Quantitative dissociation of glucose transport stimulation and insulin receptor tyrosine kinase activation in isolated adipocytes with a covalent insulin dimer (B29,B29'-suberoyl-insulin).
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Summary
It is concluded that a partial phosphorylation of insulin receptors and a submaximal tyrosine kinase activation are sufficient for full stimulation of glucose transport in the adipocyte and suggested that negative cooperativity of the insulin receptor and activation of its tyrosin kinase require a similar conformational change of the receptor protein.
- Type
- article
- Published
- 1989-07-15
- Cited by
- 4
- References
- 33
- OpenAlex
- https://openalex.org/W1968470837
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:24385167
Keywords
Insulin receptor, Autophosphorylation, Insulin, Insulin receptor substrate, Internal medicine
References
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- Evidence concerning the mechanism of insulin-receptor interaction and the structure of the insulin receptor from biological properties of covalently linked insulin dimers.
- cAMP-dependent protein kinase and lipolysis in rat adipocytes. I. Cell preparation, manipulation, and predictability in behavior.
- Differences in the sites of phosphorylation of the insulin receptor in vivo and in vitro.
- Insulin-induced internalization of the insulin receptor in the isolated rat adipose cell. Detection of the internalized 138-kilodalton receptor subunit using a photoaffinity 125I-insulin.
- Human insulin receptors mutated at the ATP-binding site lack protein tyrosine kinase activity and fail to mediate postreceptor effects of insulin.
- Insulin stimulation of phosphorylation of the beta subunit of the insulin receptor. Formation of both phosphoserine and phosphotyrosine.
- Insulin-dependent phosphorylation of the insulin receptor-protein kinase and activation of glucose transport in 3T3-L1 adipocytes.
- Reevaluation of the evidence that an antibody to the insulin receptor is insulinmimetic without activating the protein tyrosine kinase activity of the receptor.
- Structural requirements for the transmembrane activation of the insulin receptor kinase.
- Site-site interactions among insulin receptors. Characterization of the negative cooperativity.
- Predominance of tyrosine phosphorylation of insulin receptors during the initial response of intact cells to insulin.
- The Metabolism of Isolated Fat Cells: I. Effects of Hormones on Glucose Metabolism and Lipolysis
- Insulin stimulates the phosphorylation of the 95,000-dalton subunit of its own receptor.
- The nonclassical insulin binding of insulin receptors from rat liver is due to the presence of two interacting alpha-subunits in the receptor complex.
- Effects of covalently linked insulin dimers on receptor kinase activity and receptor down regulation
- Insulin receptor phosphorylation may not be a prerequisite for acute insulin action.
- Acute insulin action requires insulin receptor kinase activity: introduction of an inhibitory monoclonal antibody into mammalian cells blocks the rapid effects of insulin.
- Kinetic evidence for activating and non-activating components of autophosphorylation of the insulin receptor protein kinase.
Cited by
- The regulation of glucose transport in insulin-sensitive cells
- In vivo glucose uptake and glucose transporter proteins GLUT1 and GLUT4 in heart and various types of skeletal muscle from streptozotocin-diabetic rats.
- Structural and functional heterogeneity of insulin receptors.
- Action of insulin in rat adipocytes and membrane properties.
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