Abstract
Clouston's hydrotic ectodermal dyplasia is caused by a single dose of an autosomal gene whose effects are confined to the skin and its appendages. ED hair contains more tyrosine and phenylalanine and less serine and proline than normal hair, suggesting a defect in the matrix protein. Further investigation of this protein has confirmed this hypothesis. Electrophoresis of the S-carboxymethyl derovative of the matrix protein (SCMK-B) on starch gel at pH 2.4 generates an abnormal pattern of bands. Moving boundary electrophoresis yields an abnormal peak not present in this protein fraction from normal hair, and sedimentation velocity studies at 360,000 x g show an abnormally high proportion of low molecular weight protein. Hydrolytic cystine yields suggest, and polarography confirms, that the disulphide content in ED hair is abnormally low. This corresponds with an abnormally low-S-carboxymethyl cysteine yield when the fibrillar fraction (SCMK-A) is hydrolysed. The physical and chemical properties of the mutant hair can be explained by these findings which also give considerable insight into the structure of normal keratin.
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Gold, R., Scriver, C. Demonstration of a defect in the matrix fraction of keratin in Clouston's ectodermal dysplasia. Pediatr Res 5, 421 (1971). https://doi.org/10.1203/00006450-197108000-00208
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DOI: https://doi.org/10.1203/00006450-197108000-00208