Production of overmodified type I procollagen in a case of osteogenesis imperfecta

S. Tajima, M. Takehana, N. Azuma

Research output: Contribution to journalArticle

14 Citations (Scopus)

Abstract

Collagen synthesis in cultured skin fibroblasts from a patient with osteogenesis imperfecta was studied. Approximately 2 fold accumulation of collagen in the cell layer was found. The slower mobility of proα1 (I) and proα2 (I) as well as α1 and α2 (I) polypeptide on sodium dodecylsulfate-polyacrylamide gel electrophoresis was detected, indicating that abnormal posttranslational modification could be present in type I procollagen in patient fibroblasts. The degrees of hydroxylation and subsequent glycosylation of lysine residues in the affected collagen were elevated 1.5 and 1.4 fold, respectively. There were no significant changes in the relative content of type III to type I collagen nor the incorporation of mannose into the carboxyterminal propeptide of proα1 (I) and proα2 (I). These results indicate that the patient produces an over-modified type I procollagen which is responsible for the clinical features and has a collagen abnormality already reported in type II osteogenesis imperfecta.

Original languageEnglish
Pages (from-to)219-222
Number of pages4
JournalJournal of Dermatology
Volume21
Issue number4
Publication statusPublished - 1994

Fingerprint

Osteogenesis Imperfecta
Collagen Type I
Collagen
Fibroblasts
Hydroxylation
Post Translational Protein Processing
Mannose
Glycosylation
Lysine
Polyacrylamide Gel Electrophoresis
Sodium
Skin
Peptides

ASJC Scopus subject areas

  • Dermatology

Cite this

Production of overmodified type I procollagen in a case of osteogenesis imperfecta. / Tajima, S.; Takehana, M.; Azuma, N.

In: Journal of Dermatology, Vol. 21, No. 4, 1994, p. 219-222.

Research output: Contribution to journalArticle

Tajima, S, Takehana, M & Azuma, N 1994, 'Production of overmodified type I procollagen in a case of osteogenesis imperfecta', Journal of Dermatology, vol. 21, no. 4, pp. 219-222.
Tajima, S. ; Takehana, M. ; Azuma, N. / Production of overmodified type I procollagen in a case of osteogenesis imperfecta. In: Journal of Dermatology. 1994 ; Vol. 21, No. 4. pp. 219-222.
@article{c88c09142eb0473a91678277310e566a,
title = "Production of overmodified type I procollagen in a case of osteogenesis imperfecta",
abstract = "Collagen synthesis in cultured skin fibroblasts from a patient with osteogenesis imperfecta was studied. Approximately 2 fold accumulation of collagen in the cell layer was found. The slower mobility of proα1 (I) and proα2 (I) as well as α1 and α2 (I) polypeptide on sodium dodecylsulfate-polyacrylamide gel electrophoresis was detected, indicating that abnormal posttranslational modification could be present in type I procollagen in patient fibroblasts. The degrees of hydroxylation and subsequent glycosylation of lysine residues in the affected collagen were elevated 1.5 and 1.4 fold, respectively. There were no significant changes in the relative content of type III to type I collagen nor the incorporation of mannose into the carboxyterminal propeptide of proα1 (I) and proα2 (I). These results indicate that the patient produces an over-modified type I procollagen which is responsible for the clinical features and has a collagen abnormality already reported in type II osteogenesis imperfecta.",
author = "S. Tajima and M. Takehana and N. Azuma",
year = "1994",
language = "English",
volume = "21",
pages = "219--222",
journal = "Journal of Dermatology",
issn = "0385-2407",
publisher = "Wiley-Blackwell",
number = "4",

}

TY - JOUR

T1 - Production of overmodified type I procollagen in a case of osteogenesis imperfecta

AU - Tajima, S.

AU - Takehana, M.

AU - Azuma, N.

PY - 1994

Y1 - 1994

N2 - Collagen synthesis in cultured skin fibroblasts from a patient with osteogenesis imperfecta was studied. Approximately 2 fold accumulation of collagen in the cell layer was found. The slower mobility of proα1 (I) and proα2 (I) as well as α1 and α2 (I) polypeptide on sodium dodecylsulfate-polyacrylamide gel electrophoresis was detected, indicating that abnormal posttranslational modification could be present in type I procollagen in patient fibroblasts. The degrees of hydroxylation and subsequent glycosylation of lysine residues in the affected collagen were elevated 1.5 and 1.4 fold, respectively. There were no significant changes in the relative content of type III to type I collagen nor the incorporation of mannose into the carboxyterminal propeptide of proα1 (I) and proα2 (I). These results indicate that the patient produces an over-modified type I procollagen which is responsible for the clinical features and has a collagen abnormality already reported in type II osteogenesis imperfecta.

AB - Collagen synthesis in cultured skin fibroblasts from a patient with osteogenesis imperfecta was studied. Approximately 2 fold accumulation of collagen in the cell layer was found. The slower mobility of proα1 (I) and proα2 (I) as well as α1 and α2 (I) polypeptide on sodium dodecylsulfate-polyacrylamide gel electrophoresis was detected, indicating that abnormal posttranslational modification could be present in type I procollagen in patient fibroblasts. The degrees of hydroxylation and subsequent glycosylation of lysine residues in the affected collagen were elevated 1.5 and 1.4 fold, respectively. There were no significant changes in the relative content of type III to type I collagen nor the incorporation of mannose into the carboxyterminal propeptide of proα1 (I) and proα2 (I). These results indicate that the patient produces an over-modified type I procollagen which is responsible for the clinical features and has a collagen abnormality already reported in type II osteogenesis imperfecta.

UR - http://www.scopus.com/inward/record.url?scp=0028338656&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0028338656&partnerID=8YFLogxK

M3 - Article

C2 - 8056893

AN - SCOPUS:0028338656

VL - 21

SP - 219

EP - 222

JO - Journal of Dermatology

JF - Journal of Dermatology

SN - 0385-2407

IS - 4

ER -