Home > Publications Database > SWATH Mass Spectrometry-Based CSF Proteome Profile of GBA-Linked Parkinson's Disease Patients. > print

001     165626
005     20240722121855.0
024 7 _ |a pmc:PMC9699576
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024 7 _ |a 10.3390/ijms232214166
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024 7 _ |a pmid:36430645
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024 7 _ |a 1422-0067
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024 7 _ |a 1661-6596
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037 _ _ |a DZNE-2022-01759
041 _ _ |a English
082 _ _ |a 540
100 1 _ |a Zafar, Saima
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245 _ _ |a SWATH Mass Spectrometry-Based CSF Proteome Profile of GBA-Linked Parkinson's Disease Patients.
260 _ _ |a Basel
|c 2022
|b Molecular Diversity Preservation International
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520 _ _ |a β-glucocerebrosidase (GBA)-associated mutations are a significant risk factor for Parkinson's disease (PD) that aggravate the disease pathology by upregulating the deposition of α-Synuclein (α-Syn). The resultant clinical profile varies for PD patients without GBA mutations. The current study aimed to identify the proteomic targets involved in the pathogenic pathways leading to the differential clinical presentation of GBA-associated PD. CSF samples (n = 32) were obtained from PD patients with GBA mutations (n = 22), PD patients without GBA mutations (n = 7), and healthy controls that were carriers of GBA mutations (n = 3). All samples were subjected to in-gel tryptic digestion followed by the construction of the spectral library and quantitative SWATH-based analysis. CSF α-Syn levels were reduced in both PDIdiopathic and PDGBA cases. Our SWATH-based mass spectrometric analysis detected 363 proteins involved in immune response, stress response, and cell signaling in various groups. Intergroup analysis showed that 52 proteins were significantly up- or downregulated in various groups. Of these 52 targets, 20 proteins were significantly altered in PDGBA cases only while 2 showed different levels in PDIdiopathic patients. Our results show that the levels of several pathologically relevant proteins, including Contactin-1, Selenium-binding protein 1, Adhesion G Protein-Coupled Receptor, and Apolipoprotein E are significantly different among the sporadic and genetic variants of PD and hint at aggravated synaptic damage, oxidative stress, neuronal loss, and aggregation of α-Syn in PDGBA cases.
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650 _ 7 |a α-synuclein
|2 Other
650 _ 7 |a CSF
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650 _ 7 |a SWATH
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650 _ 7 |a proteomics
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650 _ 7 |a α-synuclein
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650 _ 7 |a β-glucocerebrosidase
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650 _ 7 |a Glucosylceramidase
|0 EC 3.2.1.45
|2 NLM Chemicals
650 _ 7 |a Proteome
|2 NLM Chemicals
650 _ 7 |a β-glucocerebrosidase
|2 Other
650 _ 2 |a Glucosylceramidase: metabolism
|2 MeSH
650 _ 2 |a Humans
|2 MeSH
650 _ 2 |a Glucosylceramidase: genetics
|2 MeSH
650 _ 2 |a Proteome
|2 MeSH
650 _ 2 |a Parkinson Disease: genetics
|2 MeSH
650 _ 2 |a Proteomics
|2 MeSH
650 _ 2 |a Mass Spectrometry
|2 MeSH
650 _ 2 |a Parkinson Disease: metabolism
|2 MeSH
650 _ 2 |a Cerebrospinal Fluid: chemistry
|2 MeSH
650 _ 2 |a Cerebrospinal Fluid: metabolism
|2 MeSH
700 1 _ |a Noor, Aneeqa
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700 1 _ |a Younas, Neelam
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700 1 _ |a Shafiq, Mohsin
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700 1 _ |a Schmitz, Matthias
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700 1 _ |a Wurster, Isabel
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700 1 _ |a Brockmann, Kathrin
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700 1 _ |a Gasser, Thomas
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700 1 _ |a Zerr, Inga
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770 _ _ |a Mechanisms and Interventions for Neurological and Psychological Disorders 2.0
773 _ _ |a 10.3390/ijms232214166
|g Vol. 23, no. 22, p. 14166 -
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