Grewal Prabhjit K, Hewitt Jane E
Institute of Genetics, Queen's Medical Centre, The University of Nottingham, UK.
Biochim Biophys Acta. 2002 Dec 19;1573(3):216-24. doi: 10.1016/s0304-4165(02)00387-2.
The myodystrophy (myd) mutation arose spontaneously and has an autosomal recessive mode of inheritance. Homozygous mutant mice display a severe, progressive muscular dystrophy. Using a positional cloning approach, we identified the causative mutation in myd as a deletion within the Large gene, which encodes a putative glycosyltransferase with two predicted catalytic domains. By immunoblotting, the alpha-subunit of dystroglycan, a key muscle membrane protein, is abnormal in myd mice. This aberrant protein might represent altered glycosylation of the protein and contribute to the muscular dystrophy phenotype. Our results are discussed in the light of recent reports describing mutations in other glycosyltransferase genes in several forms of human muscular dystrophy.
肌营养不良(myd)突变是自发产生的,具有常染色体隐性遗传模式。纯合突变小鼠表现出严重的、进行性的肌肉营养不良。我们采用定位克隆方法,确定myd的致病突变是Large基因内的一个缺失,该基因编码一种具有两个预测催化结构域的假定糖基转移酶。通过免疫印迹法发现,肌营养不良蛋白聚糖的α亚基(一种关键的肌膜蛋白)在myd小鼠中异常。这种异常蛋白可能代表该蛋白糖基化改变,并导致肌肉营养不良表型。我们结合最近关于几种人类肌肉营养不良症中其他糖基转移酶基因突变的报道对结果进行了讨论。