Keratin 9 gene mutations in five Korean families with epidermolytic palmoplantar keratoderma
| Autor: | Joo-Heung Lee, Dong-Youn Lee, Seong-Jae Youn, Jong Wook Kim, Peter M. Steinert, Jun-Mo Yang, Eil-Soo Lee, Kwang-Sung Ahn, Cha-Hui Lee |
|---|---|
| Rok vydání: | 2003 |
| Předmět: |
Adult
Male Adolescent Hyperkeratosis Dermatology Gene mutation Biology medicine.disease_cause Biochemistry Keratoderma Palmoplantar Keratin medicine Humans Intermediate Filament Protein Child Keratoderma Molecular Biology Family Health chemistry.chemical_classification Genetics Hyperkeratosis Epidermolytic Mutation Epidermolytic Palmoplantar Keratoderma Korea Autosomal dominant trait DNA medicine.disease Pedigree Protein Structure Tertiary chemistry Keratins Female Peptides Dimerization |
| Zdroj: | Experimental Dermatology. 12:876-881 |
| ISSN: | 1600-0625 0906-6705 |
| DOI: | 10.1111/j.0906-6705.2003.00012.x |
| Popis: | Epidermolytic palmoplantar keratoderma (EPPK) is an autosomal dominant disease characterized clinically by localized palmoplantar thickening and histopathologically by granular degeneration of the epidermis. Recent molecular biological studies have revealed that EPPK is caused by mutations of the keratin 9 gene in sequences mainly encoding the highly conserved 1 A rod domain. Here we demonstrate a novel mutation of N160H (position 8 of the 1 A domain) and two other previously reported mutations, R162W and N160S, in five unrelated Korean families with EPPK. The three-dimensional structure of the 1 A domain of the related vimentin intermediate filament protein chain is now known. Based on its likely similarity to the keratin 9 chain, we predict that inappropriate amino acid substitutions in position 10 of 1 A will likely interfere with coiled-coil dimer stability, and those in position 8 will interfere with tetramer stability. Accordingly, these mutations compromise the structural integrity of the keratin intermediate filaments leading to the pathology of EPPK. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|