You must have JavaScript enabled in your browser to utilize the functionality of this website. The alpha cell is responsible for a variety of stimuli that signal actual or potential hypoglycemia.
A study by Calbet and colleagues (2002) was conducted to find whether the hormonal response to feeding with protein solutions is influenced by the nature and degree of protein fractionation. Rocha and colleagues (1972) studied the effects of 20 amino acids on pancreatic glucagon secretion in conscious dogs. Glucagon increases the uptake of amino acids by the liver, resulting in increased availability of carbon skeletons for gluconeogenesis. Many bodybuilding coaches promote the idea that insulin secretion should be minimized and glucagon secretion should be maximized pre-competition. A study was conducted by Gravholt and colleagues (2001) to determine whether glucagon stimulated lipolysis in adipose tissue. Glucagon stimulates liver phosphorylase and promotes liver glycogen breakdown and gluconeogenesis.
In the primary steps in adipose tissue burning, triglyceride is mobilized, which refers to the breakdown to TG to three fatty acids and a glycerol molecule. Adrenaline and nor-adrenaline bind to beta-adrenergic receptors in fat cell stimulating HSL, causing FFA release. Glucagon is a hormone that is synthesized and secreted by the alpha-2 cells of the pancreatic islets of Langerhans. Elevated glucagon levels prevent hypoglycemia (assuming there’s a sufficient amount of liver glycogen to provide glucose to the bloodstream).
Insulin and glucagon responses after intake of protein solutions containing the same amount of nitrogen (2.9 grams each) in three men and three women were investigated.


During periods of stress, trauma, or severe exercise, the elevated epinephrine levels can override the affect of the alpha cell of circulating substrates. This is due to an increase in the breakdown of liver glycogen and an increase in gluconeogenesis.
With that idea in mind, the suggestion of BCAA supplementation (by the truckloads) is often advised.
The researchers found that high glucagon levels did not increase interstitial glycerol (and thus lipolysis) in adipose tissue.
Triglyceride breakdown is facilitated by three enzymes—triacylglycerol lipase, diacyclglycerol lipase, and monoacylglycerol lipase. FFA is taken up into the muscle and transported into mitochondria via carnitine palmityl transferase 1 (CPT-1).
Under these conditions, regardless of the concentration of blood glucose, glucagon levels are elevated in anticipation of increased glucose use.
Glucagon stimulates the hepatic oxidation of fatty acids and the formation of ketone bodies from acetyl CoA. This seemingly contradictory advice brings up the question do these coaches have any idea why they promote unfounded claims? Jensen and colleagues (1991) conducted a study to determine whether physiological changes in plasma glucagon concentrations are important in regulating basal adipose tissue lipolysis. The breakdown of TG occurs due to hormone sensitive lipase (HSL), which is primarily influenced by insulin and the catecholamines. It maintains blood glucose levels by activating hepatic glycogenolysis and gluconeogenesis. A study by Kuhara and colleagues (1991) examined the effects of the intravenous infusion of 17 amino acids on the secretion of insulin, glucagon, and growth hormone (GH) in six castrated male sheep.


Despite the higher carbohydrate content of the MS, the peptide hydrolysates elicited a peak insulin response that was two and four times greater than that caused by the MS and glucose solutions.
Asparagine had the most glucagon-stimulating activity (GSA) followed by glycine, phenylalanine, serine, aspartate, cysteine, tryptophan, alanine, glutamate, threonine, glutamine, arginine, ornithine, proline, methionine, lysine, and histidine. Leucine was the most effective amino acid in stimulating insulin secretion but did not produce any increase in glucagon and GH secretion.
The insulin response was closely related to the increase in plasma amino acids, especially leucine, isoleucine, valine, phenylalanine, and arginine. Let me repeat that sentence—the lipolytic effect of glucagon in adipose tissue is minimal in humans. This causes a rise in cAMP (the second messenger), which activates cAMP-dependent protein kinase and increases the phosphorylation of specific enzymes or other proteins.
Alanine, glycine, and serine induced a greater enhancement of both glucagon and insulin secretion than other amino acids.
The three protein solutions elicited similar increases of plasma glucagon, although the response was fastest for both peptide hydrolysates and more prolonged for the MS. No amino acid was able to specifically stimulate glucagon secretion without also increasing insulin or GH secretion.
The glucagon response was linearly related to the increase in plasma amino acids, regardless of the rate of gastric emptying or meal composition. Among the plasma amino acids, tyrosine and methionine were most closely related to the plasma glucagon response.



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