Direct visualization of affected collagen molecules synthesized by cultured fibroblasts from an osteogenesis imperfecta patient.

Abstract

Human skin fibroblasts obtained from normal controls and a patient with osteogenesis imperfecta were cultured in the presence of ascorbic acid 2-phosphate, a long-acting vitamin C derivative. Crude collagen samples extracted from the cell layer were made to form lateral aggregates of collagen molecules, segment-long-spacing crystallites. Under the electron microscope, normal and abnormal crystallites of type I collagen were identified with the patient's collagen. While the carboxyl-terminal half of the abnormal crystallite was tightly packed, the amino-terminal half was loose and spreading, indicating the site of abnormality in the amino-terminal half of one of type I collagen alpha chains. The method is simple and useful to detect abnormal collagen and to predict the site of mutation.

• Authors: K Kobayashi, R Hata, S Nagai, J Niwa, T Hoshino
• Journal: Biochemical and biophysical research communications (Biochem Biophys Res Commun) Vol. 172 Issue 1 Pg. 217-22 (Oct 15 1990) ISSN: 0006-291X [Print] United States
• PMID: 2222471 (Publication Type: Case Reports, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Collagen

Topics

• Adult
• Amino Acid Sequence
• Cells, Cultured
• Collagen (biosynthesis, ultrastructure)
• Female
• Fibroblasts (metabolism)
• Humans
• Infant, Newborn
• Male
• Microscopy, Electron
• Mutation
• Osteogenesis Imperfecta (metabolism)
• Protein Conformation
• Reference Values
• Skin (metabolism)