Arvio Maria, Mononen Ilkka
Päijät-Häme Social Welfare & Healthcare Joint Municipal Board, Lahti, Finland.
KTO, The Special Welfare District of Southwestern Finland, Paimio, Finland.
Orphanet J Rare Dis. 2016 Dec 1;11(1):162. doi: 10.1186/s13023-016-0544-6.
Aspartylglucosaminuria (AGU), a recessively inherited lysosomal storage disease, is the most common disorder of glycoprotein degradation with a high prevalence in the Finnish population. It is a lifelong condition affecting on the patient's appearance, cognition, adaptive skills, physical growth, personality, body structure, and health. An infantile growth spurt and development of macrocephalia associated to hernias and respiratory infections are the key signs to an early identification of AGU. Progressive intellectual and physical disability is the main symptom leading to death usually before the age of 50 years.The disease is caused by the deficient activity of the lysosomal enzyme glycosylasparaginase (aspartylglucosaminidase, AGA), which leads to a disorder in the degradation of glycoasparagines - aspartylglucosamine or other glycoconjugates with an aspartylglucosamine moiety at their reducing end - and accumulation of these undegraded glycoasparagines in tissues and body fluids. A single nucleotide change in the AGA gene resulting in a cysteine to serine substitution (C163S) in the AGA enzyme protein causes the deficiency of the glycosylasparaginase activity in the Finnish population. Homozygosity for the single nucleotide change causing the C163S mutation is responsible for 98% of the AGU cases in Finland simplifying the carrier detection and prenatal diagnosis of the disorder in the Finnish population. A mouse strain, which completely lacks the Aga activity has been generated through targeted disruption of the Aga gene in embryonic stem cells. These Aga-deficient mice share most of the clinical, histopathologic and biochemical characteristics of human AGU disease. Treatment of AGU mice with recombinant AGA resulted in rapid correction of the pathophysiologic characteristics of AGU in non-neuronal tissues of the animals. The accumulation of aspartylglucosamine was reduced by up to 40% in the brain tissue of the animals depending on the age of the animals and the therapeutic protocol. Enzyme replacement trials on human AGU patients have not been reported so far. Allogenic stem cell transplantation has not proved effective in curing AGU.
天冬氨酰葡糖胺尿症(AGU)是一种隐性遗传的溶酶体贮积病,是芬兰人群中最常见的糖蛋白降解障碍疾病。它是一种终身疾病,会影响患者的外貌、认知、适应能力、身体发育、性格、身体结构和健康。婴儿期生长突增以及与疝气和呼吸道感染相关的巨头畸形发育是早期识别AGU的关键体征。进行性智力和身体残疾是导致死亡的主要症状,通常在50岁之前。该疾病是由溶酶体酶糖基天冬酰胺酶(天冬氨酰葡糖胺酶,AGA)活性不足引起的,这导致糖天冬酰胺(天冬氨酰葡糖胺或其他在还原端带有天冬氨酰葡糖胺部分的糖缀合物)降解紊乱,并使这些未降解的糖天冬酰胺在组织和体液中蓄积。AGA基因中的单个核苷酸变化导致AGA酶蛋白中的半胱氨酸被丝氨酸取代(C163S),从而导致芬兰人群中糖基天冬酰胺酶活性缺乏。导致C163S突变的单个核苷酸变化的纯合性导致芬兰98%的AGU病例,这简化了芬兰人群中该疾病的携带者检测和产前诊断。通过在胚胎干细胞中靶向破坏Aga基因,已培育出一种完全缺乏Aga活性的小鼠品系。这些Aga缺陷小鼠具有人类AGU疾病的大多数临床、组织病理学和生化特征。用重组AGA治疗AGU小鼠可迅速纠正动物非神经组织中AGU的病理生理特征。根据动物年龄和治疗方案,动物脑组织中天冬氨酰葡糖胺的蓄积减少了多达40%。目前尚未报道对人类AGU患者进行酶替代试验。异体干细胞移植尚未证明对治愈AGU有效。