Sugars + Proteins = Glycation

Want to feel better than you’ve ever felt?

Here’s another excerpt from my 10th book, The Secret of Vigor – How to Overcome Burnout, Restore Biochemical Balance and Reclaim Your Natural Energy

Some of the most popular New Year’s resolutions every year are:
*Lose Weight
*Get in Shape
*Reduce Stress
*Get Healthier
*Win the Lottery

The Secret of Vigor can help you with 4 out of 5 of the most popular resolution goals, so I’ll be posting excerpts from the book for the next several weeks – so please stay tuned for each installment.

If you simply can’t wait, then you can certainly get a copy at or at your favorite library or bookstore.

Sugars + Proteins = Glycation
Glycation is a process by which a sugar molecule (typically glucose or fructose) becomes bonded to a protein or lipid. Most often, glycation occurs in the body when glucose or fructose in the blood remains too high for too long and becomes bonded to cell-surface proteins. A related biochemical process called glycosylation is a very precise enzyme-controlled bonding of specific sugars to specific proteins at defined cellular sites (to help control metabolism). But compared to this precise process, glycation is actually a haphazard process that randomly adds sugars to proteins, impairing normal function and interfering with healthy cell-to-cell communication. A glycated protein—referred to as an “AGE” (advanced glycation end product)—can be highly reactive and set off a chain reaction of oxidative and inflammatory damage in whatever tissues they occur. AGEs also tend to be “cleared” from the body very slowly, so they have the potential to stimulate these chain reactions for prolonged periods of time.

Some of the main dietary offenders that lead to AGE accumulation and upset biochemical balance are high-sugar foods (such as soda, ice cream, donuts, cookies, or sugary breakfast cereals) and other foods that quickly convert to sugar or glucose in the bloodstream (like highly processed grains, such as white bread, rolls, or instant rice). Sugar can be toxic to many tissues by permanently attaching to proteins through the glycation process. Wherever sugar attaches, it triggers cellular microdamage that creates inflammation. The inflammation, in turn, produces enzymes that break down protein, thus resulting in damage to surrounding tissues.

To make matters worse, glycation also leads to cross-linking of proteins, changing healthy tissues from soft, supple, and flexible to stiff, brittle, and painful. These stiffened sugar-protein bonds form in every type of tissue, including joint cartilage, muscle tendons, brain neurons, blood vessels, skin, and even immune-system cells, which is why scientists are finding links between glycation and the chronic diseases of “aging,” such as cardiovascular disease, Alzheimer’s disease, and arthritis.

We know from Chapter 4 that inflammation in any tissue can be caused by excessive exposure to free radicals and can lead to accelerated “aging” and generalized tissue breakdown. AGEs demonstrate a “direct” problem with cell-to-cell signaling that is compromised by sugar-coated proteins. “Indirect” damage is also caused by an AGE-stimulated increase in oxidation and inflammation. Stress hormones, which we’ll discuss in the next chapter, stimulate the creation of AGEs through an increase in blood-sugar levels.

People with diabetes are obviously at high risk for developing AGEs in a wide range of tissues because of their problems regulating blood-sugar levels. The extreme development of AGEs in diabetics is a key reason for their high rates of oxidative and inflammatory diseases, including nephropathy (kidney damage) and circulatory problems (due to blood-vessel damage).

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