Article
In vivo and in vitro noncovalent association of excised alpha 1 (I) amino-terminal propeptides with mutant pN alpha 2(I) collagen chains in native mutant collagen in a case of Ehlers-Danlos syndrome, type VII.
The Journal of biological chemistry - 15 Apr 1990
Wirtz M K, Keene D R, Hori H, Glanville R W, Steinmann B, Rao V H, Hollister D W
Abstract excerpt
The cause of the Ehlers-Danlos syndrome Type VII (EDS VII) is considered to be defective removal of the amino-terminal propeptide (N-propeptide) of Type I procollagen due to deficiency of procollagen N-proteinase, the enzyme responsible for the normal proteolytic excision of this precursor-specific domain. Molecules retaining the N-propeptide (pN-collagen molecules) are thought to cause defective fibrillogenesis...
Topics
- Amino Acid Sequence
- Amino Acids
- Blotting, Western
- Collagen
- Ehlers-Danlos Syndrome
- Fibroblasts
- Humans
- Macromolecular Substances
- Microscopy, Electron
- Models, Structural