Myoglobin glycation is the end product of carbohydrate oxidation. Normally, myoglobin is produced by the liver, pancreas, and kidney. In some individuals, myoglobin can be synthesized from glucose via gluconeogenesis. Myoglobin is accumulated in the liver, kidneys, and ferns at the end of exercise, during periods of fasting, and following surgery. Myoglobin production usually peaks during workouts lasting at least one hour because the muscles are exposed to elevated concentrations of glucose during this time.
Exercise and diet can affect levels of myoglobin glycation. It has been found that the consumption of caffeine, alcohol, and black tea, increases the oxidation of glucose and can stimulate the production of myoglobin glycation. Exercise prevents the excess accumulation of myoglobin. In addition, certain drugs such as aspirin, azathioprine, carbamazepine, and thalidomide increase blood acid levels. The increase in acid results in decreased production of myoglobin by the liver.
Studies suggest that the risk of myoglobin glycation is increased by the intake of antibiotics such as erythromycin, clarithromycin, and tetracycline. Furthermore, the consumption of insulin can increase the risk of glycation especially if the cells of the intestine are overgrown. The consumption of free iron from the heme moiety of myoglobin can prevent glycation by blocking the entry of glucose into the cell, preventing the accumulation of free iron in the glycation regions.
The treatment for myoglobin glycation involves the reduction of the amount of glucose in the body. This can be achieved through carbohydrate restriction, including the reduction of sugars, sweeteners, and white flour products. This treatment also prevents formation of new myoglobin. Another treatment for myoglobin glycation is fibrinolytic therapy, where a fibrin cross-linking agent is used in combination with a low-molecular-weight cross-linking agent. This treatment prevents the formation of new fibrins which, in turn, prevents further glycation.
Myoglobin glycation can be determined via the study of the absorption of infrared and chemiluminescence. Infrared absorbance determines the amount of iron released from the heme moiety of myoglobin. The absorption of chemiluminescence determines the extent to which the iron is absorbed. Myoglobin is formed when the heme moiety of myoglobin combines with an oxidizing agent like glycogen. There are different types of myoglobin glycation and different factors associated with its formation.
Individuals at risk of myoglobin glycation should consume foods rich in low-fat dairy products as well as lean meats, fish, poultry, and legumes. A diet rich in fruits and vegetables should be included as an additional source of nutrients for preventing and controlling myoglobin glycation. Furthermore, individuals at risk of myoglobin glycation should maintain a low intake of salt as sodium is one of the known precipitating agents of myoglobin glycation.
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