Mutations in the Rod Domains of Keratins 1 and 10 in Epidermolytic Hyperkeratosis
| Autor: | Mary A. Longley, Dennis R. Roop, Marcel Huber, T. A. Gagne, Edgar Frenk, Andrea M. Dominey, Daniel Hohl, L. D. Dempsey, Joseph A. Rothnagel, David A. Greenhalgh |
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| Rok vydání: | 1992 |
| Předmět: |
Macromolecular Substances
Protein Conformation Molecular Sequence Data macromolecular substances Biology medicine.disease_cause Polymerase Chain Reaction Epidermolytic hyperkeratosis Type II keratin Keratin medicine Humans Amino Acid Sequence Genetics chemistry.chemical_classification Mutation Epidermolytic Palmoplantar Keratoderma Multidisciplinary Base Sequence integumentary system DNA Keratin 6A Ichthyosiform Erythroderma Congenital Keratin 1 medicine.disease Ichthyosis bullosa of Siemens Pedigree Cell biology chemistry Keratins |
| Zdroj: | Science. 257:1128-1130 |
| ISSN: | 1095-9203 0036-8075 |
| DOI: | 10.1126/science.257.5073.1128 |
| Popis: | Epidermolytic hyperkeratosis is a hereditary skin disorder characterized by blistering and a marked thickening of the stratum corneum. In one family, affected individuals exhibited a mutation in the highly conserved carboxyl terminal of the rod domain of keratin 1. In two other families, affected individuals had mutations in the highly conserved amino terminal of the rod domain of keratin 10. Structural analysis of these mutations predicts that heterodimer formation would be unaffected, although filament assembly and elongation would be severely compromised. These data imply that an intact keratin intermediate filament network is required for the maintenance of both cellular and tissue integrity. |
| Databáze: | OpenAIRE |
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