TECHNOLOGY
DUAL MECHANISM OF ACTION
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RyR leaky Channel repair
Normal calcium conductance of ryanodine tetrameric channels (RyR) in highly-excitable cells such as neurons, photor ceptors or muscle cells requires the participation of FKBP12, a prolyl isomerase protein that stabilizes the closed state of RyR and facilitates the coupling between adjacent channels.
The channel
FKBP12 functions as an allosteric molecular switch, regulating RyR activity through non-covalent interactions (trans/cis isomerism).
Ryanodine receptor (RyR)-FKBP12 interaction is involved in several conditions
When FKBP12-RyR interaction fails, the risk of increased leakage of calcium from endoplasmic reticulum stores may compromise the intracellular calcium handling and, eventually, become toxic for cells.
Indeed, dysfunctional RyR-mediated calcium handling has been implicated in the pathogenesis of inherited and non inherited disorders, including:
Modulation of RyR-FKBP12 interaction as the main Mechanism of Action of MP products.
MP products are novel FKBP12 ligands designed to prevent calcium mishandling from “leaky” RyR channels when they are oxidized and dysfunctional upon certain pathological conditions.
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ROS scavenger
MP Compounds show intrinsic ROS scavening activity by reducing the formation of highly reactive deleterious species
MP products are novel FKBP12 ligands designed to prevent calcium mishandling from “leaky” RyR channels when they are oxidized and dysfunctional upon certain pathological conditions.
Through this dual mechanism of action, MP products are intended to keep the intracellular concentration of calcium below the toxic levels that usually trigger cell death, particularly in highly excitable cells which are vulnerable to imbalances of the intracellular calcium content.