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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)

X-linked cutis laxa: defective cross-link formation in collagen due to decreased lysyl oxidase activity.

We studied several members of a family with an X-linked form of cutis laxa; the affected males have mild skin laxity, a characteristic facies, skeletal abnormalities, structural abnormalities of the genitourinary tract, and low serum copper levels. The activity of lysyl oxidase, a copper-dependent enzyme involved in cross-link formation in collagen, was decreased in skin-biopsy specimens (13 to 26 per cent of normal) and in culture medium from cells to two affected males (15 to 20 per cent of normal). Immunoreactive lysyl oxidase from skin of both patients was virtually undetectable by immunodiffusion assay. The amounts of lysyl-derived aldehydes (the product formed in collagen and elastin by lysyl oxidase) and of cross-links formed from these products were decreased in dermal fibroblasts in culture. Collagen extractability from these cells was increased in culture. These findings suggest that lysyl oxidase deficiency provides the biochemical basis of the X-linked form of cutis laxa.[1]


  1. X-linked cutis laxa: defective cross-link formation in collagen due to decreased lysyl oxidase activity. Byers, P.H., Siegel, R.C., Holbrook, K.A., Narayanan, A.S., Bornstein, P., Hall, J.G. N. Engl. J. Med. (1980) [Pubmed]
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