hydroxylysine has been researched along with Osteosarcoma* in 2 studies
2 other study(ies) available for hydroxylysine and Osteosarcoma
| Article | Year |
|---|---|
Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias.
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. Topics: Adolescent; Adult; Bone Neoplasms; Cell Division; Child; Collagen; Electrophoresis, Polyacrylamide Gel; Fibrous Dysplasia of Bone; Glycosylation; Humans; Hydroxylation; Hydroxylysine; Lysine; Osteosarcoma; Proline; Protein Processing, Post-Translational; Sodium Dodecyl Sulfate | 1995 |
Collagen polymorphism in extracellular matrix of human osteosarcoma.
The collagenous matrix of human osteosarcoma was characterized biochemically and ultrastructurally. The highly cellular regions of the tumors contained many osteoblast-like cells filled with dilated rough endoplasmic reticulum. The extracellular matrix displayed a random weave of banded collagen fibrils (30--90 nm in diameter) interspersed with thinner, unbanded fibrils (15 nm in diameter). Tumors from 9 patients were analyzed for collagen composition. All gave a similar collagen profile. Three main molecular species of collagen were abundant: type I, type III, and type V, which occurred in the approximate proportions of 65:25:10. A high ratio of alpha 1(I) to alpha 2(I) chains suggested that one-third of the type I collagen was present as a type I trimer molecule. In contrast, normal bone matrix consisted almost exclusively of type I collagen. The fibrillar collagens in the soft tumor seemed unusually rich in hydroxylysine and hydroxylysine glycosides; type I collagen had two to three times the hydroxylysine content of normal bone collagen. Topics: Adolescent; Adult; Bone Neoplasms; Child; Collagen; Extracellular Space; Humans; Hydroxylysine; Molecular Weight; Osteosarcoma; Polymorphism, Genetic | 1982 |