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Increased risk of developing\n PD<\/jats:styled-content>\n has been observed in both\n GD<\/jats:styled-content>\n patients and carriers. It has been estimated that\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n mutations confer a 20\u2010 to 30\u2010fold increased risk for the development of\n PD<\/jats:styled-content>\n , and that at least 7\u201310% of\n PD<\/jats:styled-content>\n patients have a\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n mutation. To date, mutations in the\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n gene constitute numerically the most important risk factor for\n PD<\/jats:styled-content>\n . The type of\n PD<\/jats:styled-content>\n associated with\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n mutations (\n PD<\/jats:styled-content>\n \u2010\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n ) is almost identical to idiopathic\n PD<\/jats:styled-content>\n , except for a slightly younger age of onset and a tendency to more cognitive impairment. Importantly, the pathology of\n PD<\/jats:styled-content>\n \u2010\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n is identical to idiopathic\n PD<\/jats:styled-content>\n , with nigral dopamine cell loss, Lewy bodies, and neurites containing alpha\u2010synuclein. The mechanism by which\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n mutations increase the risk for\n PD<\/jats:styled-content>\n is still unknown. However, given that clinical manifestation and pathological findings in\n PD<\/jats:styled-content>\n \u2010\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n patients are almost identical to those in idiopathic\n PD<\/jats:styled-content>\n individuals, it is likely that, as in idiopathic\n PD<\/jats:styled-content>\n , alpha\u2010synuclein accumulation, mitochondrial dysfunction, autophagic impairment, oxidative and endoplasmic reticulum stress may contribute to the development and progression of\n PD<\/jats:styled-content>\n \u2010\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n . Here, we review the\n \n GBA<\/jats:styled-content>\n 1\n <\/jats:italic>\n gene, its role in\n GD<\/jats:styled-content>\n , and its link with\n PD<\/jats:styled-content>\n .\n <\/jats:p>\n <\/jats:sec>\n \n \n \n \n \n image<\/jats:alt-text>\n <\/jats:graphic>\n <\/jats:boxed-text>\n The impact of glucocerebrosidase 1 (\n GBA1<\/jats:italic>\n ) mutations on functioning of endoplasmic reticulum (ER), lysosomes, and mitochondria.\n GBA1<\/jats:italic>\n mutations resulting in production of misfolded glucocerebrosidase (GCase) significantly affect the ER functioning. Misfolded GCase trapped in the ER leads to both an increase in the ubiquitin\u2013proteasome system (UPS) and the ER stress. The presence of ER stress triggers the unfolded protein response (UPR) and\/or endoplasmic reticulum\u2010associated degradation (ERAD). The prolonged activation of UPR and ERAD subsequently leads to increased apoptosis. The presence of misfolded GCase in the lysosomes together with a reduction in wild\u2010type GCase levels lead to a retardation of alpha\u2010synuclein degradation via chaperone\u2010mediated autophagy (CMA), which subsequently results in alpha\u2010synuclein accumulation and aggregation. Impaired lysosomal functioning also causes a decrease in the clearance of autophagosomes, and so their accumulation.\n GBA1<\/jats:italic>\n mutations perturb normal mitochondria functioning by increasing generation of free radical species (ROS) and decreasing adenosine triphosphate (ATP) production, oxygen consumption, and membrane potential.\n GBA1<\/jats:italic>\n mutations also lead to accumulation of dysfunctional and fragmented mitochondria.\n <\/jats:p>\n \n This article is part of a<\/jats:bold>\n special issue on Parkinson disease<\/jats:ext-link>\n .<\/jats:bold>\n <\/jats:p>\n <\/jats:sec>","DOI":"10.1111\/jnc.13385","type":"journal-article","created":{"date-parts":[[2016,2,10]],"date-time":"2016-02-10T05:55:38Z","timestamp":1455083738000},"page":"77-90","source":"Crossref","is-referenced-by-count":225,"title":["The relationship between glucocerebrosidase mutations and Parkinson disease"],"prefix":"10.1111","volume":"139","author":[{"given":"Anna","family":"Migdalska\u2010Richards","sequence":"first","affiliation":[{"name":"Department of Clinical Neurosciences UCL Institute of Neurology London UK"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Anthony H. 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