Mechanism by which the pathogenesis of Parkinson's disease is stimulated by Gaucher's mutation.

我们观察到α突触核蛋白(αS)-和P123H Βsynuclein （βS）转基因小鼠均形成轴突小球。αS-和P123H β s -球的溶酶体病理相似，氧化应激与αS-球相关，与P123H β s -球相关程度较低。其他病理，如线粒体改变和LRRK2积累，仅检测α - s球。总的来说，αS-和P123H β s -球是通过相似但不同的致病机制形成的。

We observed that axonal globules are formed in both αsynuclein (αS)- and P123H Βsynuclein (βS) transgenic mice. Lysosomal pathology was similarly observed for both αS- and P123H βS-globules, while oxidative stress was associated with the αS-globules, and to a lesser extent with the P123H βS-globules. Other pathologies, such as mitochondrial alteration and LRRK2 accumulation, were exclusively detected for αS-globules. Collectively, both αS- and P123H βS-globules were formed through similar but distinct pathogenic mechanisms.