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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, Vol. 121, No. 7, 1995, p. 413-8.

Research output: SCORING: Contribution to journal › SCORING: Journal article › Research › peer-review

Harvard

Lehmann, HW, Wolf, E, Röser, K, Bodo, M, Delling, G & Müller, PK 1995, 'Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias', J CANCER RES CLIN, vol. 121, no. 7, pp. 413-8.

APA

Lehmann, H. W., Wolf, E., Röser, K., Bodo, M., Delling, G., & Müller, P. K. (1995). Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias. J CANCER RES CLIN, 121(7), 413-8.

Vancouver

Lehmann HW, Wolf E, Röser K, Bodo M, Delling G, Müller PK. Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias. J CANCER RES CLIN. 1995;121(7):413-8.

Bibtex

@article{0a3295edb0a0435a8baa4c226c14fc32,
title = "Composition and posttranslational modification of individual collagen chains from osteosarcomas and osteofibrous dysplasias",
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.",
keywords = "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, Comparative Study, Journal Article, Research Support, Non-U.S. Gov't",
author = "Lehmann, {H W} and E Wolf and K R{\"o}ser and M Bodo and G Delling and M{\"u}ller, {P K}",
year = "1995",
language = "English",
volume = "121",
pages = "413--8",
journal = "J CANCER RES CLIN",
issn = "0171-5216",
publisher = "Springer",
number = "7",

}

RIS

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 -