Establishment of stably transfected rat neuronal cell lines expressing alpha-synuclein GFP fusion proteins.

Mutations in the alpha-synuclein gene have been linked to rare cases of familial Parkinson's disease (PD). alpha-Synuclein, a 140 amino acid polypeptide, is a major component of Lewy bodies (LB), a pathological hallmark of PD. Transgenic mice, Drosophila and marmosets (Challitrix jacchus) expressing either wild type (WT) or mutant human alpha-synuclein develop motor deficits, LB-like inclusions in some neurons and neuronal degeneration.

Lysosomal pathology associated with alpha-synuclein accumulation in transgenic models using an eGFP fusion protein.

Disorders with Lewy body (LB) formation, such as Parkinson's disease (PD) and dementia with Lewy bodies (DLB), are characterized by alpha-synuclein accumulation in the neuronal cell body. Recent studies have suggested that in addition to LBs, alpha-synuclein might accumulate more widely throughout the neurons and their processes, leading to neurodegeneration and functional impairment. The precise patterns of alpha-synuclein accumulation in vivo, however, and its relationship with subcellular neuronal alterations such as lysosomal pathology are not completely clear.

Beta-Synuclein-derived peptides with neuroprotective activity: an alternative treatment of neurodegenerative disorders?

The 140-amino-acid protein alpha-synuclein (alpha-syn) is the major constituent of Lewy bodies. The protein interacts with several intracellular signal transduction pathways. Reasons for onset of abnormal aggregation of alpha-syn are unclear.

A Penicillium chrysogenum gene ( aox) identified by specific induction upon shifting pH encodes for a protein which shows high homology to fungal alcohol oxidases.

Parallel cultures of Penicillium chrysogenum were grown in controlled bioreactors under conditions of penicillin production and one was shifted from the initial pH 6.0 to pH 8.0.