Caffey disease: new perspectives on old questions.

Abstract

The autosomal dominant form of Caffey disease is a largely self-limiting infantile bone disorder characterized by acute inflammation of soft tissues and localized thickening of the underlying bone cortex. It is caused by a recurrent arginine-to-cysteine substitution (R836C) in the α1(I) chain of type I collagen. However, the functional link between this mutation and the underlying pathogenetic mechanisms still remains elusive. Importantly, it remains to be established as to how a point-mutation in type I collagen leads to a cascade of inflammatory events and spatio-temporally limited hyperostotic bone lesions, and how structural and inflammatory components contribute to the different organ-specific manifestations in Caffey disease. In this review we attempt to shed light on these questions based on the current understanding of other mutations in type I collagen, their role in perturbing collagen biogenesis, and consequent effects on cell-cell and cell-matrix interactions.

• Authors: Harikiran Nistala, Outi Mäkitie, Harald Jüppner
• Journal: Bone (Bone) Vol. 60 Pg. 246-51 (Mar 2014) ISSN: 1873-2763 [Electronic] United States
• PMID: 24389367 (Publication Type: Journal Article, Research Support, N.I.H., Extramural, Review)
• Copyright: Copyright © 2013 Elsevier Inc. All rights reserved.

Chemical References

• Collagen Type I

Topics

• Amino Acid Sequence
• Collagen Type I (chemistry, genetics)
• Humans
• Hyperostosis, Cortical, Congenital (diagnostic imaging, pathology, physiopathology)
• Models, Biological
• Molecular Sequence Data
• Mutation (genetics)
• Radiography