Ryoo Y W, Kim B C, Lee K S
Department of Dermatology, Keimyung University School of Medicine, 194 Dong San Dong, Joong-Gu, 700-712, Taegu, South Korea.
J Dermatol Sci. 2001 Jun;26(2):125-32. doi: 10.1016/s0923-1811(00)00168-7.
In recent years, the molecular basis for the main subtypes of epidermolysis bullosa (EB) has been elucidated with pathogenetic mutations delineated in ten different genes encoding structural components of the dermal-epidermal junction. Both the autosomal dominant and recessive forms of dystrophic EB (DEB) is caused by mutations in the COL7A1 gene. Type VII collagen is a major component of anchoring fibrils, structural elements that stabilize the attachment of the basement membrane to underlying dermis. Recent delineation of the exon-intron organization of the COL7A1 gene provided the basis for the comprehensive design of PCR primer pairs that amplified exons in genomic DNA by placing the primers on the flanking introns. A number of COL7A1 mutations have been reported and some genotype-phenotype correlations are starting to emerge. In this study, we examined mutational analyses from three Korean patients with recessive dystrophic EB (RDEB) mitis. We designed and optimized primers according to the previously reported sequences. Such PCR amplification products can be examined by electrophoretic scanning technique, CSGE heteroduplex analyses. Utilizing heteroduplex analyses, we have identified a number of sequence variants in COL7A1 both in unaffected individuals and in patients with M-RDEB. Mutation detection of the COL7A1 gene revealed six allelic mutations (V6677E, P6685S, Y3749S, P6084S, P6695R and G6697C). We suggest that the full length of type VII collagen polypeptide are synthesized, but those missense mutations, that may affect a critical amino acid, can alter the conformation of the protein and interferes with the assembly and packing of type VII collagen molecules into anchoring fibrils. Immunohistochemical study of skin biopsies by use of anti-type VII collagen antibody showed markedly reduced staining and presence of a dermo/epidermal cleavage. This is the first report of a COL7A1 mutation study in DEB from Korean patients. We hope that these data contribute to the expanding database on COL7A1 mutations in dystrophic epidermolysis bullosa, and further illustrate the extensive diversity of mutational events that led to the RDEB phenotype.
近年来,大疱性表皮松解症(EB)主要亚型的分子基础已被阐明,在编码真皮 - 表皮连接结构成分的10个不同基因中确定了致病突变。常染色体显性和隐性营养不良性EB(DEB)均由COL7A1基因突变引起。VII型胶原蛋白是锚定原纤维的主要成分,锚定原纤维是稳定基底膜与下方真皮附着的结构元件。最近对COL7A1基因外显子 - 内含子组织的描述为PCR引物对的全面设计提供了基础,这些引物对通过将引物置于侧翼内含子上,在基因组DNA中扩增外显子。已经报道了许多COL7A1突变,并且一些基因型 - 表型相关性开始显现。在本研究中,我们检查了三名韩国轻型隐性营养不良性EB(RDEB)患者的突变分析。我们根据先前报道的序列设计并优化了引物。此类PCR扩增产物可通过电泳扫描技术、CSGE异源双链分析进行检测。利用异源双链分析,我们在未受影响的个体和M - RDEB患者中均鉴定出COL7A1中的一些序列变异。COL7A1基因的突变检测揭示了六个等位基因突变(V6677E、P6685S、Y3749S、P6084S、P6695R和G6697C)。我们认为VII型胶原蛋白多肽全长被合成,但那些可能影响关键氨基酸的错义突变可改变蛋白质的构象,并干扰VII型胶原蛋白分子组装和包装成锚定原纤维。使用抗VII型胶原蛋白抗体对皮肤活检进行免疫组织化学研究显示染色明显减少且存在真皮/表皮分离。这是韩国患者DEB中COL7A1突变研究的首次报告。我们希望这些数据有助于扩大营养不良性大疱性表皮松解症中COL7A1突变的数据库,并进一步说明导致RDEB表型的突变事件的广泛多样性。