A highly sensitive fluorescence biosensor for the detection of cytochrome c based on polydopamine nanotubes and exonuclease I amplification

2021 ◽  
Author(s):  
yanmei shen ◽  
Xueping Shen ◽  
Jia Ge ◽  
Lingbo Qu ◽  
Zhaohui Li
Keyword(s):  
Electron Transport ◽  
Cytochrome C ◽  
Cell Apoptosis ◽  
Electron Transport Chain ◽  
Mitochondrial Electron Transport Chain ◽  
Exonuclease I ◽  
Transport Chain ◽  
Highly Sensitive ◽  
Cyt C ◽  
Fluorescence Biosensor

Cytochrome c (Cyt c), as an important biomarker, plays an important role in cell apoptosis and mitochondrial electron transport chain. Here, we have developed a novel biosensor for the Cyt...

Double-edged sword in cells: chemical biology studies of the vital role of cytochrome c in the intrinsic pre-apoptotic mitochondria leakage pathway

RSC Advances ◽  
2015 ◽  
Vol 5 (36) ◽  
pp. 28258-28269 ◽  
Author(s):  
Zhi-Peng Wang ◽  
Xiao-Zhe Ding ◽  
Jun Wang ◽  
Yi-Ming Li
Keyword(s):  
Cell Death ◽  
Electron Transport ◽  
Cytochrome C ◽  
Electron Transport Chain ◽  
Chemical Biology ◽  
Vital Role ◽  
Mitochondrial Electron Transport Chain ◽  
Transport Chain ◽  
Cyt C

Besides functioning as an electron transporter in the mitochondrial electron transport chain, cytochrome c (cyt c) is also one of the determinants in the execution of cell death.

scholarly journals Cytochrome c phosphorylation: Control of mitochondrial electron transport chain flux and apoptosis

2020 ◽  
Vol 121 ◽  
pp. 105704 ◽  
Author(s):  
Hasini A. Kalpage ◽  
Junmei Wan ◽  
Paul T. Morse ◽  
Matthew P. Zurek ◽  
Alice A. Turner ◽  
...  
Keyword(s):  
Electron Transport ◽  
Cytochrome C ◽  
Electron Transport Chain ◽  
Mitochondrial Electron Transport Chain ◽  
Transport Chain

Decrease in cytochrome c oxidase reserve capacity diminishes robustness of Drosophila melanogaster and shortens lifespan

2014 ◽  
Vol 459 (1) ◽  
pp. 127-135 ◽  
Author(s):  
Vladimir Klichko ◽  
Barbara H. Sohal ◽  
Svetlana N. Radyuk ◽  
William C. Orr ◽  
Rajindar S. Sohal
Keyword(s):  
Drosophila Melanogaster ◽  
Electron Transport ◽  
Cytochrome C ◽  
Structure Function ◽  
Cytochrome C Oxidase ◽  
Electron Transport Chain ◽  
Reserve Capacity ◽  
Mitochondrial Electron Transport Chain ◽  
Transport Chain

The suppression of cytochrome c oxidase function exerts deleterious rather than benign effects on fitness and survival. The structure/function of cytochrome c oxidase, a mitochondrial electron-transport chain oxidoreductase, can be re-engineered in vivo.

Supercomplex Assembly Determines Electron Flux in the Mitochondrial Electron Transport Chain

Science ◽  
2013 ◽  
Vol 340 (6140) ◽  
pp. 1567-1570 ◽  
Author(s):  
Esther Lapuente-Brun ◽  
Raquel Moreno-Loshuertos ◽  
Rebeca Acín-Pérez ◽  
Ana Latorre-Pellicer ◽  
Carmen Colás ◽  
...  
Keyword(s):  
Electron Transport ◽  
Electron Transport Chain ◽  
Electron Flux ◽  
Fluid Model ◽  
Coenzyme Q ◽  
Mitochondrial Electron Transport Chain ◽  
C Pools ◽  
Transport Chain ◽  
Cyt C

The textbook description of mitochondrial respiratory complexes (RCs) views them as free-moving entities linked by the mobile carriers coenzyme Q (CoQ) and cytochrome c (cyt c). This model (known as the fluid model) is challenged by the proposal that all RCs except complex II can associate in supercomplexes (SCs). The proposed SCs are the respirasome (complexes I, III, and IV), complexes I and III, and complexes III and IV. The role of SCs is unclear, and their existence is debated. By genetic modulation of interactions between complexes I and III and III and IV, we show that these associations define dedicated CoQ and cyt c pools and that SC assembly is dynamic and organizes electron flux to optimize the use of available substrates.

scholarly journals AB0031 T HELPER 17 CELLS WERE SIGNIFICANTLY DECREASED BY MITOCHONDRIAL ELECTRON TRANSPORT CHAIN COMPLEX INHIBITOR IN PATIENTS WITH RHEUMATOID ARTHRITIS

2020 ◽  
Vol 79 (Suppl 1) ◽  
pp. 1318.2-1318
Author(s):  
H. R. Lee ◽  
S. J. Yoo ◽  
J. Kim ◽  
I. S. Yoo ◽  
C. K. Park ◽  
...  
Keyword(s):  
Rheumatoid Arthritis ◽  
Electron Transport ◽  
Disease Activity ◽  
Th17 Cells ◽  
Electron Transport Chain ◽  
Chain Complex ◽  
Complex Iii ◽  
Mitochondrial Electron Transport Chain ◽  
Transport Chain ◽  
Healthy Control

Background:Reactive oxygen species (ROS) and T helper 17 (TH17) cells have been known to play an important role in the pathogenesis of rheumatoid arthritis (RA). However, the interrelationship between ROS and TH17 remains unclear in RAObjectives:To explore whether ROS affect TH17 cells in peripheral blood mononuclear cells (PBMC) of RA patients, we analyzed ROS expressions among T cell subsets following treatment with mitochondrial electron transport chain complex inhibitors.Methods:Blood samples were collected from 40 RA patients and 10 healthy adult volunteers. RA activity was divided according to clinical parameter DAS28. PBMC cells were obtained from the whole blood using lymphocyte separation medium density gradient centrifugation. Following PBMC was stained with Live/Dead stain dye, cells were incubated with antibodies for CD3, CD4, CD8, and CD25. After fixation and permeabilization, samples were stained with antibodies for FoxP3 and IL-17A. MitoSox were used for mitochondrial specific staining.Results:The frequency of TH17 cells was increased by 4.83 folds in moderate disease activity group (5.1>DAS28≥3.2) of RA patients compared to healthy control. Moderate RA activity patients also showed higher ratio of TH17/Treg than healthy control (3.57 folds). All RA patients had elevated expression of mitochondrial specific ROS than healthy control. When PBMC cells were treated with 2.5uM of antimycin A (mitochondrial electron transport chain complex III inhibitor) for 16 h, the frequency of TH17 cells was significantly decreased.Conclusion:The mitochondrial electron transport chain complex III inhibitor markedly downregulated the frequency of TH17 cells in moderate disease activity patients with RA. These findings provide a novel approach to regulate TH17 function in RA through mitochondrial metabolism related ROS production.References:[1]Szekanecz, Z., et al., New insights in synovial angiogenesis. Joint Bone Spine, 2010. 77(1): p. 13-9.[2]Prevoo, M.L., et al., Modified disease activity scores that include twenty-eight-joint counts. Development and validation in a prospective longitudinal study of patients with rheumatoid arthritis. Arthritis Rheum, 1995. 38(1): p. 44-8.Disclosure of Interests:None declared

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