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• W2091239256 abstract "To the Editor: Dystrophic epidermolysis bullosa (DEB) is caused by mutations in the COL7A1 gene encoding collagen VII (Uitto and Christiano, 1994Uitto J. Christiano A.M. Molecular basis for the dystrophic forms of epidermolysis bullosa: mutations in the type VII collagen gene.Arch Dermatol Res. 1994; 287: 16-22Crossref PubMed Scopus (93) Google Scholar;Hovnanian et al., 1997Hovnanian A. Rochat A. Bodemer C. et al.Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation.Am J Human Genet. 1997; 61: 599-610Abstract Full Text PDF PubMed Scopus (123) Google Scholar;Hammami-Hauasli et al., 1998bHammami-Hauasli N. Schumann H. Raghunath M. Kilgus O. Luthi U. Luger T. Bruckner-Tuderman L. Some but not all glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils and skin blister.J Biol Chem. 1998; 273: 19228-19234Crossref PubMed Scopus (62) Google Scholar), the major component of anchoring fibrils. In autosomal dominant and recessive DEB, different phenotypes are caused by heterozygous, compound heterozygous, or homozygous mutations in COL7A1. Premature termination codon mutations in both alleles lead to the most severe phenotype, the Hallopeau-Siemens subtype, with lack of expression of collagen VII (Uitto and Christiano, 1994Uitto J. Christiano A.M. Molecular basis for the dystrophic forms of epidermolysis bullosa: mutations in the type VII collagen gene.Arch Dermatol Res. 1994; 287: 16-22Crossref PubMed Scopus (93) Google Scholar;Hovnanian et al., 1997Hovnanian A. Rochat A. Bodemer C. et al.Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation.Am J Human Genet. 1997; 61: 599-610Abstract Full Text PDF PubMed Scopus (123) Google Scholar). Among the different mutations, substitution of a glycine residue in the triple helical collagenous domain by other, bulkier amino acids present a biologically intriguing situation. Glycine substitutions associated with dominant DEB interfere with folding and secretion of collagen VII in a dominant negative manner (Christiano and Uitto, 1996Christiano A.M. Uitto J. Molecular complexity of the cutaneous basement membrane zone. Revelations from the paradigms of epidermolysis bullosa.Exp Dermatol. 1996; 5: 1-11Crossref PubMed Scopus (177) Google Scholar;Hammami-Hauasli et al., 1998bHammami-Hauasli N. Schumann H. Raghunath M. Kilgus O. Luthi U. Luger T. Bruckner-Tuderman L. Some but not all glycine substitution mutations in COL7A1 result in intracellular accumulation of collagen VII, loss of anchoring fibrils and skin blister.J Biol Chem. 1998; 273: 19228-19234Crossref PubMed Scopus (62) Google Scholar); however, when combined with a normal allele, certain heterozygous glycine substitutions do not interfere with the biosynthesis of collagen VII in this way and thus do not lead to a clinical phenotype (Christiano et al., 1996Christiano A.M. McGrath J.A. Tan K.C. Uitto J. Glycine substitutions in the triple-helical region of type VII collagen result in a spectrum of dystrophic epidermolysis bullosa phenotypes and patterns of inheritance.Am J Hum Genet. 1996; 58: 671-681PubMed Google Scholar;Shimizu et al., 1996Shimizu H. McGrath J.A. Christiano A.M. Nishikawa T. Uitto J. Molecular basis of recessive dystrophic epidermolysis bullosa: genotype/phenotype correlation in a case of moderate clinical severity.J Invest Dermatol. 1996; 106: 119-124Crossref PubMed Scopus (76) Google Scholar;Hovnanian et al., 1997Hovnanian A. Rochat A. Bodemer C. et al.Characterization of 18 new mutations in COL7A1 in recessive dystrophic epidermolysis bullosa provides evidence for distinct molecular mechanisms underlying defective anchoring fibril formation.Am J Human Genet. 1997; 61: 599-610Abstract Full Text PDF PubMed Scopus (123) Google Scholar). These mutations were termed silent glycine substitutions. Combination of the silent glycine substitutions and different COL7A1 mutations in the other allele have been shown to lead to various DEB phenotypes (Shimizu et al., 1996Shimizu H. McGrath J.A. Christiano A.M. Nishikawa T. Uitto J. Molecular basis of recessive dystrophic epidermolysis bullosa: genotype/phenotype correlation in a case of moderate clinical severity.J Invest Dermatol. 1996; 106: 119-124Crossref PubMed Scopus (76) Google Scholar;Hammami-Hauasli et al., 1998aHammami-Hauasli N. Raghunath M. Koter W. Bruckner-Tuderman L. Transient bullous dermolysis of the newborn associated with compound heterozygosity for recessive and dominant COL7A1 mutations.J Invest Dermatol. 1998; 111: 1214-1219Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar;Terracina et al., 1998Terracina M. Posteraro P. Schubert M. et al.Compound heterozygosity for a recessive glycine substitution and a splice site mutation in the COL7A1 gene causes an unusually mild form of localized recessive dystrophic epidermolysis bullosa.J Invest Dermatol. 1998; 111: 744-750Abstract Full Text Full Text PDF PubMed Scopus (35) Google Scholar). In this study, we explored the molecular basis of unusual DEB phenotype similar to transient bullous dermolysis of the newborn (TBDN) (Hashimoto et al., 1985Hashimoto K. Matsumoto M. Iacobelli D. Transient bullous dermolysis of the newborn.Arch Dermatol. 1985; 121: 1429-1438Crossref PubMed Scopus (56) Google Scholar). The proband, a 10-year-old girl was born in September 1988 as the second child of nonconsanguineous healthy parents of Japanese ethnic origin as described previously (Hatta et al., 1995Hatta N. Takata M. Shimizu H. Spontaneous disappearance of intraepidermal type VII collagen in a patient with dystrophic epidermolysis bullosa.Br J Dermatol. 1995; 133: 619-624Crossref PubMed Scopus (15) Google Scholar). At birth she presented with blisters on the entire integument and on mucous membranes. Although the severity of the skin condition has slightly decreased, the blister formation and deformities of the nails have continued since then. At the age of 10, she had large scarring and ulcerated plaques and lost all her nails, and deformity of the left toes had developed (Figure 1a–e). In order to study the expression and processing of procollagen VII in the patient’s skin at the age of 3 d, 4 y, and 10 y, we used three domain specific antibodies for indirect immunofluorescence staining. Antibodies against the NC-1 (Leigh et al., 1987Leigh I.M. Purkis P.E. Bruckner-Tuderman L. L.H. 2 monoclonal antibody detects type VII collagen in the sublamina densa zone of ectodermally-derived epithelia, including skin.Epithelia. 1987; 1: 17-29Google Scholar) and the triple-helical domain (Bruckner-Tuderman et al., 1987Bruckner-Tuderman L. Schnyder U.W. Winterhalter K.H. Bruckner P. Tissue form of type VII collagen from human skin and dermal fibroblasts in culture.Eur J Biochem. 1987; 165: 607-611Crossref PubMed Scopus (77) Google Scholar) recognize both procollagen VII and mature collagen VII. In contrast, antibodies against the carboxyterminal NC-2 domain (Bruckner-Tuderman et al., 1995Bruckner-Tuderman L. Nilssen O. Zimmermann D.R. Dours Zimmermann M.T. Kalinke D.U. Gedde Dahl Jr, T. Winberg J.O. Immunohistochemical and mutation analyses demonstrate that procollagen VII is processed to collagen VII through removal of the NC-2 domain.J Cell Biol. 1995; 131: 551-559Crossref PubMed Scopus (123) Google Scholar) react only with procollagen VII, which has not yet been processed to mature collagen. At 3 d of age, abundant intracytoplasmic accumulation and weak linear BMZ distribution of collagen VII was observed in the proband’s skin with antibodies to the NC-1 domain and to the triple helical domain. While BMZ was negative with antibodies to the NC-2 domain, the abundant intracytoplasmically retained material was clearly positive, indicating that most of the accumulating molecules were immature procollagen VII still possessing the NC-2 domain (Figure 2). In the skin at the age 4 y and 10 y, bright linear labeling with antibodies to the NC-1 and the triple helical domains was seen along BMZ. In addition, infrequent punctuate labeling within the epidermis was positive with antibody to NC-2 domain, indicating that this corresponded to residual accumulation of procollagen VII (Figure 2). For mutation detection, genomic DNA from the patient and her family members (Figure 3) were subjected to polymerase chain reaction amplification and heteroduplex analysis and dideoxynucleotide sequencing. The mutation screening identified a heterozygous 6946G→A transition in exon 89 and a heterozygous 6859G→A transition in exon 87 (Figure 3). Both transitions substitute Arg for Gly and were designated as G2316R and G2287R. The paternal mutation G2316R, also found in the sister’s DNA, created a Mae I site (Figure 3d,left). The maternal mutation G2287R eliminated an Ava II site (Figure 3d,right). These sequence variations in exons 87 and 89 were not found in 150 normal chromosomes, indicating that they did not represent neutral polymorphisms. Screening of the entire coding sequence and of all intron-exon borders of the COL7A1 gene (Christiano et al., 1997aChristiano A.M. Hoffman G.G. Zhang X. Xu Y. Tamai Y. Greenspan D.S. Uitto J. Strategy for identification of sequence variants in COL7A1 and a novel 2-bp deletion mutation in recessive dystrophic epidermolysis bullosa.Human Mut. 1997; 10: 408-414Crossref PubMed Scopus (94) Google Scholar) (L23982) did not reveal other nucleotide variations predicting changes in collagen VII polypeptide sequence. Although the mother was described as clinically unaffected according to the previous report (Hatta et al., 1995Hatta N. Takata M. Shimizu H. Spontaneous disappearance of intraepidermal type VII collagen in a patient with dystrophic epidermolysis bullosa.Br J Dermatol. 1995; 133: 619-624Crossref PubMed Scopus (15) Google Scholar), careful clinical re-examination of all the family members disclosed the presence of mild nail dystrophy restricted to both big toes, without skin fragility, only in individuals heterozygous for G2287R. These included the mother (Figure 1g: no. 4 in Figure 3), the maternal uncle (Figure 1h: no. 5 in Figure 3), and the maternal grandmother (Figure 1i: no. 6 in Figure 3) of the index patient. Other family members without the G2287R mutation did not show any sings of nail deformities or skin fragility. Therefore, G2287R was interpreted as a dominantly inherited glycine substitution mutation leading to a very mild phenotype, which was overlooked at the time of the previous case report of this patient (Hatta et al., 1995Hatta N. Takata M. Shimizu H. Spontaneous disappearance of intraepidermal type VII collagen in a patient with dystrophic epidermolysis bullosa.Br J Dermatol. 1995; 133: 619-624Crossref PubMed Scopus (15) Google Scholar). Individuals carrying the paternal mutation G2316R were clinically unaffected. Recently we identified another dominant glycine substitution mutation in COL7A1, G2251E, which caused only toe nail dystrophy but not skin blistering when combined with a normal allele (Hammami-Hauasli et al., 1998aHammami-Hauasli N. Raghunath M. Koter W. Bruckner-Tuderman L. Transient bullous dermolysis of the newborn associated with compound heterozygosity for recessive and dominant COL7A1 mutations.J Invest Dermatol. 1998; 111: 1214-1219Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar); however, when compound heterozygous with another silent glycine substitution in the daughter of the index patient, the mutation led to an extensive TBDN phenotype at birth. These results suggest the possibility that some individuals who have been diagnosed as suffering from idiopathic toe nail dystrophy of unknown origin without skin fragility, might have been carriers of certain glycine substitution mutations of COL7A1, such as G2251E or G2287R. There are only two previously reported cases with TBDN in which molecular defects have been identified. One is a COL7A1 splice site mutation in a TBDN child in a family with a dominant pedigree (Christiano et al., 1997aChristiano A.M. Hoffman G.G. Zhang X. Xu Y. Tamai Y. Greenspan D.S. Uitto J. Strategy for identification of sequence variants in COL7A1 and a novel 2-bp deletion mutation in recessive dystrophic epidermolysis bullosa.Human Mut. 1997; 10: 408-414Crossref PubMed Scopus (94) Google Scholar). The second case is a combination of silent glycine substitution (G1519D) and dominant glycine substitution mutations (G2251E) (Hammami-Hauasli et al., 1998aHammami-Hauasli N. Raghunath M. Koter W. Bruckner-Tuderman L. Transient bullous dermolysis of the newborn associated with compound heterozygosity for recessive and dominant COL7A1 mutations.J Invest Dermatol. 1998; 111: 1214-1219Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar), a similar constellation as seen in the present proband. The morphologic hallmark of TBDN, marked transient accumulation of procollagen VII might represent mutant, slowly secreted collagen VII molecules in postnatal skin where the rate of collagen synthesis is high. Accordingly, transitory blistering in TBDN has possibly more to do with the quantity rather than quality of the abnormal collagen VII molecules. Interestingly, the cessation of blister formation in TBDN roughly coincides with a reduction in the biosynthesis rate and the normalization of collagen VII deposition at the dermo–epidermal junction, which is likely to indicate deposition of sufficiently functional anchoring fibrils (Hammami-Hauasli et al., 1998aHammami-Hauasli N. Raghunath M. Koter W. Bruckner-Tuderman L. Transient bullous dermolysis of the newborn associated with compound heterozygosity for recessive and dominant COL7A1 mutations.J Invest Dermatol. 1998; 111: 1214-1219Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar). Although a combination of silent and dominant glycine substitution mutations was also found in the above case with TBDN (Hammami-Hauasli et al., 1998aHammami-Hauasli N. Raghunath M. Koter W. Bruckner-Tuderman L. Transient bullous dermolysis of the newborn associated with compound heterozygosity for recessive and dominant COL7A1 mutations.J Invest Dermatol. 1998; 111: 1214-1219Abstract Full Text Full Text PDF PubMed Scopus (59) Google Scholar), this is the first case in which these combinations were shown to be associated with a moderately severe classical DEB phenotype with marked transient epidermal retention of procollagen VII at birth. We thank Ms. Yuriko Kanzaki and Ms. Margit Schubert for technical assistance. This work was supported by Grants-in-Aid for Scientific Research (Nos.05404036 and 07457191) from the Ministry of Education, Science, and Culture of Japan, by Keio Gijuku Academic Development Funds to H.S. and by grant Nr. Br 1475/2–3 from the German Research Council (DFG) and by a grant from DEBRA U.K. to L. B.-T." @default.
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• W2091239256 title "Compound Heterozygosity for Silent and Dominant Glycine Substitution Mutations in COL7A1 Leads to a Marked Transient Intracytoplasmic Retention of Procollagen VII and a Moderately Severe Dystrophic Epidermolysis Bullosa Phenotype" @default.
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