Receptor regulation of phosphoinositide 3-hydroxykinase in the NG115-401L-C3 neuronal cell line: stimulation by insulin-like growth factor-I

David R. Poyner, Michael R. Hanley, T.R. Jackson, Phillip T. Hawkins

Research output: Contribution to journalArticlepeer-review

Abstract

The activation of phosphoinositide 3-hydroxykinase (P13K) is currently believed to represent the critical regulatory event which leads to the production of a novel intracellular signal. We have examined the control of this pathway by a number of cell-surface receptors in NG115-401L-C3 neuronal cells. Insulin-like growth factor-I stimulated the accumulation of 3-phosphorylated inositol lipids in intact cells and the appearance of P13K in antiphosphotyrosine-antibody-directed immunoprecipitates prepared from lysed cells, suggesting that P13K had been activated by a mechanism involving a protein tyrosine kinase. In contrast, P13K in these cells was not regulated by a variety of G-protein-coupled receptors, nerve growth factor acting via a low affinity receptor, or receptors for transforming growth factor-beta and interleukin-1. The receptor-specificity of P13K activation in these cells places significant constraints on the possible physiological function(s) of this pathway.
Original languageEnglish
Pages (from-to)901-905
Number of pages5
JournalBiochemical Journal
Volume290
Issue number3
Publication statusPublished - 21 Apr 1993

Keywords

  • 1-Phosphatidylinositol
  • 3-Kinase
  • animals
  • cell line
  • cell membrane
  • enzyme activation
  • immunosorbent techniques
  • insulin-like growth factor
  • I kinetics
  • nerve growth factors
  • neurons
  • phosphatidylinositol phosphates
  • phosphatidylinositols
  • phosphotransferases receptors
  • cCell surface receptors

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