Journal
BIOLOGICAL CHEMISTRY
Volume 394, Issue 7, Pages 807-818Publisher
WALTER DE GRUYTER GMBH
DOI: 10.1515/hsz-2012-0322
Keywords
alpha-synuclein; Gaucher disease; GBA1; glycolipid; lysosome; Parkinson's disease
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Funding
- National Research Foundation
- Korean Government (MEST) [2010-0015188]
- Ministry of Health & Welfare, Republic of Korea [A111228]
- Korea Health Promotion Institute [A111228] Funding Source: Korea Institute of Science & Technology Information (KISTI), National Science & Technology Information Service (NTIS)
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Mutations in the gene encoding glucocerebrosidase (GBA1) cause Gaucher disease (GD), a lysosomal storage disease with recessive inheritance. Glucocerebrosidase (GCase) is a lysosomal lipid hydrolase that digests glycolipid substrates, such as glucosylceramide and glucosylsphingosine. GBA1 mutations have been implicated in Lewy body diseases (LBDs), such as Parkinson's disease and dementia with Lewy bodies. Parkinsonism occurs more frequently in certain types of GD, and GBA1 mutation carriers are more likely to have LBDs than non-carriers. Furthermore, GCase is often found in Lewy bodies, which are composed of alpha-synuclein fibrils as well as a variety of proteins and vesicles. In this review, we discuss potential mechanisms of action of GBA1 mutations in LBDs with particular emphasis on alpha-synuclein aggregation by reviewing the current literature on the role of GCase in lysosomal functions and glycolipid metabolism.
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