Monday, June 21, 2021 3:35:23 PM
tRNAs grab specific amino acids floating in the cytosol, the fluid inside the cell, and transfer it to the ribosome, where peptides, protein fractions are synthesized. No one appears to claim that tRNAs are involved in blarcamesine-modulated function. So, we'll leave tRNAs out of the picture.
mRNAs carry genetic messages (hence, "messenger RNA") from the DNA in chromosomes also out to the ribosomes, which align the mRNAs in proper sequence inside the extremely complex ribosomes. The ribosomes then bond the amino acids, end to end, creating a peptide. The peptides are connected, making a crude protein. Then (crucially) the crude proteins are moved to the endoplasmic reticula where they are carefully folded and locked into shape.
Of course, that's a major problem in central nervous system diseases. Most of the proteins being made are enzymes, which in a lock-and-key arrangement cause desired chemical reactions to proceed. If the enzyme proteins are mis-folded, they can't control any biochemical reactions. Such is the case with Alzheimer's and beta-amyloid waste protein accumulations (causing Alzheimer's symptoms). The enzymes that normally clear those wastes no longer do. They are mis-shaped. By its facilitated activation of the sigma-1 receptor, blarcamesine allows the neuron to, once again, fold proteins (enzymes) properly. The protein wastes that cause Alzheimer's symptoms are, once again, functionally cleared.
But in all of that, I don't see where there is any direct blarcamesine/mRNA interaction. Blarcamesine also apparently facilitates the enzymatic processing of chromatin, histone proteins that safely package and protect DNA in the cell. The chromatin has to be chemically pealed away so that mRNA can take the genetic message in the genes in the DNA out to the ribosomes. So, in that regard, blarcamesine is helpful.
Is it accurate to think that blarcamesine works in multitude of complex ways? Very much so.
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