There are six essential nutrients necessary to sustain the human body: carbohydrates, protein, fat, vitamins, minerals and water. Protein is made from amino acids. Some of the amino acids are manufactured within the body (non-essential amino acids) and some are not (essential amino acids). All amino acids are important for the body. “Essential” amino acids just means they must be obtained from our diet as the body cannot make them. But it is always good to supply all amino acids through diet so the body doesn’t have to expend the energy required to make them via backup systems. The primary system of eating them is always more efficient and effective. We have backup systems to keep us alive during times of starvation, winter and drought.
There are 22 amino acids. Nine of them have been identified as “essential.” They include histidine, isoleucine, leucine, lysine, methionine, phenylalanine, threonine, tryptophan, and valine. Arginine and tyrosine are sometimes considered to be essential because some people’s bodies don’t produce enough of it. Nutrition is not an exact science. It turns out to be very complex. For example, there are also two rare amino acids called (selenocysteine and pyrrolysine) that science didn’t even know existed until recently. Selenocysteine is a selenium-based signaling amino acid that communicates with other amino acids to inhibit the growing cycle. Pyrrolysine functions like lysine as a building block for protein.
There is no question protein is important in the body. The question is, “Do we get enough protein in our diet or do we need to supplement?” For the vast majority of people in western society, the answer is ‘we get enough in our diet.’ There is no need to supplement. Animal protein and plant protein are a staple of our diet. Plant protein is the healthiest option. Too much animal protein and dairy protein have been linked to cancer (see blog article on the China Study) and other disease processes. You can have animal protein but it needs to be eaten sparingly. Don’t let it be star of the show. It shouldn’t be the centerpiece on your plate every meal!
There was a time when scientists thought protein was the most important nutrient of them all. Protein is coded and created by our genes. The human genome project was dedicated to decoding what made the ‘king’ of nutrition. Scientists had expected over 120,000 genes to make all the different “proteins” human bodies seemed to require. It was an ironic twist of fate when they completed the decades long genome project in 2003. Humans had only a measly 20,500 genes to encode protein! The Heinz 1706 variety tomato had 31,760 genes! A tomato was 1.5 times more complicated than a human? Something was missing.
Scientists would eventually discover that carbohydrates (sugar) made all the difference for creating the vast array of “protein” needed in the body. A scientist stated it this way, “This finding that the human genome contains fewer genes than previously predicted might be compensated by combinatorial diversity generated at the level of…posttranslational modification of proteins.” Glycosylation is the most common “posttranslational modification of proteins.” 75% of all human protein is glycoprotein. After protein is created sugars are added to the protein structures. Scientists had been fixated on protein but it was the sugar attached to the protein that was differentiating them and making them biologically unique. The same exact amino acid sequence attached to different sugars act completely different in the body. The body was paying attention to sugar while the scientists were looking at protein.
Glycosylation creates glycoproteins. It is the glycans that generate the billions of different varieties in proteins necessary to account for diverse human gene expression. Scientists had never focused on sugar. They thought sugar was just for energy. They had no idea certain sugars were being used as structural sugars. What complicated the mystery was the syntheses of DNA, RNA, and proteins are all template-driven. There was a clear blueprint used to construct them. The sequence of one can generally be predicted from that of another. The genetic translation process was pretty well defined concerning how proteins are made from genes. But glycosylation, is extremely complex and it is not template-driven. It varies according to different cell types, cell age and nutrient availability. It cannot be predicted from simple rules. The cell makes these structures in real time as it needs them. It was epigenetic. This was communication above the genes. The cell was responding to it’s environment–not its DNA. It was a living thing–not a robot!
It was hypothesized that the potential sugar coding capacity (the number of unique sugar structures possible—the glycome) was somewhere between 1 x 1014 (100,000,000,000,000) and 1 x 1015 “letters.” There were between 100 trillion and 1 quadrillion possible unique patterns in this sugar-coded alphabet! This was the language/vocabulary of the immune system. It was how cells differentiated themselves from one another. The proteins could have exactly the same amino acids but be viewed by the body as radically different because of the attached sugars. These glycoprotein structures were uniquely recognized. They communicated different messages based upon the sugar patterns attached. The flag pole was protein but the flag was sugar. The antenna was made of amino acids but the attached sugars were the binding agents which allowed specific biologic processes to initiate, continue, or terminate. This was the language of life and no one had seen it and no one knew how to speak it.
Our diet is missing critical sugars not protein. This is why we focus our educational efforts on nutritional glycobiology. It isn’t the protein. Protein is important but we are not missing it in our normal diet. It is the sugar attached to the protein (the glycoprotein) that makes all the difference to health. When you study autoimmune and degenerative disease, there are always sugars missing on those glycoprotein cell receptors. Missing sugars cause miscommunication within the body and affects our immune system function. This is why the science of glycobiology is a major focus of the GRM.
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