Glucagon, the more obscure of the hormonal sisters, is the dieter's friend. Glucagon is a protein molecule made up of a configuration of twenty-nine amino acids, including threonine, methionine, leucine, tryptophan, glycine, valine, tyrosine, and other essential and nonessential amino acids. (Vegetarian diets are low in some of these critical amino acids.)3 While insulin is secreted into the bloodstream from the beta cells in the pancreas in response to high levels of blood sugars, glucagon is secreted from the alpha cells in the pancreas in response to low levels of blood sugar.

Glucagon pulls stored sugars out of storage, first from the liver and then from adipose or fat tissue as it converts fatty tissue back into glucose. The very presence of insulin in the bloodstream suppresses the release of glucagon, as does the ratio of carbohydrates to proteins in a meal. The greater the carbohydrate content of a meal, the more insulin will be secreted and the less glucagon will be secreted, tipping the scales in favor of fat storage through the dominating effect of insulin.4 Conversely, the lower the carbohydrate content of the meal (or more accurately, the more balanced the meal among proteins, carbohydrates, and fats), the less insulin is secreted in favor of glucagon release.

Glucagon is stimulated by exercise and a number of amino acids, but it is primarily stimulated by a diet that is fairly low in carbohydrates and a little higher in proteins and fats than many of us are accustomed to eating. In other words, by our unwitting dietary choices, we are underutilizing this "friend of the dieter" in favor of glucagon's more aggressive sister, insulin.


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