Lucchiari S, Donati M A, Melis D, Filocamo M, Parini R, Bresolin N, Comi G P
Dino Ferrari Centre, Department of Neurological Sciences, University of Milan, I.R.C.C.S. Policlinico, Milan, Italy.
Hum Mutat. 2003 Oct;22(4):337. doi: 10.1002/humu.9177.
Total or partial lack of glycogen debranching enzyme (GDE or AGL, amylo-1,6-glucosidase, 4-alpha-glucanotransferase) is responsible for Glycogen Storage Disease type III (GSDIII), a rare autosomal recessive disorder of glycogen metabolism. The clinical and biochemical features of GSDIII subjects are quite heterogeneous, and this mirrors the genotype-phenotype heterogeneity among patients. In this paper, we report the molecular characterisation of five unrelated subjects, four Italian and one Tunisian. The following new mutations are described and confirm the genetic heterogeneity of this disease: p.R864X, p.R428K, c.3911 insA, p.G1087R and c.3512_3549dup+c.3512_3519del. The functional relevance of these mutations is discussed on the basis of the recently acquired knowledge about the boundaries and structures of the two catalytic domains.
糖原脱支酶（GDE或AGL，淀粉-1,6-葡萄糖苷酶，4-α-葡聚糖转移酶）的完全或部分缺乏会导致III型糖原贮积病（GSDIII），这是一种罕见的常染色体隐性糖原代谢紊乱疾病。GSDIII患者的临床和生化特征非常异质，这反映了患者之间的基因型-表型异质性。在本文中，我们报告了五名无关个体的分子特征，其中四名意大利人，一名突尼斯人。描述了以下新突变并证实了该疾病的遗传异质性：p.R864X、p.R428K、c.3911 insA、p.G1087R和c.3512_3549dup+c.3512_3519del。基于最近获得的关于两个催化结构域的边界和结构的知识，讨论了这些突变的功能相关性。
