The new vision of mitochondrial permeability transition pore opening
نویسندگان
چکیده
Mitochondria play a fundamental role in the functioning of body but are also responsible for dysfunction, apoptosis, and death, associated with mPTP (mitochondrial permeability transition pore) opening. Despite fact that there many articles on this topic, none them solve problem PTP identification. The opening is elicited by matrix Ca2+ stimulated binding cyclophilin D (CyPD), Pi, elevated concentration reactive oxygen species (ROS), free fatty acids, or diminished transmembrane potential. Nucleotides, Mg2+, (cyclosporin A) CsA known molecular inhibitors opening, whereas arginine-specific adducts phenylglyoxal modulate net-charge-dependent manner. It seems to us reason unresolved lies ignorance ATP synthase. According our mechano-chemiosmotic mechanism we suggest synthase two channels connected, consisting c-ring Fо and, α3β3-hexamer cap oligomycin sensitivity conferring protein (OSCP) subunit F1 mitochondria closing c-ring. In opinion, OSCP together act as an analogue adenine nucleotide translocase (ANT), which can be designated F1-ANT. exchanges synthesized 3-ATP molecules active center 3-ADP from participation sodium magnesium ions. Thus, conclude both ANT membrane F1-ANT (OSCP α3β3-hexamer) complex jointly involved mPTP.
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ژورنال
عنوان ژورنال: World Journal Of Advanced Research and Reviews
سال: 2023
ISSN: ['2581-9615']
DOI: https://doi.org/10.30574/wjarr.2023.18.2.0913