Hatsell S J, Eady R A, Wennerstrand L, Dopping-Hepenstal P, Leigh I M, Munro C, Kelsell D P
Center for Cutaneous Research, St. Bartholomews, and the Royal London School of Medicine and Dentistry, Queen Mary College, London, UK.
J Invest Dermatol. 2001 Apr;116(4):606-9. doi: 10.1046/j.1523-1747.2001.13041234.x.
We report a novel mutation in the exon 6 splice donor site of keratin 1 (G4134A) that segregates with a palmoplantar keratoderma in three kindreds. The nucleotide substitution leads to the utilization of a novel in-frame splice site 54 bases downstream of the mutation with the subsequent insertion of 18 amino acids into the 2B rod domain. This mutation appears to have a milder effect than previously described mutations in the helix initiation and termination sequence on the function of the rod domain, with regard to filament assembly and stability. Affected individuals displayed only mild focal epidermolysis in the spinous layer of palmoplantar epidermis, in comparison with cases of bullous congenital ichthyosiform erythroderma also due to keratin 1 mutations, which show widespread and severe epidermolysis. This study describes a novel mutation in KRT1 that results in a phenotype distinct from classical bullous congenital ichthyosiform erythroderma.
我们报告了角蛋白1外显子6剪接供体位点的一个新突变（G4134A），该突变在三个家族中与掌跖角化病共分离。核苷酸替换导致在突变下游54个碱基处使用一个新的框内剪接位点，随后在2B杆状结构域插入18个氨基酸。就细丝组装和稳定性而言，该突变对角蛋白杆状结构域功能的影响似乎比先前在螺旋起始和终止序列中描述的突变更为轻微。与同样由角蛋白1突变引起的大疱性先天性鱼鳞病样红皮病病例相比，受影响个体仅在掌跖表皮棘层表现出轻度局灶性表皮松解，后者表现为广泛而严重的表皮松解。本研究描述了KRT1中的一种新突变，该突变导致了一种不同于经典大疱性先天性鱼鳞病样红皮病的表型。
