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HandWiki. GSK-3 Inhibitor. Encyclopedia. Available online: https://encyclopedia.pub/entry/32522 (accessed on 25 September 2026).
HandWiki. GSK-3 Inhibitor. Encyclopedia. Available at: https://encyclopedia.pub/entry/32522. Accessed September 25, 2026.
HandWiki. "GSK-3 Inhibitor" Encyclopedia, https://encyclopedia.pub/entry/32522 (accessed September 25, 2026).
HandWiki. (2022, November 02). GSK-3 Inhibitor. In Encyclopedia. https://encyclopedia.pub/entry/32522
HandWiki. "GSK-3 Inhibitor." Encyclopedia. Web. 02 November, 2022.
GSK-3 Inhibitor
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Glycogen synthase, an enzyme that is responsible in glycogen synthesis, is activated by glucose 6-phosphate (G6P), and inhibited by glycogen synthase kinases (GSK3). Those two mechanisms play an important role in glycogen metabolism. Glycogen synthase kinase (GSK-3) is a serine/threonine kinase that phosphorylate either threonine or serine, and this phosphorylation permits a variety of biological activities as glycogen metabolism, cell signaling, cellular transport, and others. GS inhibition by GSK-3β leads to a decrease in glycogen synthesis in the liver and muscles, along with increased blood glucose or hyperglycemia. This is why GSK-3β is associated with the pathogenesis and progression of many diseases, such as diabetes, obesity, and cancer. Human GSK-3 has two isoforms, α and β. It is active in resting cells and is inhibited by several hormones such as insulin, endothelial growth factor, and platelet-derived growth factor. Insulin inactivates it by phosphorylation of the specific serine residues Ser21 and Ser9 in GSK-3 isoforms α and β, respectively. In a phosphatidylinositol 3-kinase-dependent way. Glycogen synthase kinase inhibitors are different chemotypes and have variable mechanisms of action; they may be cations, from natural sources, synthetic ATP and non-ATP competitive inhibitors and substrate-competitive inhibitors. GSK3 is a bi-lobar architecture with N-terminal and C-terminal, the N-terminal is responsible for ATP binding and C-terminal which is called as activation loop mediates the kinase activity, Tyrosine located at the C-terminal it essential for full GSK3 activity.

glycogen synthesis glycogen synthase phosphatidylinositol

References

  1. "Naproxen and cromolyn as new glycogen synthase kinase 3β inhibitors for amelioration of diabetes and obesity: an investigation by docking simulation and subsequent in vitro/in vivo biochemical evaluation". Journal of Biochemical and Molecular Toxicology 27 (9): 425–36. September 2013. doi:10.1002/jbt.21503. PMID 23784744.  https://dx.doi.org/10.1002%2Fjbt.21503
  2. https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1415316/
  3. "Olanzapine inhibits glycogen synthase kinase-3beta: an investigation by docking simulation and experimental validation". European Journal of Pharmacology 584 (1): 185–91. April 2008. doi:10.1016/j.ejphar.2008.01.019. PMID 18295757.  https://dx.doi.org/10.1016%2Fj.ejphar.2008.01.019
  4. Eldar-Finkelman, H. and Martinez, A. (2018). GSK-3 Inhibitors: Preclinical and Clinical Focus on CNS.
  5. "Effects of Ranitidine, Famotidine and Omeprazole on Some Haematobiochemical Parameters in Mice". Journal of Animal and Veterinary Advances 2: 321–6. 2003. http://medwelljournals.com/abstract/?doi=javaa.2003.321.326. 
  6. "Famotidine inhibits glycogen synthase kinase-3β: an investigation by docking simulation and experimental validation". Journal of Enzyme Inhibition and Medicinal Chemistry 28 (4): 690–4. August 2013. doi:10.3109/14756366.2012.672413. PMID 22512725.  https://dx.doi.org/10.3109%2F14756366.2012.672413
  7. "Multiple biological activities of curcumin: a short review". Life Sciences 78 (18): 2081–7. March 2006. doi:10.1016/j.lfs.2005.12.007. PMID 16413584.  https://dx.doi.org/10.1016%2Fj.lfs.2005.12.007
  8. Balasubramanian, Krishnan (2006). "Molecular Orbital Basis for Yellow Curry Spice Curcumin's Prevention of Alzheimer's Disease". Journal of Agricultural and Food Chemistry 54 (10): 3512–3520. doi:10.1021/jf0603533.  https://dx.doi.org/10.1021%2Fjf0603533
  9. "NMR study of the solution structure of curcumin". Journal of Natural Products 70 (2): 143–6. February 2007. doi:10.1021/np060263s. PMID 17315954.  https://dx.doi.org/10.1021%2Fnp060263s
  10. "Curcumin: A natural antiinflammatory agent". Indian Journal of Pharmacology 37 (3): 141. 2005. doi:10.4103/0253-7613.16209. http://www.bioline.org.br/pdf?ph05037. 
  11. "Antibacterial activity of turmeric oil: a byproduct from curcumin manufacture". Journal of Agricultural and Food Chemistry 47 (10): 4297–300. October 1999. doi:10.1021/jf990308d. PMID 10552805.  https://dx.doi.org/10.1021%2Fjf990308d
  12. "Enhancement of wound healing by curcumin in animals". Wound Repair and Regeneration 6 (2): 167–77. 1998. doi:10.1046/j.1524-475X.1998.60211.x. PMID 9776860.  https://dx.doi.org/10.1046%2Fj.1524-475X.1998.60211.x
  13. "Curcumin inhibits formation of amyloid beta oligomers and fibrils, binds plaques, and reduces amyloid in vivo". The Journal of Biological Chemistry 280 (7): 5892–901. February 2005. doi:10.1074/jbc.M404751200. PMID 15590663.  https://dx.doi.org/10.1074%2Fjbc.M404751200
  14. "Synthesis and exploration of novel curcumin analogues as anti-malarial agents". Bioorganic & Medicinal Chemistry 16 (6): 2894–902. March 2008. doi:10.1016/j.bmc.2007.12.054. PMID 18194869.  https://dx.doi.org/10.1016%2Fj.bmc.2007.12.054
  15. "Curcumin, the active principle of turmeric (Curcuma longa), ameliorates diabetic nephropathy in rats". Clinical and Experimental Pharmacology & Physiology 33 (10): 940–5. October 2006. doi:10.1111/j.1440-1681.2006.04468.x. PMID 17002671.  https://dx.doi.org/10.1111%2Fj.1440-1681.2006.04468.x
  16. "Glycogen synthase kinase-3 beta regulates NF-kappa B1/p105 stability". The Journal of Biological Chemistry 278 (41): 39583–90. October 2003. doi:10.1074/jbc.M305676200. PMID 12871932.  https://dx.doi.org/10.1074%2Fjbc.M305676200
  17. "Inhibition of glycogen synthase kinase by curcumin: Investigation by simulated molecular docking and subsequent in vitro/in vivo evaluation". Journal of Enzyme Inhibition and Medicinal Chemistry 24 (3): 771–8. June 2009. doi:10.1080/14756360802364377. PMID 18720192.  https://dx.doi.org/10.1080%2F14756360802364377
  18. "Antipsychotics A-Z". Mind.org.uk. 2018. https://www.mind.org.uk/information-support/drugs-and-treatments/antipsychotics-a-z. 
  19. "Antipsychotic Medication for Bipolar Disorder". WebMD. https://www.webmd.com/bipolar-disorder/guide/antipsychotic-medication. 
  20. "Characterization of olanzapine-induced weight gain in rats". Journal of Psychopharmacology 16 (4): 291–6. December 2002. doi:10.1177/026988110201600402. PMID 12503827.  https://dx.doi.org/10.1177%2F026988110201600402
  21. "Profile of olanzapine long-acting injection for the maintenance treatment of adult patients with schizophrenia". Neuropsychiatric Disease and Treatment 6: 573–81. September 2010. doi:10.2147/NDT.S5463. PMID 20856920.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2938306
  22. Murphy, Felicity; Middleton, Mark (2012). "Cytostatic and cytotoxic drugs". A worldwide yearly survey of new data in adverse drug reactions and interactions. Side Effects of Drugs Annual. 34. pp. 731–747. doi:10.1016/B978-0-444-59499-0.00045-3. ISBN 9780444594990.  https://dx.doi.org/10.1016%2FB978-0-444-59499-0.00045-3
  23. "Small-Molecule Inhibitors of GSK-3: Structural Insights and Their Application to Alzheimer's Disease Models". International Journal of Alzheimer's Disease 2012: 381029. 2012. doi:10.1155/2012/381029. PMID 22888461.  http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=3408674
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