Difference between revisions of "Diabetes"

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(Protein Pathway)
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Principally, advanced glycation end products (AGEs) are the products of a reaction between an amine and a reducing sugar (see [http://www.waiwiki.org/index.php?title=Maillard_reaction Maillard Reaction]). Non-glycated biogenic amines (including amino acids) are rapidly utilized, absorbed or converted:
 
Principally, advanced glycation end products (AGEs) are the products of a reaction between an amine and a reducing sugar (see [http://www.waiwiki.org/index.php?title=Maillard_reaction Maillard Reaction]). Non-glycated biogenic amines (including amino acids) are rapidly utilized, absorbed or converted:
  
Half-life of histamine is only 102 seconds [https://www.ncbi.nlm.nih.gov/pubmed/7080947], 72 seconds for serotonin (not taken up in platelets etc) [https://www.ncbi.nlm.nih.gov/pubmed/6823109], 2 to 2.5 minutes for norepinephrine [https://academic.oup.com/bja/article/95/6/782/257220/Norepinephrine-kinetics-and-dynamics-in-septic], 2 to 3 minutes for epinephrine [https://www.medicines.org.uk/emc/medicine/20909], , depending on the volume of distribution [https://www.ncbi.nlm.nih.gov/pubmed/28011216]. Half life of amino acids may be less than 10 minutes for all amino acids [https://www.ncbi.nlm.nih.gov/pubmed/562318], <1 hour [https://www.ncbi.nlm.nih.gov/pubmed/1163079], 11 minutes for glutamate [https://www.ncbi.nlm.nih.gov/pubmed/6784801], 35 minutes for leucine [https://www.ncbi.nlm.nih.gov/pubmed/6992488], 36 minutes for cysteine [https://www.ncbi.nlm.nih.gov/pubmed/2596429], +/-1 hour for phenylalanine [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1799570/?page=2]76 minutes for arginine [https://examine.com/supplements/arginine/], +/-2 hours for tryptophan [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1429269/?page=5][https://www.ncbi.nlm.nih.gov/pubmed/6865262], 3.6 hours for homocysteine [https://www.ncbi.nlm.nih.gov/pubmed/8330395], 12 hours for 3-methylhistidine [https://www.ncbi.nlm.nih.gov/pubmed/6694553]; higher intakes lead to shorter half-lives [https://www.ncbi.nlm.nih.gov/pubmed/6162471]. Half life of peptides may be less than 1 hour [https://www.ncbi.nlm.nih.gov/pubmed/1907548][https://www.ncbi.nlm.nih.gov/pubmed/16622600][https://www.ncbi.nlm.nih.gov/pubmed/6291099][http://onlinelibrary.wiley.com/doi/10.1016/0014-5793(80)80299-7/epdf])[https://www.ncbi.nlm.nih.gov/pubmed/3120689][http://www.jbc.org/content/257/4/2002.long].
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Half-life of histamine is only 102 seconds [https://www.ncbi.nlm.nih.gov/pubmed/7080947], 72 seconds for serotonin (not taken up in platelets etc) [https://www.ncbi.nlm.nih.gov/pubmed/6823109], 2 to 2.5 minutes for norepinephrine [https://academic.oup.com/bja/article/95/6/782/257220/Norepinephrine-kinetics-and-dynamics-in-septic], 2 to 3 minutes for epinephrine [https://www.medicines.org.uk/emc/medicine/20909], 2 minutes for dopamine [https://www.ncbi.nlm.nih.gov/pubmed/2682552][https://dailymed.nlm.nih.gov/dailymed/archives/fdaDrugInfo.cfm?archiveid=27875], depending on the volume of distribution [https://www.ncbi.nlm.nih.gov/pubmed/28011216]. Half life of amino acids may be less than 10 minutes for all amino acids [https://www.ncbi.nlm.nih.gov/pubmed/562318], <1 hour [https://www.ncbi.nlm.nih.gov/pubmed/1163079], 11 minutes for glutamate [https://www.ncbi.nlm.nih.gov/pubmed/6784801], 35 minutes for leucine [https://www.ncbi.nlm.nih.gov/pubmed/6992488], 36 minutes for cysteine [https://www.ncbi.nlm.nih.gov/pubmed/2596429], +/-1 hour for phenylalanine [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1799570/?page=2]76 minutes for arginine [https://examine.com/supplements/arginine/], +/-2 hours for tryptophan [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1429269/?page=5][https://www.ncbi.nlm.nih.gov/pubmed/6865262], 3.6 hours for homocysteine [https://www.ncbi.nlm.nih.gov/pubmed/8330395], 12 hours for 3-methylhistidine [https://www.ncbi.nlm.nih.gov/pubmed/6694553]; higher intakes lead to shorter half-lives [https://www.ncbi.nlm.nih.gov/pubmed/6162471]. Half life of peptides may be less than 1 hour [https://www.ncbi.nlm.nih.gov/pubmed/1907548][https://www.ncbi.nlm.nih.gov/pubmed/16622600][https://www.ncbi.nlm.nih.gov/pubmed/6291099][http://onlinelibrary.wiley.com/doi/10.1016/0014-5793(80)80299-7/epdf])[https://www.ncbi.nlm.nih.gov/pubmed/3120689][http://www.jbc.org/content/257/4/2002.long].
  
 
Aggressive, reactive AGEs don't have a very long half-life (half-life of MeIQx is 3.5 hours [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4831706/], and 6 hours for acrylamide [https://www.ncbi.nlm.nih.gov/pubmed/21781917]), but AGEs usually have a much longer half-life [https://www.ncbi.nlm.nih.gov/pubmed/8248084]. As a result, a glycated amino acid may repeatedly trigger the release of insulin, as compared to its original non-glycatede version.
 
Aggressive, reactive AGEs don't have a very long half-life (half-life of MeIQx is 3.5 hours [https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4831706/], and 6 hours for acrylamide [https://www.ncbi.nlm.nih.gov/pubmed/21781917]), but AGEs usually have a much longer half-life [https://www.ncbi.nlm.nih.gov/pubmed/8248084]. As a result, a glycated amino acid may repeatedly trigger the release of insulin, as compared to its original non-glycatede version.

Revision as of 20:56, 14 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 (and fatty acids), but also amino acids (protein) directly trigger the release of insulin (eg glycine [1], arginine [2], leucine [3], isoleucine, valine [4], aspartic acid, alanine and serine [5]). Amino acids also affect glucose uptake (particularly phenylalanine [6]) and compete as oxidative fuels.[7] Lysine, tyrosine, alanine, serine and aspartic acid may play a key role in glucose-stimulated insulin secretion.[8] 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.[9] A mixture of leucine, isoleucine, valine, lysine and threonine resulted in significant glycemic and insulinemic responses.[10] Insulin responses are positively correlated with plasma leucine, phenylalanine, and tyrosine concentrations.[11]

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.[12] Dysregulated leucine metabolism progressively develops into insulin resistance [13], and high leucine exposure induced insulin resistance may be reversed by removing the high leucine exposure.[14] 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.[15]

Overweight Pathway

Obesity is a leading pathogenic factor for developing insulin resistance.[16] 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.[17] 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, due to the need for 3 free fatty acids for each single glycerol molecule. Full glycogen stores can therefore give way to repeated triggering of insulin release (and fat deposition), which may lead to insulin resistance.

Protein Pathway

Principally, advanced glycation end products (AGEs) are the products of a reaction between an amine and a reducing sugar (see Maillard Reaction). Non-glycated biogenic amines (including amino acids) are rapidly utilized, absorbed or converted:

Half-life of histamine is only 102 seconds [18], 72 seconds for serotonin (not taken up in platelets etc) [19], 2 to 2.5 minutes for norepinephrine [20], 2 to 3 minutes for epinephrine [21], 2 minutes for dopamine [22][23], depending on the volume of distribution [24]. Half life of amino acids may be less than 10 minutes for all amino acids [25], <1 hour [26], 11 minutes for glutamate [27], 35 minutes for leucine [28], 36 minutes for cysteine [29], +/-1 hour for phenylalanine [30]76 minutes for arginine [31], +/-2 hours for tryptophan [32][33], 3.6 hours for homocysteine [34], 12 hours for 3-methylhistidine [35]; higher intakes lead to shorter half-lives [36]. Half life of peptides may be less than 1 hour [37][38][39][40])[41][42].

Aggressive, reactive AGEs don't have a very long half-life (half-life of MeIQx is 3.5 hours [43], and 6 hours for acrylamide [44]), but AGEs usually have a much longer half-life [45]. As a result, a glycated amino acid may repeatedly trigger the release of insulin, as compared to its original non-glycatede version. A diet that is low in AGEs may reduce the risk of type 2 diabetes by increasing insulin sensitivity.[46] This may be due to the longer half-life of AGEs versus non-glycated protein. In addition, higher blood-sugar levels resulting from insulin resistance endogenous AGE formation, accelerating AGE accumulation.[47]

Author

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Author of this article is Thijs Klompmaker, born in 1966