agen III and, in all but one osteosarcoma, pepsin-extracted collagens
I and III were overmodified. Furthermore, the proportion of diglycosid
es in collagen I was about four times higher than in controls. The col
lagen composition and modification resembled those of bones at early s
tages of human development. One osteosarcoma and both osteofibrous dys
plasias were in the normal range of lysyl hydroxylation. There was no
correlation between the collagen properties and the histopathological
marker of tumor proliferation.