Difference between revisions of "Diabetes"

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Author of this article is Thijs Klompmaker, born in 1966
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* Author's [http://www.topfitafter50.com/ website, as personal trainer] (specialized in isolation exercises and dietary solutions)
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* Author's [https://www.instagram.com/topfitafter50/ Instagram account]
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* Author's [https://www.youtube.com/channel/UCLZULfm7l2dZFyDdhrROJKg YouTube Channel]
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* Author's [https://twitter.com/topfitafter50/ Twitter account]

Revision as of 14:30, 7 April 2017

Insulin Secretion

As a key regulator of whole body metabolism, the hormone insulin is secreted by pancreatic β-cells as a response to an elevation in nutrients. Insulin facilitates the conversion of glucose into liver- and muscle-glycogen, as well as the uptake of amino acids in cells.

Not just glucose, but also amino acids (protein) directly trigger the release of insulin (eg glycine [1], arginine [2], leucine, isoleucine, valine [3], aspartic acid, alanine and serine [4]). Amino acids affect glucose uptake and compete as oxidative fuels.[5] Lysine, tyrosine, alanine, serine and aspartic acid may play a key role in glucose-stimulated insulin secretion.[6] In pancreatic islets from both healthy young children and adults, insulin secretion is stimulated by arginine and the combination of leucine and glutamine, concentration-dependent and in an biphasic pattern, similarly to glucose-induced insulin secretion.[7] Dysregulated leucine metabolism progressively develops into insulin resistance.[8] A mixture of leucine, isoleucine, valine, lysine and threonine resulted in significant glycemic and insulinemic responses.[9] Insulin responses are positively correlated with plasma leucine, phenylalanine, and tyrosine concentrations.[10]

Insulin Resistance

Insulin resistance is related to valine, glutamate, tyrosine, glutamine and glycine levels. β-cell functioning is related to leucine, tryptophan, valine, glutamate, glutamine, glycine and serine levels.[11] In a 12-year follow-up study involving adult Japanese individuals, plasma levels of isoleucine, leucine, valine, tyrosine, and phenylalanine (particularly any combination of minimally 3 of these amino acids) were reported to predict the development of diabetes in nondiabetic subjects.[12]

Overweight Pathway

Obesity is a leading pathogenic factor for developing insulin resistance.[13] Obese women show a blunted protein anabolic response to hyperinsulinemia that is consistent with resistance to the action of insulin on protein concurrent with that on glucose metabolism.[14] Insulin evokes the storage of blood glucose as liver glycogen. Once liver glycogen is completely repleted, additional blood glucose needs to be stored as glycerol in triglycerides. The latter is a relatively slow process, which can give way to repeated triggering of insulin release.

Protein Pathway

A diet that is low in AGEs (see Maillard Reaction) may reduce the risk of type 2 diabetes by increasing insulin sensitivity.[15] This may be due to the longer half lifetime of AGEs versus non-glycated amino acids and peptides.

Author

Instagram.jpg
YouTube.jpg

Author of this article is Thijs Klompmaker, born in 1966