Huie M L, Tsujino S, Sklower Brooks S, Engel A, Elias E, Bonthron D T, Bessley C, Shanske S, DiMauro S, Goto Y I, Hirschhorn R
Department of Medicine, NYU Med Center, New York 10016, USA.
Biochem Biophys Res Commun. 1998 Mar 27;244(3):921-7. doi: 10.1006/bbrc.1998.8255.
Glycogen storage disease type II (GSDII), an autosomal recessive myopathic disorder, results from deficiency of lysosomal acid alpha-glucosidase. We searched for mutations in an evolutionarily conserved region in 54 patients of differing phenotype. Four novel mutations (D645N, G448S, R672W, and R672Q) and a previously described mutation (C647W) were identified in five patients and their deleterious effect on enzyme expression demonstrated in vitro. Two novel frame-shifting insertions/deletions (delta nt766-785/insC and +insG@nt2243) were identified in two patients with exon 14 mutations. The remaining three patients were either homozygous for their mutations (D645N/D645 and C647W/C647W) or carried a previously described leaky splice site mutation (IVS1-13T-->G). For all patients "in vivo" enzyme activity was consistent with clinical phenotype. Agreement of genotype with phenotype and in vitro versus in vivo enzyme was seen in three patients (two infantile patients carrying C647W/C647W and D645N/+insG@nt2243 and an adult patient heteroallelic for G648S/IVS1-13T-->G). Relative discordance was found in a juvenile patient homozygous for the non-expressing R672Q and an adult patient heterozygous for the minimally expressing R672W and delta nt766-785/+insC. Possible explanations include differences in in vitro assays vs in vivo enzyme activity, tissue specific expression with diminished enzyme expression/stability in fibroblasts vs muscle, somatic mosaicism, and modifying genes.
糖原贮积病II型(GSDII)是一种常染色体隐性遗传性肌病,由溶酶体酸性α-葡萄糖苷酶缺乏所致。我们在54例不同表型的患者中,对一个进化保守区域进行了突变筛查。在5例患者中发现了4个新突变(D645N、G448S、R672W和R672Q)以及1个先前报道的突变(C647W),并在体外证实了它们对酶表达的有害影响。在2例有外显子14突变的患者中发现了2个新的移码插入/缺失突变(δnt766 - 785/insC和+insG@nt2243)。其余3例患者要么其突变是纯合的(D645N/D645和C647W/C647W),要么携带一个先前报道的渗漏剪接位点突变(IVS1 - 13T→G)。对于所有患者,“体内”酶活性与临床表型一致。3例患者(2例携带C647W/C647W和D645N/+insG@nt2243的婴儿患者以及1例G648S/IVS1 - 13T→G杂合子的成年患者)的基因型与表型以及体外和体内酶活性相符。在1例非表达性R672Q纯合的青少年患者和1例低表达性R672W和δnt766 - 785/+insC杂合的成年患者中发现了相对不一致的情况。可能的解释包括体外检测与体内酶活性的差异、成纤维细胞与肌肉中酶表达/稳定性降低的组织特异性表达、体细胞镶嵌现象以及修饰基因。