Pelletier-Galarneau 2021 Curr Cardiol Rep: Difference between revisions
No edit summary |
No edit summary Β |
||
Line 10: | Line 10: | ||
|editor=Gnaiger E | |editor=Gnaiger E | ||
}} | }} | ||
[[File:Pelletier-Galarneau 2021 Curr Cardiol Rep CORRECTION.png|right| | [[File:Pelletier-Galarneau 2021 Curr Cardiol Rep CORRECTION.png|right|300px]] | ||
{{Template:Correction FADH2 and S-pathway}} | {{Template:Correction FADH2 and S-pathway}} | ||
{{Labeling | {{Labeling | ||
|enzymes=Complex II;succinate dehydrogenase | |enzymes=Complex II;succinate dehydrogenase | ||
}} | }} |
Latest revision as of 12:15, 15 October 2023
Pelletier-Galarneau M, Detmer FJ, Petibon Y, Normandin M, Ma C, Alpert NM, El Fakhri G (2021) Quantification of myocardial mitochondrial membrane potential using PET. Curr Cardiol Rep 23:70. https://doi.org/10.1007/s11886-021-01500-8 |
Pelletier-Galarneau M, Detmer FJ, Petibon Y, Normandin M, Ma C, Alpert NM, El Fakhri G (2021) Curr Cardiol Rep
Abstract: Purpose of review: To present a method enabling in vivo quantification of tissue membrane potential (ΞΞ¨T), a proxy of mitochondrial membrane potential (ΞΞ¨m), to review the origin and role of ΞΞ¨m, and to highlight potential applications of myocardial ΞΞ¨T imaging.
Recent findings: Radiolabelled lipophilic cations have been used for decades to measure ΞΞ¨m in vitro. Using similar compounds labeled with positron emitters and appropriate compartment modeling, this technique now allows in vivo quantification of ΞΞ¨T with positron emission tomography. Studies have confirmed the feasibility of measuring myocardial ΞΞ¨T in both animals and humans. In addition, ΞΞ¨T showed very low variability among healthy subjects, suggesting that this method could allow detection of relatively small pathological changes. In vivo assessment of myocardial ΞΞ¨T provides a new tool to study the pathophysiology of cardiovascular diseases and has the potential to serve as a new biomarker to assess disease stage, prognosis, and response to therapy.
β’ Bioblast editor: Gnaiger E
Correction: FADH2 and Complex II
- FADH2 is shown as the substrate feeding electrons into Complex II (CII). This is wrong and requires correction - for details see Gnaiger (2024).
- Gnaiger E (2024) Complex II ambiguities β FADH2 in the electron transfer system. J Biol Chem 300:105470. https://doi.org/10.1016/j.jbc.2023.105470 - Β»Bioblast linkΒ«
Labels:
Enzyme: Complex II;succinate dehydrogenase