Burwinkel B, Bakker H D, Herschkovitz E, Moses S W, Shin Y S, Kilimann M W
Institut für Physiologische Chemie, Ruhr-Universität Bochum, Bochum, Germany.
Am J Hum Genet. 1998 Apr;62(4):785-91. doi: 10.1086/301790.
Deficiency of glycogen phosphorylase in the liver gives rise to glycogen-storage disease type VI (Hers disease; MIM 232700). We report the identification of the first mutations in PYGL, the gene encoding the liver isoform of glycogen phosphorylase, in three patients with Hers disease. These are two splice-site mutations and two missense mutations. A mutation of the 5' splice-site consensus of intron 14 causes the retention of intron 14 and the utilization of two illegitimate 5' splice sites, whereas a mutation of the 3' splice-site consensus of intron 4 causes the skipping of exon 5. Two missense mutations, N338S and N376K, both cause nonconservative replacements of amino acids that are absolutely conserved even in yeast and bacterial phosphorylases. We also report corrections of the PYGL coding sequence, sequence polymorphisms, and a partial PYGL gene structure with introns in the same positions as in PYGM, the gene of the muscle isoform of phosphorylase. Our findings demonstrate that PYGL mutations cause Hers disease, and they may improve laboratory diagnosis of deficiencies of the liver phosphorylase system.
肝脏中糖原磷酸化酶的缺乏会导致VI型糖原贮积病(赫斯病;MIM 232700)。我们报告了在三名赫斯病患者中首次鉴定出编码糖原磷酸化酶肝脏同工型的基因PYGL中的突变。这些是两个剪接位点突变和两个错义突变。内含子14的5'剪接位点共有序列突变导致内含子14保留,并利用了两个异常的5'剪接位点,而内含子4的3'剪接位点共有序列突变导致外显子5缺失。两个错义突变N338S和N376K均导致氨基酸的非保守替换,这些氨基酸即使在酵母和细菌磷酸化酶中也是绝对保守的。我们还报告了PYGL编码序列的校正、序列多态性以及部分PYGL基因结构,其内含子与磷酸化酶肌肉同工型基因PYGM中的内含子位于相同位置。我们的研究结果表明,PYGL突变会导致赫斯病,并且可能会改善肝脏磷酸化酶系统缺陷的实验室诊断。