carbocyanines has been researched along with 3-nitrotyrosine* in 1 studies
1 other study(ies) available for carbocyanines and 3-nitrotyrosine
| Article | Year |
|---|---|
Selective prion protein binding to synaptic components is modulated by oxidative and nitrosative changes induced by copper(II) and peroxynitrite in cholinergic synaptosomes, unveiling a role for calcineurin B and thioredoxin.
Choline acetyltransferase (ChAT) and choline transport are decreased after nitrosative stress. ChAT activity is altered in scrapie-infected neurons, where oxidative stress develops. Cellular prion protein (PrPc) may play a neuroprotective function in participating in the redox control of neuronal environment and regulation of copper metabolism, a role impaired when PrPc is transformed into PrPSc in prion pathologies. The complex cross-talk between PrPc and cholinergic neurons was analyzed in vitro using peroxynitrite and Cu2+ treatments on nerve endings isolated from Torpedo marmorata, a model of the motoneuron pre-synaptic element. Specific interactions between solubilized synaptic components and recombinant ovine prion protein (PrPrec) could be demonstrated by Biacore technology. Peroxynitrite abolished this interaction in a concentration-dependent way and induced significant alterations of neuronal targets. Interaction was restored by prior addition of peroxynitrite trapping agents. Cu2+ (in the form of CuSO4) treatment of synaptosomes triggered a milder oxidative effect leading to a bell-shaped increase of PrPrec binding to synaptosomal components, counteracted by the natural thiol agents, glutathione and thioredoxin. Copper(II)-induced modifications of thiols in several neuronal proteins. A positive correlation was observed between PrPrec binding and immunoreactive changes for calcineurin B and its partners, suggesting a synergy between calcineurin complex and PrP for copper regulation. Topics: 14-3-3 Proteins; Animals; Blotting, Western; Calcineurin; Carbocyanines; Choline O-Acetyltransferase; Copper Sulfate; Cyclophilin A; Cysteine; Dose-Response Relationship, Drug; Epitopes; Humans; In Vitro Techniques; Membrane Glycoproteins; Membrane Proteins; Mercaptoethanol; Nerve Tissue Proteins; Neurons; Nitrosation; Oxidation-Reduction; Peroxynitrous Acid; Prions; Protein Binding; Pyruvic Acid; Qa-SNARE Proteins; R-SNARE Proteins; Recombinant Proteins; S-Nitrosothiols; Sheep; Synapsins; Synaptic Vesicles; Synaptosomes; Tacrolimus Binding Proteins; Thioredoxins; Time Factors; Torpedo; Tyrosine; Tyrosine 3-Monooxygenase | 2003 |