Top

Research Article

Split Viewer

Mol. Cells 1996; 6(4): 494-498

Published online August 31, 1996

© The Korean Society for Molecular and Cellular Biology

Activation of Akt by Nerve Growth Factor via Phosphatidylinositol-3 Kinase in PC12 Pheochromocytoma Cells

Eui Kyun Park, Sung-II Yang and Shin-Sung Kang

Abstract

Akt, a serine/threonine kinase has been recently shown to be activated by mitogenic growth factors via phosphatidylinositol-3 kinase (PI-3 kinase). PI-3 kinase can also be activated by a G-protein linked receptor as well as a receptor tyrosine kinase (RTK). In this study, activation of Akt by a nerve growth factor (NGF) in pheochromocytoma 12 (PC12) cells was analyzed using histone H2B as a kinase substrate. Akt was activated by NGF in a time- and a dose-dependent manner in PC12 cells. This activation was blocked by wortmannin, a PI-3 kinase inhibitor, indicating that PI-3 kinase mediated the NGF-induced activation of Akt. However, treatment of human neutrophils and human myeloid-derived U937 cells with formylated methionylleucylphenylalanine (tMLP) showed no effect on Akt activity, although activation of PI-3 kinase by tMLP-stimulated G-protein induced an increase in the tyrosine phosphorylation of p56lyn protein. These results indicate that, like by mitogenic growth factors, activation of Akt by NGF in PC12 cells is mediated by RTK-associated PI-3 kinase, and suggest a possible role of Akt in the physiological functions of NGF as well.

Article

Research Article

Mol. Cells 1996; 6(4): 494-498

Published online August 31, 1996

Copyright © The Korean Society for Molecular and Cellular Biology.

Activation of Akt by Nerve Growth Factor via Phosphatidylinositol-3 Kinase in PC12 Pheochromocytoma Cells

Eui Kyun Park, Sung-II Yang and Shin-Sung Kang

Abstract

Akt, a serine/threonine kinase has been recently shown to be activated by mitogenic growth factors via phosphatidylinositol-3 kinase (PI-3 kinase). PI-3 kinase can also be activated by a G-protein linked receptor as well as a receptor tyrosine kinase (RTK). In this study, activation of Akt by a nerve growth factor (NGF) in pheochromocytoma 12 (PC12) cells was analyzed using histone H2B as a kinase substrate. Akt was activated by NGF in a time- and a dose-dependent manner in PC12 cells. This activation was blocked by wortmannin, a PI-3 kinase inhibitor, indicating that PI-3 kinase mediated the NGF-induced activation of Akt. However, treatment of human neutrophils and human myeloid-derived U937 cells with formylated methionylleucylphenylalanine (tMLP) showed no effect on Akt activity, although activation of PI-3 kinase by tMLP-stimulated G-protein induced an increase in the tyrosine phosphorylation of p56lyn protein. These results indicate that, like by mitogenic growth factors, activation of Akt by NGF in PC12 cells is mediated by RTK-associated PI-3 kinase, and suggest a possible role of Akt in the physiological functions of NGF as well.

Mol. Cells
Nov 30, 2022 Vol.45 No.11, pp. 763~867
COVER PICTURE
Naive (cyan) and axotomized (magenta) retinal ganglion cell axons in Xenopus tropicalis (Choi et al., pp. 846-854).

Share this article on

  • line
  • mail

Molecules and Cells

eISSN 0219-1032
qr-code Download