The DOI matches its Crossref record; 9 of the 9 references it cites were found in a registry or an index.
Functional Consequences of α-Synuclein Tyrosine Nitration
Open accessAbstract
Previous studies have shown the presence of nitrated alpha-synuclein (alpha-syn) in human Lewy bodies and other alpha-syn inclusions. Herein, the effects of tyrosine nitration on alpha-syn fibril formation, lipid binding, chaperone-like function, and proteolytic degradation were systematically examined by employing chromatographically isolated nitrated monomeric, dimeric, and oligomeric alpha-syn. Nitrated alpha-syn monomers and dimers but not oligomers accelerated the rate of fibril formation of unmodified alpha-syn when present at low concentrations. Immunoelectron microscopy revealed that nitrated monomers and dimers are incorporated into the fibrils. However, the purified nitrated alpha-syn monomer by itself was unable to form fibrils. Nitration of the tyrosine residue at position 39 was largely responsible for decreased binding of nitrated monomeric alpha-syn to synthetic vesicles, which correlated with an impairment of the nitrated protein to adopt alpha-helical conformation in the presence of liposomes. The chaperone-like activity of alpha-syn was not inhibited by nitration or oxidation. Furthermore, the 20 S proteasome and calpain I degraded nitrated monomeric alpha-syn, although at a slower rate compared with control alpha-syn. Collectively, these data suggest that post-translational modification of alpha-syn by nitration can promote the formation of intracytoplasmic inclusions that constitute the hallmark of Parkinson disease and other synucleinopathies.
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Self-citationProteasomal function is impaired in substantia nigra in Parkinson’s disease
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Cytochrome c Nitration by Peroxynitrite
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-Synuclein in Parkinson's Disease
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Oxidative Stress and Neurotoxicity
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Metadata
- Authors
- Hodara, R., Norris, E. H., Giasson, B. I., Mishizen-Eberz, A. J., Lynch, D. R., Lee, V. M.-Y., & Ischiropoulos, H.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2004-11
- Volume
- 279
- Issue
- 46
- Pages
- 47746-47753
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1969366577
- Cited by
- 286
- References
- 9
- FWCI
- 5.91
- Type
- journal article
- Language
- en
- Open access
- hybrid
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