Tropak Michael B, Reid Stephen P, Guiral Marianne, Withers Stephen G, Mahuran Don
Research Institute, The Hospital for Sick Children, Toronto, Ontario M5G 1X8.
J Biol Chem. 2004 Apr 2;279(14):13478-87. doi: 10.1074/jbc.M308523200. Epub 2004 Jan 14.
Tay-Sachs and Sandhoff diseases are lysosomal storage disorders that result from an inherited deficiency of beta-hexosaminidase A (alphabeta). Whereas the acute forms are associated with a total absence of hexosaminidase A and early death, the chronic adult forms exist with activity and protein levels of approximately 5%, and unaffected individuals have been found with only 10% of normal levels. Surprisingly, almost all disease-associated missense mutations do not affect the active site of the enzyme but, rather, inhibit its ability to obtain and/or retain its native fold in the endoplasmic reticulum, resulting in its retention and accelerated degradation. By growing adult Tay-Sachs fibroblasts in culture medium containing known inhibitors of hexosaminidase we have raised the residual protein and activity levels of intralysosomal hexosaminidase A well above the critical 10% of normal levels. A similar effect was observed in fibroblasts from an adult Sandhoff patient. We propose that these hexosaminidase inhibitors function as pharmacological chaperones, enhancing the stability of the native conformation of the enzyme, increasing the amount of hexosaminidase A capable of exiting the endoplasmic reticulum for transport to the lysosome. Therefore, pharmacological chaperones could provide a novel approach to the treatment of adult Tay-Sachs and possibly Sandhoff diseases.
泰-萨克斯病和桑德霍夫病是溶酶体贮积症,由遗传性β-己糖胺酶A(αβ)缺乏引起。急性形式与完全缺乏己糖胺酶A及早期死亡相关,而慢性成人形式的己糖胺酶A活性和蛋白水平约为5%,且发现未受影响个体的水平仅为正常水平的10%。令人惊讶的是,几乎所有与疾病相关的错义突变并不影响该酶的活性位点,而是抑制其在内质网中获得和/或保持天然折叠的能力,导致其滞留并加速降解。通过在含有已知己糖胺酶抑制剂的培养基中培养成年泰-萨克斯病成纤维细胞,我们将溶酶体内己糖胺酶A的残余蛋白和活性水平提高到远高于正常水平的关键10%。在一名成年桑德霍夫病患者的成纤维细胞中也观察到了类似的效果。我们提出,这些己糖胺酶抑制剂起药理学伴侣的作用,增强酶天然构象的稳定性,增加能够离开内质网转运到溶酶体的己糖胺酶A的量。因此,药理学伴侣可能为成年泰-萨克斯病以及可能的桑德霍夫病提供一种新的治疗方法。