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• W2077469105 abstract "To the Editor: Bullous ichthyosiform erythroderma (BCIE, MIM #113800), also known as epidermolytic hyperkeratosis (EH), is an autosomal dominant genodermatosis despite the fact that half of the cases occur sporadically as the result of a new mutation (Goldsmith, 1976Goldsmith L.A. The ichthyoses.Prog Med Genet. 1976; 1: 185-210PubMed Google Scholar). The patients show blistering and erythema at birth, which diminishes with age, and a generalized epidermolytic hyperkeratosis in adulthood (Brocq, 1902Brocq L. Erythrodermie congenitale ichthyosiforme avec hyperepidermotrophie.Ann Dermatol Syph (Paris). 1902; 4: 1-31Google Scholar). In BCIE, several point mutations have been described in highly conserved regions of the rod domain of either K1 (Chipev et al., 1992Chipev C.C. Korge B.P. Markova N. Bale S.J. DiGiovanna J.J. Compton J.G. Steinert P.M. A leucine–proline mutation in the H1 subdomain of keratin 1 causes epidermolytic hyperkeratosis.Cell. 1992; 70: 821-828Abstract Full Text PDF PubMed Scopus (244) Google Scholar) or K10 (Rothnagel et al., 1992Rothnagel J.A. Dominey A.M. Dempsey L.D. et al.Mutations in the rod domains of keratins 1 and 10 in epidermolytic hyperkeratosis.Science. 1992; 257: 1128-1130Crossref PubMed Scopus (306) Google Scholar), resulting in deleterious effects for filament assembly. Among them, Arg156 of the keratin 10, which corresponds to the residue 10 of helix initiation motif (HIM), is the most recurrent target of mutations in patients with BCIE (Rothnagel et al., 1993Rothnagel J.A. Fisher M.P. Axtell S.M. et al.A mutational hot spot in keratin 10 (KRT 10) in patients with epidermolytic hyperkeratosis.Hum Mol Genet. 1993; 2: 2147-2150Crossref PubMed Scopus (40) Google Scholar); however, there have been no reports of BCIE patients with mutations at residue 7 of the HIM in either K10 or K1. Here we report a case with a typical phenotype of BCIE caused by a novel missense mutation, which leads to a single amino acid exchange from leucine to valine at residue 7 in the HIM of K10 1A domain. The proband, a 3-y-old male, was born at full term as the first child of healthy unrelated parents who had no eruption indicative of nevoid BCIE (Figure 1a). Within a day after the birth, erythema with thick scale developed on the whole body and blisters and erosions were noticed on the hips and the flexural surface of extremities. Skin biopsy was performed and the diagnosis of BCIE was made. Neither cutaneous nor extracutaneous abnormalities were noted except for BCIE. Although the severity of skin lesions gradually decreased, hyperkeratosis with pigmentation continued and small blisters sometimes appeared on the extremities at the age of three. Histologic examination revealed the typical features of epidermolytic hyperkeratosis; vacuolization with large cytoplasmic granules in the granular layer and marked hyperkeratosis in the stratum corneum. Electron microscopy showed perinuclear clumping of keratin filaments, or deposits of clumps as large electron dense materials in the cytoplasm of keratinocytes, compatible with BCIE. For mutational analysis, genomic DNA was extracted from the peripheral blood and DNA encoding the 1A region of K10 was amplified using specific oligonucleotides, 5′-GGAAGCTATGGAAGTAGCAGCT-3′ and antisense, 5′-GCATAGTGAACAGCCACATTGTGC-3′. Direct sequencing of polymerase chain reaction products including exon 1 of KRT 10 using an ABI 310 automated sequencer revealed that the proband had a C to G transversion at nucleotide position 457 (457C→G), compared with the normal sequence (Figure 1b). This transversion resulted in substitution of a leucine (CTG) by valine (GTG) at codon 153 (L153V), which corresponded to the residue 7 of the HIM of keratin 10. The sequences from both unaffected parents showed the wild-type sequence at codon 153. The L153V mutation abolished a recognition site of the restriction enzyme AlwN I (New England BioLabs, Beverly, MA, Figure 1c). This mutation was not found in 50 normal unrelated Japanese individuals using the enzyme digestion method and was not likely to be a polymorphism (data not shown). No pathogenic mutations were detected within the helix initiation and termination motifs of keratin 1 and 10, and linker domain (L12) of keratin 10 in the patient's DNA. The L153V in the HIM of the K10 polypeptide described in the Japanese patient with typical BCIE was confirmed to be a novel mutation. This region of the keratin rod domain has been implicated in intermediate filament assembly by cell culture (Letai et al., 1992Letai A. Coulombe P.A. Fuchs E. Do the ends justify the mean? Proline mutations at the ends of the keratin coiled-coil rod segment are more disruptive than internal mutations.J Cell Biol. 1992; 116: 1181-1195Crossref PubMed Scopus (134) Google Scholar), murine transgenic studies (Vassar et al., 1991Vassar R. Coulombe P.A. Degenstein L. Albers K. Fuchs E. Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease.Cell. 1991; 64: 365-380Abstract Full Text PDF PubMed Scopus (322) Google Scholar), and chemical cross-linking analysis (Steinert et al., 1993Steinert P.M. Marekov L.N. Fraser R.D. Parry D.A. Keratin intermediate filament structure. Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly.J Mol Biol. 1993; 230: 436-452https://doi.org/10.1006/jmbi.1993.1161Crossref PubMed Scopus (232) Google Scholar). The first 15 residues of the 1A segment (KVTMQNLNDRLASYL) are highly conserved among type I keratins and thought to be involved in filament assembly through interactions with the 2B segment of neighboring molecules (Steinert et al., 1993Steinert P.M. Marekov L.N. Fraser R.D. Parry D.A. Keratin intermediate filament structure. Crosslinking studies yield quantitative information on molecular dimensions and mechanism of assembly.J Mol Biol. 1993; 230: 436-452https://doi.org/10.1006/jmbi.1993.1161Crossref PubMed Scopus (232) Google Scholar). Therefore any mutations in this conserved region are likely to be deleterious and lead to a disease phenotype. To date, 32 BCIE cases with a K10 mutation and 14 BCIE cases with a K1 mutation were reported. Among the cases with a K10 mutation, 19 cases had the mutation of Arg156 at the highly conserved residue 10 within the HIM, and this site is thought to be mutation prone; however, there have been no reports of mutations at Leu153 in BCIE that correspond to the residue 7 of the HIM. The leucine at the residue 7 of HIM is highly conserved throughout the human keratins and intermediate filaments gene and from other species. Valine is a hydrophobic amino acid possessing similar structure to leucine but shorter side-chain. The mutation from leucine to valine is pathogenic despite the fact that it is a substitution to a similar amino acid attesting the conservation and functional importance of this protein motif. In K14, a type 1 keratin expressed in the basal keratinocytes, there was one report with a mutation at residue 7 of HIM (L122F), resulting in a milder disease phenotype of epidermolysis bullosa simplex (Yamanishi et al., 1994Yamanishi K. Matsuki M. Konishi K. Yasuno H. A novel mutation of Leu122 to Phe at a highly conserved hydrophobic residue in the helix initiation motif of keratin 14 in epidermolysis bullosa simplex.Hum Mol Genet. 1994; 3: 1171-1172Crossref PubMed Scopus (27) Google Scholar). Phenylalanine is a hydrophobic amino acid similar to leucine but having a larger side chain. This case further supports the idea that the mutation at HIM residue 7 of type I keratin is pathogenic, even if the mutation is a substitution to a similar, hydrophobic residue. More cases should be accumulated to clarify the genotype-phenotype relationship of the mutation at this residue. We thank Ms Yukiko Kanzaki for technical assistance. This work was supported by Medical School Faculty and Alumni Grants to H.S. from the Keio University Medical Science Fund." @default.
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• W2077469105 title "A Novel Leucine to Valine Mutation in Residue 7 of the Helix Initiation Motif of Keratin10 Leads to Bullous Congenital Ichthyosiform Erythroderma" @default.
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