» Articles » PMID: 34757539

Glycoconjugate Journal Special Issue On: the Glycobiology of Parkinson's Disease

Overview
Journal Glycoconj J
Publisher Springer
Date 2021 Nov 10
PMID 34757539
Citations 1
Authors
Affiliations
Soon will be listed here.
Abstract

Parkinson's disease (PD) is a neurodegenerative disorder that affects over 10 million aging people worldwide. This condition is characterized by the degeneration of dopaminergic neurons in the pars compacta region of the substantia nigra (SNpc) and by aggregation of proteins, commonly α-synuclein (SNCA). The formation of Lewy bodies that encapsulate aggregated proteins in lipid vesicles is a hallmark of PD. Glycosylation of proteins and neuroinflammation are involved in the pathogenesis. SNCA has many posttranslational modifications and interacts with components of membranes that affect aggregation. The large membrane lipid dolichol accumulates in the brain upon age and has a significant effect on membrane structure. The replacement of dopamine and dopaminergic neurons are at the forefront of therapeutic development. This review examines the role of membrane lipids, glycolipids, glycoproteins and dopamine in the aggregation of SNCA and development of PD. We discuss the SNCA-dopamine-neuromelanin-dolichol axis and the role of membranes in neuronal stem cells that could be a regenerative therapy for PD patients.

Citing Articles

Protein profiling of extracellular vesicles from iPSC-derived astrocytes of patients with ALS/PDC in Kii peninsula.

Kobayashi H, Ueda K, Morimoto S, Ishikawa M, Leventoux N, Sasaki R Neurol Sci. 2023; 44(12):4511-4516.

PMID: 37615876 DOI: 10.1007/s10072-023-07000-7.

References
1.
Gai W, Yuan H, Li X, Power J, Blumbergs P, Jensen P . In situ and in vitro study of colocalization and segregation of alpha-synuclein, ubiquitin, and lipids in Lewy bodies. Exp Neurol. 2000; 166(2):324-33. DOI: 10.1006/exnr.2000.7527. View

2.
Dehay B, Bourdenx M, Gorry P, Przedborski S, Vila M, Hunot S . Targeting α-synuclein for treatment of Parkinson's disease: mechanistic and therapeutic considerations. Lancet Neurol. 2015; 14(8):855-866. PMC: 5217462. DOI: 10.1016/S1474-4422(15)00006-X. View

3.
Videira P, Castro-Caldas M . Linking Glycation and Glycosylation With Inflammation and Mitochondrial Dysfunction in Parkinson's Disease. Front Neurosci. 2018; 12:381. PMC: 5999786. DOI: 10.3389/fnins.2018.00381. View

4.
Li J, Uversky V, Fink A . Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T. Neurotoxicology. 2002; 23(4-5):553-67. DOI: 10.1016/s0161-813x(02)00066-9. View

5.
Poklar Ulrih N, Barry C, Fink A . Impact of Tyr to Ala mutations on alpha-synuclein fibrillation and structural properties. Biochim Biophys Acta. 2008; 1782(10):581-5. DOI: 10.1016/j.bbadis.2008.07.004. View