Woeste Marina A, Wachten Dagmar
Institute of Innate Immunity, University Hospital, University of Bonn, Bonn, Germany.
Molecular Physiology, Center of Advanced European Studies and Research, Minerva Max Planck Research Group, Bonn, Germany.
Front Mol Neurosci. 2017 Nov 28;10:386. doi: 10.3389/fnmol.2017.00386. eCollection 2017.
The non-lysosomal glucosylceramidase GBA2 catalyzes the hydrolysis of glucosylceramide to glucose and ceramide. Loss of GBA2 function results in accumulation of glucosylceramide. Mutations in the human gene have been associated with hereditary spastic paraplegia (HSP) and autosomal-recessive cerebellar ataxia (ARCA). Patients suffering from these disorders exhibit impaired locomotion and neurological abnormalities. mutations found in these patients have been proposed to impair GBA2 function. However, the molecular mechanism underlying the occurrence of mutations in the gene and the development of locomotor dysfunction is not well-understood. In this review, we aim to summarize recent findings regarding mutations in the gene and their impact on GBA2 function in health and disease.
非溶酶体葡糖神经酰胺酶GBA2催化葡糖神经酰胺水解为葡萄糖和神经酰胺。GBA2功能丧失会导致葡糖神经酰胺积累。人类该基因的突变与遗传性痉挛性截瘫（HSP）和常染色体隐性小脑共济失调（ARCA）有关。患有这些疾病的患者表现出运动障碍和神经异常。已提出在这些患者中发现的突变会损害GBA2功能。然而，该基因突变发生的分子机制以及运动功能障碍的发展尚未得到充分理解。在本综述中，我们旨在总结关于该基因突变及其对健康和疾病中GBA2功能影响的最新发现。
