Lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) are mutated in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to chromosome 17p13.1
| Autor: | Ayşen Karaduman, Florence Jobard, Judith Fischer, Jean Weissenbach, Claudine Blanchet-Bardon, Mark Lathrop, Meral Özgüç, Caroline Lefèvre, Serap Emre, Jean-François Prud'homme |
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| Přispěvatelé: | Deri ve Zührevi Hastalıkları |
| Rok vydání: | 2002 |
| Předmět: |
Male
Biochemistry & Molecular Biology Congenital ichthyosiform erythroderma Genotype DNA Mutational Analysis Lipoxygenase Molecular Sequence Data ALOX12B Biology medicine.disease_cause Polymerase Chain Reaction Linkage Disequilibrium ALOXE3 CYP4F22 Congenital ichthyosis Genetics medicine Humans ABCA12 Child Molecular Biology Genetics (clinical) DNA Primers Genetics & Heredity Mutation General Medicine Ichthyosiform Erythroderma Congenital medicine.disease Pedigree Chromosome 17 (human) Phenotype Haplotypes Child Preschool biology.protein Female Chromosomes Human Pair 17 Microsatellite Repeats |
| Zdroj: | Scopus-Elsevier |
| ISSN: | 1460-2083 |
| Popis: | We report the identification of mutations in lipoxygenase-3 (ALOXE3) and 12(R)-lipoxygenase (ALOX12B) genes in non-bullous congenital ichthyosiform erythroderma (NCIE) linked to chromosome 17. Linkage disequilibrium analysis of six families affected by NCIE permitted us to reduce a recently reported interval of 8.4 cM on chromosome 17p13.1 to a 600 kb region around the marker D17S1796, which contains LOX genes. LOX products have long been implicated in skin disorders. Two point mutations and one deletion were found in ALOXE3 and three point mutations were found in ALOX12B in these consanguineous families from the Mediterranean basin. ALOXE3 and ALOX12B are two genes which are physically linked and functionally related. They are separated by 38 kb, have one more exon than the other LOX genes and are mainly expressed in epithelial cells including keratinocytes. Although the main substrate(s) of the two enzymes is (are) still unknown, the products of ALOX12B obtained in experimental systems have been demonstrated to be of R-chirality. It seems likely that the product of one of these enzymes may be the substrate of the other, and that they belong to the same metabolic pathway. |
| Databáze: | OpenAIRE |
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