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一种导致经典型佩利措伊斯-梅茨巴赫病的新型蛋白脂质蛋白1基因突变。

A novel proteolipid protein 1 gene mutation causing classical type Pelizaeus-Merzbacher disease.

作者信息

Fukumura Shinobu, Adachi Noriaki, Nagao Masayoshi, Tsutsumi Hiroyuki

机构信息

Department of Pediatrics, Sapporo Medical University School of Medicine, Sapporo, Hokkaido, Japan.

出版信息

Brain Dev. 2011 Sep;33(8):697-9. doi: 10.1016/j.braindev.2010.11.010. Epub 2010 Dec 21.

Abstract

Pelizaeus-Merzbacher disease (PMD) is a rare dysmyelinating disorder caused by mutations in the proteolipid protein 1 (PLP1) gene. PMD is generally classified according to its clinical or pathological features into classical or connatal forms. We describe here a 19-year-old male with classical form PMD who presented with stridor and nystagmus in early infancy and whose psychomotor development has been severely delayed. Brain magnetic resonance imaging revealed white matter abnormalities typical of PMD. Direct sequencing of the PLP1 gene identified two nucleotide substitutions. One was a C-to-T transition at -31 in the 5'-flanking region of exon 1; the other was a novel point mutation, T-to-C transition in exon 4, which led to substitution of cysteine for arginine at residue 184. Because Cys184 forms a disulphide bridge with Cys228, the Cys184Arg mutation probably removes the bridge and changes the tertiary structure of PLP protein. A defective disulfide bond in PLP protein could be important in the pathogenesis of PMD.

摘要

佩利措伊斯-梅茨巴赫病(PMD)是一种罕见的脱髓鞘疾病,由蛋白脂蛋白1(PLP1)基因突变引起。PMD通常根据其临床或病理特征分为经典型或先天性型。我们在此描述一名19岁的经典型PMD男性患者,他在婴儿早期出现喘鸣和眼球震颤,其精神运动发育严重延迟。脑磁共振成像显示出PMD典型的白质异常。对PLP1基因进行直接测序鉴定出两个核苷酸替代。一个是外显子1的5'侧翼区域中-31处的C到T转换;另一个是外显子4中的一个新的点突变,T到C转换,导致第184位残基处的精氨酸被半胱氨酸替代。由于Cys184与Cys228形成二硫键,Cys184Arg突变可能会消除该二硫键并改变PLP蛋白的三级结构。PLP蛋白中缺陷的二硫键可能在PMD的发病机制中起重要作用。

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