AI Article Synopsis
- The researchers used RNA interference (RNAi) plasmids and α-synuclein-pEGFP recombinant plasmids to study α-synuclein in HEK293 cells, observing protein aggregation in the cytoplasm and nucleus.
- Transfected cells showed Lewy body-like inclusions when using the α-synuclein-pEGFP plasmid, while RNAi transfection prevented these inclusions from forming.
- Although RNAi stopped the formation of these inclusions, it did not alter the way wild-type α-synuclein localized with mitochondria.
Article Abstract
The specific and effective α-synuclein RNA interference (RNAi) plasmids, and the α-synuclein-pEGFP recombinant plasmids were co-transfected into human embryonic kidney 293 (HEK293) cells using the lipofectamine method. Using an inverted fluorescence microscope, α-synuclein proteins were observed to aggregate in the cytoplasm and nucleus. Wild-type α-synuclein proteins co-localized with mitochondria. Hematoxylin-eosin staining revealed round eosinophilic bodies (Lewy body-like inclusions) in the cytoplasm of some cells transfected with α-synuclein-pEGFP plasmid. However, the formation of Lewy body-like inclusions was not observed following transfection with the RNAi pSYN-1 plasmid. RNAi blocked Lewy body-like inclusions in the cytoplasm of HEK293 cells induced by wild-type α-synuclein overexpression, but RNAi did not affect the subcellular localization of wild-type α-synuclein in mitochondria.
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| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4354134 | PMC |
| http://dx.doi.org/10.3969/j.issn.1673-5374.2012.02.001 | DOI Listing |
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