Dephosphorylation increases insulin-stimulated receptor kinase activity in skeletal muscle of obese Zucker rats
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Summary
It is suggested that excessive serine/threonine phosphorylation of the insulin receptor in obese Zucker rats may be a cause for insulin resistance in skeletal muscle.
- Type
- article
- Published
- 1999-04-01
- Cited by
- 21
- References
- 33
- OpenAlex
- https://openalex.org/W180493640
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:25934586
Keywords
Internal medicine, Insulin receptor, Endocrinology, Insulin receptor substrate, Insulin resistance
References
- Generation and use of anti-phosphotyrosine antibodies for immunoblotting.
- Effect of exercise on synthesis and degradation of muscle protein.
- A defective intramolecular autoactivation cascade may cause the reduced kinase activity of the skeletal muscle insulin receptor from patients with non-insulin-dependent diabetes mellitus.
- Tumor-promoting phorbol esters increase the Km of the ATP-binding site of the insulin receptor kinase from rat adipocytes.
- Serine/threonine phosphorylation of insulin receptor substrate 1 modulates insulin receptor signaling.
- Purification and partial sequence analysis of pp185, the major cellular substrate of the insulin receptor tyrosine kinase.
- Phorbol ester-induced serine phosphorylation of the insulin receptor decreases its tyrosine kinase activity.
- Predominance of tyrosine phosphorylation of insulin receptors during the initial response of intact cells to insulin.
- Insulin-stimulated serine and threonine phosphorylation of the human insulin receptor. An assessment of the role of serines 1305/1306 and threonine 1348 by their replacement with neutral or negatively charged amino acids.
- Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor.
- Impaired Insulin Signaling in Skeletal Muscles from Transgenic Mice Expressing Kinase-deficient Insulin Receptors (*)
- Protein kinase C directly phosphorylates the insulin receptor in vitro and reduces its protein-tyrosine kinase activity.
- IRS-1-Mediated Inhibition of Insulin Receptor Tyrosine Kinase Activity in TNF-α- and Obesity-Induced Insulin Resistance
- Defective insulin receptor tyrosine kinase in human skeletal muscle in obesity and Type 2 (non-insulin-dependent) diabetes mellitus
- Insulin stimulates tyrosine phosphorylation of the insulin receptor in a cell-free system
- Replacement of insulin receptor tyrosine residues 1162 and 1163 compromises insulin-stimulated kinase activity and uptake of 2-deoxyglucose.
- Expression of the major isoenzyme of protein kinase-C in skeletal muscle, nPKC theta, varies with muscle type and in response to fructose-induced insulin resistance.
- Increased abundance of the receptor-type protein-tyrosine phosphatase LAR accounts for the elevated insulin receptor dephosphorylating activity in adipose tissue of obese human subjects.
- Insulin Receptor Signaling Is Augmented by Antisense Inhibition of the Protein Tyrosine Phosphatase LAR (*)
- Nonketotic diabetes mellitus: insulin deficiency or insulin resistance?
Cited by
- Hepatic‐dependent and ‐independent Insulin Actions Are Impaired in the Obese Zucker Rat Model
- Roux-en-Y gastric bypass corrects hyperinsulinemia implications for the remission of type 2 diabetes.
- Insulin Sensitivity and Mitochondrial Function Are Improved in Children With Burn Injury During a Randomized Controlled Trial of Fenofibrate
- Regulation of insulin receptor function
- Insulin sensitivity is related to fat oxidation and protein kinase C activity in children with acute burn injury
- Severe Obesity: Evidence for a Deranged Metabolic Program in Skeletal Muscle?
- PPAR-α agonism improves whole body and muscle mitochondrial fat oxidation, but does not alter intracellular fat concentrations in burn trauma children in a randomized controlled trial
- Is There a Metabolic Program in the Skeletal Muscle of Obese Individuals?
- High-Fat Diet Induces IKKβ and Reduces Insulin Sensitivity in Rats with Low Running Capacity
- Insulin receptor signaling in normal and insulin-resistant states.
- Characterization of insulin signaling in rat retina in vivo and ex vivo.
- The effect of insulin and exercise on c-Cbl protein abundance and phosphorylation in insulin-resistant skeletal muscle in lean and obese Zucker rats
- Regulation of Insulin Signalling by Exercise in Skeletal Muscle
- Increased in vivo phosphorylation of insulin receptor at serine 994 in the liver of obese insulin-resistant Zucker rats.
- The molecular mechanism linking muscle fat accumulation to insulin resistance
- Metabolic regulation of human vascular endothelial cell function in vitro
- Mechanism for improved insulin sensitivity after gastric bypass surgery.
- Constitutive insulin receptor signaling in retina and changes induced by diabetes
- Reduced Tyrosine and Serine-632 Phosphorylation of Insulin Receptor Substrate-1 in the Gastrocnemius Muscle of Obese Zucker Rat
- Insulin Resistance and Inhibitors of the Insulin Receptor Tyrosine Kinase
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