No evidence for substrate accumulation in Parkinson brains with GBA mutations. Issue 8 (11th June 2015)

• Record Type: Journal Article
• Authors: Gegg, Matthew E.; Sweet, Lindsay; Wang, Bing H.; Shihabuddin, Lamya S.; Sardi, Sergio Pablo; Schapira, Anthony H.V.
• Is Part Of: Movement disorders. Volume 30:Issue 8(2015)
• Page Start: 1085
• Page End: 1089
• Publication Date: 2015-06-11
• Subjects: Movement disorders -- Periodicals; 610
• DOI: 10.1002/mds.26278
• Languages: English
• ISSNs: 0885-3185

Abstract

<abstract abstract-type="main"> <title>Abstract</title> <sec id="mds26278-sec-0101" sec-type="section"> <title>Background</title> <p>To establish whether Parkinson's disease (PD) brains previously described to have decreased glucocerebrosidase activity exhibit accumulation of the lysosomal enzyme's substrate, glucosylceramide, or other changes in lipid composition.</p> </sec> <sec id="mds26278-sec-1001" sec-type="section"> <title>Methods</title> <p>Lipidomic analyses and cholesterol measurements were performed on the putamen (n = 5‐7) and cerebellum (n = 7‐14) of controls, Parkinson's disease brains with heterozygote <italic>GBA1</italic> mutations (PD+GBA), or sporadic PD.</p> </sec> <sec id="mds26278-sec-2001" sec-type="section"> <title>Results</title> <p>Total glucosylceramide levels were unchanged in both PD+GBA and sporadic PD brains when compared with controls. No changes in glucosylsphingosine (deacetylated glucosylceramide), sphingomyelin, gangliosides (GM2, GM3), or total cholesterol were observed in either putamen or cerebellum.</p> </sec> <sec id="mds26278-sec-3001" sec-type="section"> <title>Conclusions</title> <p>This study did not demonstrate glucocerebrosidase substrate accumulation in PD brains with heterozygote <italic>GBA1</italic> mutations in areas of the brain with low α‐synuclein pathology. © 2015 The Authors. Movement Disorders published by Wiley Periodicals, Inc. on behalf of International Parkinson and Movement Disorder Society.</p> </sec> </abstract>