Parkin is metabolized by the ubiquitin/proteosome system. Neuroreport 2000 Aug 21;11(12):2635-8
Date
09/08/2000Pubmed ID
10976934DOI
10.1097/00001756-200008210-00006Scopus ID
2-s2.0-0034698945 (requires institutional sign-in at Scopus site) 46 CitationsAbstract
Mutations in the parkin gene cause autosomal recessive juvenile parkinsonism. Immunostaining of substantia nigra sections from sporadic Parkinson's disease (PD) cases shows that Parkin accumulates in axonal spheroids and in some Lewy bodies. Because ubiquitin is a major component of Lewy bodies and axonal spheroids, we investigated whether Parkin is metabolized via the ubiquitin/proteosomal pathway. Treatment of BE-M17 neuroblastoma cells with the proteosomal inhibitor, MG132, produced a band corresponding to di-ubiquitinated Parkin that was apparent by immunoblot using two different anti-Parkin antibodies. This higher mol. wt band also co-immunoprecipitated with Parkin. These data suggest that Parkin plays a role in the pathophysiology of sporadic PD, and that Parkin is a substrate for ubiquitination that is degraded by the proteosomal complex.
Author List
Choi P, Ostrerova-Golts N, Sparkman D, Cochran E, Lee JM, Wolozin BMESH terms used to index this publication - Major topics in bold
AgedAntibodies
Cysteine Endopeptidases
Humans
Immunoblotting
Immunohistochemistry
Leupeptins
Ligases
Middle Aged
Multienzyme Complexes
Parkinson Disease
Precipitin Tests
Proteasome Endopeptidase Complex
Reference Values
Substantia Nigra
Substrate Specificity
Tumor Cells, Cultured
Ubiquitin-Protein Ligases
Ubiquitins