Dolichols, Glycoproteins, Statins

Whether to be bound to a cell surface or destined to be secreted, proteins, those magic particles so important to our function and destiny, are synthesized within the membranes of the endoplasmic reticulum (ER), a tubular marvel of complexity within each of our cells.

It is within this microscopic structure that amino acids are linked together into a popcorn string-like peptide. Some peptides will ultimately serve for cell identification so they may wander about our immune system without being challenged; others produce insulin because our blood sugar is rising or make us fall in love because of the attractive qualities of that person to us.

This class of proteins contains a signal as a recipe to guide the ER assembly of our necessary peptide, thereby matching our immediate needs.

This entire process is orchestrated by dolichols in the form of dolichol phosphate. In terms of chain of command, I cannot tell you who issues the command for a certain peptide, for that is beyond our understanding at this time, but the command once given is carried out by dolichol, the executive officer of this amazing process. We are dealing with a factory producing a substance, assembly-line fashion, under an administration process familiar to any production line facility.

In case you have not already suspected, this peptide assembly process is greatly influenced by statin drug use. The inevitability of dolichol inhibition secondary to reductase blocking of our mevalonate pathway by Statins has been known to drug company biochemists from the very beginning of this multi-billion dollar industry but ignored almost completely by everyone else.

Even physicians get a smattering of this in medical school biochemistry but all memory is usually lost by the time of graduation. Drug company management must have known of this problem to come for dolichol's role in our glycolysis and glycoprotein formation has been studied for many years and is well known to researchers in the field.

During the assembly of the peptide strand within the ER, sugars are added thereby converting the product into glycoproteins. The usual sugars found in glycoproteins are glucose, galactose, mannose, fucose, N-acetyl galactosamine, N-acetyl glucosamine and N-acetyl neuraminic acid. The most frequently found sugar in this process is mannose. Their purpose is to broaden the versatility of the evolving protein structure by designating points and direction of protein folding, in this field of study, structure is function.

The final role depends on the protein structure. Just using proteins can give hundreds of options but the addition of these sugars to the protein strand gives tens of thousands of structural options. It is this almost unlimited range of structural options that gives humans our tremendous range of behavioral and emotional reactions. This process, too, is orchestrated by dolichols in its preparation of the final protein structure.

This dolichol-mediated process is involved in neuropeptide formation and cell communication, cell identification and immune system functions. This complex role is such that almost anything can be expected when dolichols are deficient. Altered emotional and behavioral reactions associated with statin use are likely explained by altered neuropeptide formation.

The reality of dolichol inhibition by Statins is thoroughly documented. The role of dolichols in the process of glycoprotein synthesis is also thoroughly documented. I have used the Indiana University School of Medicine information base to help prepare this page.

Duane Graveline MD MPH
Former USAF Flight Surgeon
Former NASA Astronaut
Retired Family Doctor

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