Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias
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Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias. / Lehmann, H W; Wolf, E; Röser, K; Bodo, M; Delling, G; Müller, P K.
in: J CANCER RES CLIN, Jahrgang 121, Nr. 7, 1995, S. 413-8.Publikationen: SCORING: Beitrag in Fachzeitschrift/Zeitung › SCORING: Zeitschriftenaufsatz › Forschung › Begutachtung
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TY - JOUR
T1 - Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias
AU - Lehmann, H W
AU - Wolf, E
AU - Röser, K
AU - Bodo, M
AU - Delling, G
AU - Müller, P K
PY - 1995
Y1 - 1995
N2 - 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.
AB - 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.
KW - Adolescent
KW - Adult
KW - Bone Neoplasms
KW - Cell Division
KW - Child
KW - Collagen
KW - Electrophoresis, Polyacrylamide Gel
KW - Fibrous Dysplasia of Bone
KW - Glycosylation
KW - Humans
KW - Hydroxylation
KW - Hydroxylysine
KW - Lysine
KW - Osteosarcoma
KW - Proline
KW - Protein Processing, Post-Translational
KW - Sodium Dodecyl Sulfate
KW - Comparative Study
KW - Journal Article
KW - Research Support, Non-U.S. Gov't
M3 - SCORING: Journal article
C2 - 7635871
VL - 121
SP - 413
EP - 418
JO - J CANCER RES CLIN
JF - J CANCER RES CLIN
SN - 0171-5216
IS - 7
ER -