Full length α-synuclein is present in cerebrospinal fluid from Parkinson's disease and normal subjects

R Borghi, R Marchese, A Negro, L Marinelli… - Neuroscience …, 2000 - Elsevier
R Borghi, R Marchese, A Negro, L Marinelli, G Forloni, D Zaccheo, G Abbruzzese
Neuroscience letters, 2000Elsevier
Several clues suggest that α-synuclein, a presynaptic protein, plays a central role in the
pathogenesis of idiopathic Parkinson's disease (PD). To search a peripheral marker of PD,
we analyzed presence and amount of α-synuclein in CSF from 12 PD patients and 10
neurologically normal subjects. The protein was extracted from CSF samples through
immunoprecipitation and immunoblotting with different specific anti-α-synuclein antibodies.
We identified a 19 kDa band that corresponds to monomeric α-synuclein, given its …
Several clues suggest that α-synuclein, a presynaptic protein, plays a central role in the pathogenesis of idiopathic Parkinson's disease (PD). To search a peripheral marker of PD, we analyzed presence and amount of α-synuclein in CSF from 12 PD patients and 10 neurologically normal subjects. The protein was extracted from CSF samples through immunoprecipitation and immunoblotting with different specific anti-α-synuclein antibodies. We identified a 19 kDa band that corresponds to monomeric α-synuclein, given its comigration with homologue human recombinant peptide as well as with the protein extracted from cerebral cortex of normal subjects. The amount of CSF 19 kDa α-synuclein did not significantly vary in PD and normal cases. These findings have two implications: (a) full length α-synuclein is released by neurons in the extracellular space; (b) α-synuclein does not appear a peripheral marker of PD pathology.
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