ArticleMolecular and cellular endocrinology2010
GSK-3beta and control of glucose metabolism and insulin action in human skeletal muscle.
Article in Molecular and cellular endocrinology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 41 citations in OpenAlex.
- Role of GSK-3 Inhibition in Alzheimer's Disease Therapy.Current Alzheimer research · 2026Review
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- Signaling defects associated with insulin resistance in nondiabetic and diabetic individuals and modification by sex.The Journal of clinical investigation · 2021Article
- Human amniotic mesenchymal stem cells-conditioned medium protects mice from high-fat diet-induced obesity.Stem cell research & therapy · 2021Article
- Article
- Protective effects of asiatic acid in a spontaneous type 2 diabetic mouse model.Molecular medicine reports · 2017Article
- Transcriptional regulation of pig GYS1 gene by glycogen synthase kinase 3β (GSK3β).Molecular and cellular biochemistry · 2017Article
- Myotubes derived from human-induced pluripotent stem cells mirror in vivo insulin resistance.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Alteration in amyloid β42, phosphorylated tau protein, interleukin 6, and acetylcholine during diabetes-accelerated memory dysfunction in diabetic rats: correlation of amyloid β42 with changes in glucose metabolism.Behavioral and brain functions : BBF · 2015Article
- Identification of porcine glycogen synthase kinase 3α (GSK-3α) gene and its association with carcass traits.Molecular and cellular biochemistry · 2013Article
- Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The involvement of the beta-isoform of glycogen synthase kinase (GSK-3) in glucose metabolism and insulin action was investigated in cultured human skeletal muscle cells. A 60% reduction in GSK-3beta protein expression was attained by treatment with siRNA; GSK-3alpha expression was unaltered. GSK-3beta knockdown did not influence total glycogen synthase (GS) activity, but increased the phosphorylation-dependent activity (fractional velocity-FV) in the basal state. Insulin responsiveness of GSFV was doubled by GSK-3beta knockdown (p<0.05). Basal rates of glucose uptake (GU) were not significantly influenced by GSK-3beta knockdown, while insulin stimulation of GU was increased. Improvements in insulin action on GS and GU did not involve changes in protein expression of either IRS-1 or Akt 1/2. Maximal insulin stimulation of phosphorylation of Akt was unaltered by GSK-3beta knockdown. Unlike GSK-3alpha, GSK-3beta directly regulates both GS activity in the absence of added insulin and through control of insulin action.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.