By Peter Beighton MD, PhD, FRCP, FRCPCH, FRSSA, Rodney Grahame CBE, MD, FRCP, FACP, Howard Bird MA, MD, FRCP (auth.)
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Extra info for Hypermobility of Joints
With age, elastin changes as well as collagen. Above the age of 45 years, a glycoprotein becomes closely bound to elastin, producing a more brittle complex that is more readily cleaved chemically. Most studies on the tensile properties of collagen have been carried out on tendons in the tails of rats, which can be easily freed from secondary tissue. There is little slack to take up, and the shapes of the load/extension curves of collagen bundles are almost independent on the number of fibres which they contain.
The multidomain functionality of collagens is dramatically demonstrated in comparing the effects of mutations in different parts of the gene or protein. Mutations in type I collagen genes that alter the repeating Gly-X-Y structure of the triple helix affect the ability of the collagen to undergo normal mineralisation during bone formation (reviewed by Culbert et al. 1995). Conversely, as described below, mutations that alter the N-propeptide of type I collagen have a major effect on the mobility of joints.
Hatched box, the major triple helical, Gly-X- Y domain of the chain. Fibrillar Collagen Types I and V in the Ehlers-Danlos Syndrome 25 and skin. Type V collagen is a minor component of several tissues where it occurs as heterotypic fibrils with type I collagen. In particular, type V collagen is thought to form the inner core of collagen fibrils comprising type I collagen in cornea, skin and ligaments. The abundance of type I/V heterotypic fibrils explains, in part, why mutations in these genes result in joint hypermobility in people with certain types of EDS.