The mechanisms underlying neuron death in Parkinson's disease are unknown, but both genetic defects and environmental factors are implicated in its pathogenesis. Mutations in the parkin gene lead to autosomal recessive juvenile Parkinsonism (AR-JP). Here we report that compared to control flies, Drosophila lacking parkin show significantly reduced lifespan but no difference in dopamine neuron numbers when raised on food supplemented with environmental pesticides or mitochondrial toxins. Moreover, chelation of redox-active metals, anti-oxidants and overexpression of superoxide dismutase 1 all significantly reversed the reduced longevity of parkin-deficient flies. Finally, parkin deficiency exacerbated the rough eye phenotype of Drosophila caused by overexpression of the copper importer B (Ctr1B). Taken together, our results demonstrate an important function of parkin in the protection against redox-active metals and pesticides implicated in the etiology of Parkinson's disease. They also corroborate that oxidative stress, perhaps as a consequence of mitochondrial dysfunction, is a major determinant of morbidity in parkin mutant flies.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.nbd.2010.05.011 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
2-Amidophenolate and 2-Iminosemiquinone Radical-Coordinated Vanadyl Complex as Catholyte for Non-Aqueous Redox-Flow Batteries.
Chem Asian J
January 2025
Indian Institute of Technology Guwahati, Department of Chemistry, Department of Chemistry, 781039, Guwahati, INDIA.
Fulfilment of energy demand by utilizing renewable energy sources that do not contribute to the production of greenhouse gases is a step forward in mitigating global warming. However, with the energy sources being intermittent in nature, renewable energy needs to be stored effectively on a grid scale. In this context, the development of redox-flow batteries has emerged as a promising technology where charging and discharging processes are accomplished by the redox shuttling of the electrolytes, namely anolytes and catholytes.
View Article and Find Full Text PDFA metal-organic framework with mixed electron donor and electron acceptor ligands for efficient lithium-ion storage.
Chem Commun (Camb)
January 2025
College of Chemistry, Chemical Engineering and Materials Science, Soochow University, Suzhou 215123, P. R. China.
Electron donor tetrathiafulvalene (TTF) and electron acceptor naphthalene diimide (NDI) derivatives were used to synthesize a 3D Zn-TTF/NDI-MOF. Multiple redox active sites and charge transfer endow the pristine MOF anode with excellent rate behavior and long term cycling performance (with an average specific capacity of 956 mA h g at 1 A g over 600 cycles). This study highlights the great potential of elaborately-designed MOFs for developing efficient anode materials.
View Article and Find Full Text PDFSynthesis, Physicochemical Properties, and Ion Recognition Ability of Azulene-Based Bis-(Thio)Semicarbazone.
Molecules
December 2024
"C. D. Nenitzescu" Institute of Organic and Supramolecular Chemistry, Splaiul Independentei 202B, 060023 Bucharest, Romania.
Azulene-1,3-bis(semicarbazone), , and azulene-1,3-bis(thiosemicarbazone), , were synthesized by the acid-catalyzed condensation reactions of semicarbazide and thiosemicarbazide, respectively, with azulene-1,3-dicarboxaldehyde in stoichiometric amounts. Compounds and were identified by high-resolution mass spectrometry and characterized by IR, H-NMR, C-NMR, and UV-vis spectroscopic techniques. Crystal structure determination of azulene-1,3-bis(thiosemicarbazone) shows that the thiosemicarbazone units exhibit a -closed conformation, with both arms oriented in the same direction and adopting an configuration with respect to the imine linkages.
View Article and Find Full Text PDFElectron transfer in polysaccharide monooxygenase catalysis.
Proc Natl Acad Sci U S A
January 2025
California Institute for Quantitative Biosciences, University of California, Berkeley, CA 94720.
Polysaccharide monooxygenase (PMO) catalysis involves the chemically difficult hydroxylation of unactivated C-H bonds in carbohydrates. The reaction requires reducing equivalents and will utilize either oxygen or hydrogen peroxide as a cosubstrate. Two key mechanistic questions are addressed here: 1) How does the enzyme regulate the timely and tightly controlled electron delivery to the mononuclear copper active site, especially when bound substrate occludes the active site? and 2) How does this electron delivery differ when utilizing oxygen or hydrogen peroxide as a cosubstrate? Using a computational approach, potential paths of electron transfer (ET) to the active site copper ion were identified in a representative AA9 family PMO from (PMO9E).
View Article and Find Full Text PDFRational design of redox active metal organic frameworks for mediated electron transfer of enzymes.
Mater Horiz
January 2025
Department of Material Sciences, Institute of Pure and Applied Sciences, University of Tsukuba, 1-1-1, Tennodai, Ibaraki 305-5358, Japan.
The efficient immobilization of redox mediators remains a major challenge in the design of mediated enzyme electrode platforms. In addition to stability, the ability of the redox-active material to mediate electron transfer from the active-site buried enzymes, such as flavin adenine dinucleotide-dependent glucose dehydrogenase (FADGDH) and lactate oxidase (LOx), is also crucial. Conventional immobilization techniques can be synthetically challenging, and immobilized mediators often exhibit limited durability, particularly in continuous operation.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!