Resistin inhibits glucose uptake in L6 cells independently of changes in insulin signaling and GLUT4 translocation.

@article{Moon2003ResistinIG,
  title={Resistin inhibits glucose uptake in L6 cells independently of changes in insulin signaling and GLUT4 translocation.},
  author={Byoung Moon and Jamie Jun-Mae Kwan and Noreen Duddy and Gary Sweeney and Najma Begum},
  journal={American journal of physiology. Endocrinology and metabolism},
  year={2003},
  volume={285 1},
  pages={
          E106-15
        }
}
  • Byoung Moon, J. Kwan, +2 authors N. Begum
  • Published 1 July 2003
  • Biology, Medicine
  • American journal of physiology. Endocrinology and metabolism
Elevated levels of resistin have been proposed to cause insulin resistance and therefore may serve as a link between obesity and type 2 diabetes. However, its role in skeletal muscle metabolism is unknown. In this study, we examined the effect of resistin on insulin-stimulated glucose uptake and the upstream insulin-signaling components in L6 rat skeletal muscle cells that were either incubated with recombinant resistin or stably transfected with a vector containing the myc-tagged mouse… 
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Effects of resistin on skeletal glucose metabolism
TLDR
It is concluded that resistin inhibits insulin induced glucose uptake in myocytes by downregulating the expression of GLUT4 and it has no effects on glucose oxidation and glycogen synthesis.
Prolonged exposure to resistin inhibits glucose uptake in rat skeletal muscles
TLDR
Observations highlight the potential role of resistin in the pathophysiology of type 2 diabetes related to obesity and downregulated expression of SNAP23 may have been partly attributed to the decrease of glucose uptake by resistin treatment.
Regulation of insulin signalling, glucose uptake and metabolism in rat skeletal muscle cells upon prolonged exposure to resistin
TLDR
The data show that resistin regulates the function of IRS-1 and Akt1 and decreases GLUT4 translocation and glucose uptake in response to insulin, highlighting the potential role of resistin in the pathophysiology of type 2 diabetes in obesity.
Oligomeric resistin impairs insulin and AICAR-stimulated glucose uptake in mouse skeletal muscle by inhibiting GLUT4 translocation.
TLDR
It is concluded that resistin impairs insulin-stimulated glucose uptake by mechanisms involving reduced plasma membrane GLUT4 translocation but independent of the proximal insulin-signaling cascade, AMPK, and SOCS-3.
Resistin and insulin resistance in hepatocytes: resistin disturbs glycogen metabolism at the protein level.
Adenovirus-mediated high expression of resistin causes dyslipidemia in mice.
TLDR
The results suggest that resistin overexpression induces dyslipidemia in mice, which is commonly seen in the insulin-resistant state, partially through enhanced secretion of lipoproteins.
Resistin acutely impairs insulin-stimulated glucose transport in rodent muscle in the presence, but not absence, of palmitate.
TLDR
The acute impairment of insulin response by resistin was manifested only in the presence of high palmitate and was alleviated when FA metabolism was manipulated (increased oxidation, inhibited ceramide synthesis).
Regulation of fatty acid uptake and metabolism in L6 skeletal muscle cells by resistin
Activation of SOCS-3 by Resistin
ABSTRACT Resistin is an adipocyte hormone that modulates glucose homeostasis. Here we show that in 3T3-L1 adipocytes, resistin attenuates multiple effects of insulin, including insulin receptor (IR)…
Human Resistin Inhibits Myogenic Differentiation and Induces Insulin Resistance in Myocytes
TLDR
Maybe human resistin has not a direct role on insulin sensitivity of myocytes through suppressing myogenesis and stimulating proliferation of myoblasts, however, maybe it impaired the insulin sensitivity in myocyte differentiation and insulin resistance.
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References

SHOWING 1-10 OF 38 REFERENCES
High leptin levels acutely inhibit insulin-stimulated glucose uptake without affecting glucose transporter 4 translocation in l6 rat skeletal muscle cells.
TLDR
High leptin levels can directly reduce insulin-stimulated glucose uptake in L6 muscle cells despite normal GLUT4 translocation, showing that insulin regulates glucose uptake via a signaling pathway sensitive to inhibitors of p38 MAP kinase.
Adipose-derived resistin and gut-derived resistin-like molecule-beta selectively impair insulin action on glucose production.
TLDR
The results support the notion that a novel family of fat- and gut-derived circulating proteins modulates hepatic insulin action, and inhibition of glucose metabolism inhibited glucose metabolism such that lower rates of glucose infusion were required to maintain the plasma glucose concentration at basal levels.
Insulin resistance and type 2 diabetes are not related to resistin expression in human fat cells or skeletal muscle.
  • I. Nagaev, U. Smith
  • Biology, Medicine
    Biochemical and biophysical research communications
  • 2001
TLDR
Resistin gene expression with real-time RT-PCR in human isolated fat cells, adipose tissue, and muscle from 42 individuals of varying degrees of overweight and who had normal insulin sensitivity or were insulin-resistant or Type 2 diabetic samples showed no difference.
Resistin / Fizz3 expression in relation to obesity and peroxisome proliferator-activated receptor-gamma action in humans.
TLDR
It is concluded that the recently described relationships of murine resistin/Fizz3 expression with obesity, insulin resistance, and PPAR-gamma action may not readily translate to humans.
Impairment of insulin signaling in human skeletal muscle cells by co-culture with human adipocytes.
TLDR
The release of fat cell factors induces insulin resistance in human skeletal muscle cells; however, TNF-alpha and resistin appear not to be involved in this process.
An Inhibitor of p38 Mitogen-activated Protein Kinase Prevents Insulin-stimulated Glucose Transport but Not Glucose Transporter Translocation in 3T3-L1 Adipocytes and L6 Myotubes*
TLDR
It is proposed that insulin stimulates two independent signals contributing to stimulation of glucose transport: phosphatidylinositol 3-kinase leads to glucose transporter translocation and a pathway involving p38 MAP kinase leadsto activation of the recruited glucose transporter at the membrane.
Phenylarsine oxide inhibits insulin-stimulated protein phosphatase 1 activity and GLUT-4 translocation.
  • N. Begum
  • Biology, Computer Science
    The American journal of physiology
  • 1994
TLDR
It is concluded that PAO may interfere with the components of insulin signal transduction pathways that lead to the activation of PP-1 and this may be responsible for the observed inhibition in insulin action.
Differential Effects of Phosphatidylinositol 3-Kinase Inhibition on Intracellular Signals Regulating GLUT4 Translocation and Glucose Transport*
TLDR
It is proposed that a distinct, high affinity target of wortmannin, other than PI 3-kinase, may be necessary for activation of p38 MAPK and GLUT4 in response to insulin.
The hormone resistin links obesity to diabetes
TLDR
It is shown that adipocytes secrete a unique signalling molecule, which is named resistin (for resistance to insulin), which circulating resistin levels are decreased by the anti-diabetic drug rosiglitazone, and increased in diet-induced and genetic forms of obesity.
Insulin-stimulated GLUT4 translocation requires the CAP-dependent activation of TC10
TLDR
It is shown that phosphorylated Cbl recruits the CrkII–C3G complex to lipid rafts, where C3G specifically activates the small GTP-binding protein TC10, which is essential for insulin-stimulated glucose uptake and GLUT4 translocation.
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