Abstract
The discovery of mutations in the gene for alpha-synuclein in familial Parkinson's disease (PD) has led to an increased interest in this pre-synaptic protein. Synphilin-1, a potential synuclein-binding protein, was cloned using yeast two-hybrid assays. The function of synphilin-1 is currently unknown, although it has been reported to be present along with alpha-synuclein in Lewy bodies in PD. In the present study, we monitored synphilin-1 aggregation directly using fusion proteins of synphilin-1 and green fluorescent protein (EGFP). Transfection of synphilin-EGFP fusion proteins formed cytoplasmic inclusions in HEK293 cells. Although these inclusions overlapped with the distribution of alpha-synuclein, they were unlike Lewy bodies in that they were not eosinophilic, and instead were membrane-bound, lipid-rich cytoplasmic inclusions.
Publication types
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Amino Acid Sequence
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Carrier Proteins / chemistry*
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Carrier Proteins / genetics
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Cell Line / chemistry
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Cell Line / ultrastructure
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Cloning, Molecular
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Cysteine Endopeptidases / metabolism
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Embryo, Mammalian
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Genes, Reporter
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Green Fluorescent Proteins
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Humans
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Inclusion Bodies / chemistry*
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Kidney
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Leupeptins / pharmacology
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Lewy Bodies / chemistry
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Lewy Bodies / ultrastructure
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Luminescent Proteins / genetics
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Molecular Sequence Data
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Multienzyme Complexes / metabolism
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Nerve Tissue Proteins / chemistry*
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Nerve Tissue Proteins / genetics
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Parkinson Disease / genetics
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Parkinson Disease / pathology
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Point Mutation
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Protease Inhibitors / pharmacology
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Proteasome Endopeptidase Complex
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Recombinant Fusion Proteins / chemistry
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Transfection
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Two-Hybrid System Techniques
Substances
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Carrier Proteins
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Leupeptins
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Luminescent Proteins
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Multienzyme Complexes
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Nerve Tissue Proteins
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Protease Inhibitors
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Recombinant Fusion Proteins
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SNCAIP protein, human
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Green Fluorescent Proteins
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Cysteine Endopeptidases
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Proteasome Endopeptidase Complex
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benzyloxycarbonylleucyl-leucyl-leucine aldehyde