{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Schechter M"],"funding":["National Institute of Neurological Disorders and Stroke","NIA NIH HHS","Israel Science Foundation","NINDS NIH HHS","National Institute on Aging"],"pagination":["24"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC7104492"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["15(1)"],"pubmed_abstract":["<h4>Background</h4>α-Synuclein (α-Syn) is a protein implicated in the pathogenesis of Parkinson's disease (PD). α-Syn has been shown to associate with membranes and bind acidic phospholipids. However, the physiological importance of these associations to the integrity of axons is not fully clear.<h4>Methods</h4>Biochemical, immunohistochemical and ultrastructural analyses in cultured neurons, transgenic mouse brains, PD and control human brains.<h4>Results</h4>We analyzed the ultrastructure of cross-sectioned axons localized to white matter tracts (WMTs), within the dorsal striatum of old and symptomatic α-Syn transgenic mouse brains. The analysis indicated a higher density of axons of thinner diameter. Our findings in cultured cortical neurons indicate a role for α-Syn in elongation of th"],"journal":["Molecular neurodegeneration"],"pubmed_title":["A role for α-Synuclein in axon growth and its implications in corticostriatal glutamatergic plasticity in Parkinson's disease."],"pmcid":["PMC7104492"],"funding_grant_id":["U24 NS072026","P30 AG019610","P30 AG19610","182/12"],"pubmed_authors":["Grigoletto J","Glickstein H","Beach TG","Serrano GE","Abd-Elhadi S","Sharon R","Friedman A","Schechter M"],"additional_accession":[]},"is_claimable":false,"name":"A role for α-Synuclein in axon growth and its implications in corticostriatal glutamatergic plasticity in Parkinson's disease.","description":"<h4>Background</h4>α-Synuclein (α-Syn) is a protein implicated in the pathogenesis of Parkinson's disease (PD). α-Syn has been shown to associate with membranes and bind acidic phospholipids. However, the physiological importance of these associations to the integrity of axons is not fully clear.<h4>Methods</h4>Biochemical, immunohistochemical and ultrastructural analyses in cultured neurons, transgenic mouse brains, PD and control human brains.<h4>Results</h4>We analyzed the ultrastructure of cross-sectioned axons localized to white matter tracts (WMTs), within the dorsal striatum of old and symptomatic α-Syn transgenic mouse brains. The analysis indicated a higher density of axons of thinner diameter. Our findings in cultured cortical neurons indicate a role for α-Syn in elongation of th","dates":{"release":"2020-01-01T00:00:00Z","publication":"2020 Mar","modification":"2025-04-18T11:48:55.576Z","creation":"2020-05-22T15:35:54Z"},"accession":"S-EPMC7104492","cross_references":{"pubmed":["32228705"],"doi":["10.1186/s13024-020-00370-y"]}}