Saturday, April 22, 2023 10:36:06 AM
This mechanism by which misfolded proteins are cleared from the cells in the study (which are yeast cells) is similar to how, in one way, they are cleared in animal cells.
In this study, in yeast cells, the aberrant proteins are enclosed in vacuoles, which are cellular waste containers which can be excreted or dumped out of the cell. In animal cells, a similar process occurs in lysosomes. A parallel process, but with very differing organelles. Yeasts are not animals.
But, in both cases, whether vacuolar or lysosomal, these cell-keeping processes rid the cell of non-functional or pathogenic proteins, which are so because they are misfolded. Bent keys, as it were; out of shape and thereby unable to properly bind to and modulate various cell processes.
It's an autophagy phenomenon, where the cell captures and rids itself of waste or non-functioning chemicals. In this particular case it does not exactly parallel blarcamesine's ability to facilitate autophagy. Even better, blarcamesine "chaperones" the ability of endoplasmic reticula to fold proteins properly right at the start of their synthesis. No misfolded proteins are actually made when blarcamesine is active. Or, if they are, blarcamesine induces downstream autophagy that clears them in the neuron.
Blarcamesine wins.
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