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Last Updated: 2 months ago

Possible Interaction: Insulin and Threonine





Research Papers that Mention the Interaction

Incubating adipocytes with insulin decreased the electrophoretic mobility and stimulated the phosphorylation of both Ser and Thr residues in lipin.
Proceedings of the National Academy of Sciences of the United States of America  •  2002  |  View Paper
Insulin induced threonine phosphorylation of this protein in a dose-dependent manner, with an ED50 of 3-6 x 10(-9) M. The 50-kilodalton phosphoprotein (pp50) was detectable 20 min after exposure of the cells to insulin, and phosphorylation reached a maximum after 90 min.
Phosphoamino acid analysis of the pp50 demonstrated that insulin increased phosphorylation, mainly of threonine and moderately of serine, whereas pp50 did not contain phosphotyrosine.
Endocrinology  •  1994  |  View Paper
Net negative balances of alanine, methionine, glycine, threonine and asparagine (typical substrates for system A amino acid transport) also were decreased by insulin , whereas serine (another substrate for system A transport) shifted from a zero balance to net uptake.
The Journal of clinical investigation  •  1993  |  View Paper
As expected, the infusion of insulin exhibited significant reduction of the release of glycine, proline, valine, phenylalanine, leucine, threonine and isoleucine.
Hoppe-Seyler's Zeitschrift fur physiologische Chemie  •  1980  |  View Paper
Insulin concentration was greater with Thr , glucagon levels were increased with Lys, Thr, Val, and Glu, whereas IGF-1 levels were enhanced with Gln, Lys, and Thr supply.
Animal science journal = Nihon chikusan Gakkaiho  •  2018  |  View Paper
Results: In Xenopus oocytes insulin increases the activity of NCC together with its phosphorylation at threonine residue 58.
Journal of hypertension  •  2013  |  View Paper
…,insulin induced the phosphorylation of extracellular signal-regulated kinases (Erks), … and ribosomal p70 S6 protein kinase (p70 S6K) at Thr 389, and the insulin-induced 2-deoxy-D-[1-3H]glucose uptake was inhibited by … wortmannin, an inhibitor of phosphatidylinositol 3-kinase (PI3K), or ML-9, an Akt inhibitor.
Biological & pharmaceutical bulletin  •  2005  |  View Paper
In addition, insulin caused an increase in Akt phosphorylation and a decrease in AMPK phosphorylation at its major regulatory site ( threonine 172 of the α catalytic subunit).
Journal of Biological Chemistry  •  2003  |  View Paper
For the leg, the uptake of His and Thr were decreased by insulin , whereas the infusion of AA stimulated the uptake of total essential AA.
Journal of dairy science  •  2001  |  View Paper
Although calmodulin is constitutively phosphorylated, insulin increases phosphate incorporation into serine, threonine and tyrosine residues.
The Biochemical journal  •  1992  |  View Paper
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