Molecular defects in the Ehlers-Danlos syndrome.

Abstract

Several abnormalities in collagen biosynthesis have been described in patients with Ehlers-Danlos syndrome. Examples of collagen structural mutations as well as post-translational enzymatic defects have been detected. Patients with hydroxylysine-deficient collagen disease (Ehlers-Danlos type VI) have diminished lysyl hydroxylase activity. One mutant enzyme has been characterized which is thermally labile and had an altered affinity for ascorbate. Another mutant enzyme had a normal requirement for cofactors but activity was diminished. Type VII Ehlers-Danlos syndrome is associated with altered processing of procollagen to collagen. Most often the disorder is associated with deficient procollagen aminoprotease activity. One patient appears to represent a structural mutation of pro alpha 2 (I) resulting in incomplete cleavage of the amino terminal propeptide. One family with x-linked Ehlers-Danlos syndrome (type V) has been described with altered lysyl oxidase activity. Other patients with this disorder have had normal lysyl oxidase activity. The ecchymotic form of Ehlers-Danlos syndrome (type IV) has defective type III collagen-synthesis. Patients have been described with absent synthesis, diminished synthesis and diminished secretion.

• Authors: S R Pinnell
• Journal: The Journal of investigative dermatology (J Invest Dermatol) Vol. 79 Suppl 1 Pg. 90s-92s (Jul 1982) ISSN: 0022-202X [Print] United States
• PMID: 7086195 (Publication Type: Journal Article, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• Hydroxylysine
• Collagen

Topics

• Collagen (biosynthesis)
• Ehlers-Danlos Syndrome (diagnosis, genetics, metabolism)
• Female
• Humans
• Hydroxylysine (deficiency)
• Male