Activation of Ras, Raf-1 and protein kinase C in differentiating human neuroblastoma cells after treatment with phorbolester and NGF
Söderholm, H ; Olsson, A ; Lavenius, E ; Rönnstrand, Lars LU
and Nånberg, Eeva
(2001)
In Cellular Signalling
13(2).
p.95-104
- Abstract
- The human neuroblastoma cell line SH-SY5Y/TrkA differentiates in vitro and acquires a sympathetic phenotype in response to phorbolester (activator of protein kinase C, PKC) in the presence of serum or growth factors, or nerve growth factor (NGF). We have now investigated to what extent phorbolester and NGF cause activation of Ras and Raf-1 and the involvement of PKC in this response in differentiating SH-SY5Y/TrkA cells. NGF stimulated increased accumulation of Ras-GTP and a threefold activation of Raf-1. In contrast, 12-O-tetradecanoylphorbol-13-acetate (TPA) had no effect on the amount of Ras-GTP but led to a smaller activation of Raf-1. NGF caused a limited increase in phosphorylation of Raf-1 compared with TPA, and NGF-induced Raf... (More)
- The human neuroblastoma cell line SH-SY5Y/TrkA differentiates in vitro and acquires a sympathetic phenotype in response to phorbolester (activator of protein kinase C, PKC) in the presence of serum or growth factors, or nerve growth factor (NGF). We have now investigated to what extent phorbolester and NGF cause activation of Ras and Raf-1 and the involvement of PKC in this response in differentiating SH-SY5Y/TrkA cells. NGF stimulated increased accumulation of Ras-GTP and a threefold activation of Raf-1. In contrast, 12-O-tetradecanoylphorbol-13-acetate (TPA) had no effect on the amount of Ras-GTP but led to a smaller activation of Raf-1. NGF caused a limited increase in phosphorylation of Raf-1 compared with TPA, and NGF-induced Raf activity was independent of PKC. Analysis of phosphorylation of the endogenous PKC substrate myristoylated alanine-rich C-kinase substrate (MARCKS), and of subcellular distribution of PKC-alpha, -delta, and -epsilon revealed that NGF only caused a very small activation of PKC in SH-SY5Y/TrkA cells. The results identify Raf-1 as a target for both TPA- and NGF-induced signals in differentiating SH-SY5Y/TrkA cells and demonstrate that signalling to Raf-1 was mediated via distinct mechanisms. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1782447
- author
- Söderholm, H
; Olsson, A
; Lavenius, E
; Rönnstrand, Lars
LU
and Nånberg, Eeva
- publishing date
- 2001
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Cellular Signalling
- volume
- 13
- issue
- 2
- pages
- 95 - 104
- publisher
- Elsevier
- external identifiers
-
- scopus:0035106696
- ISSN
- 1873-3913
- language
- English
- LU publication?
- no
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Experimental Clinical Chemistry (013016010)
- id
- befa1161-f19f-4ad2-93b1-914834643c95 (old id 1782447)
- alternative location
- http://www.ncbi.nlm.nih.gov/pubmed/11257453
- http://www.sciencedirect.com/science/article/pii/S0898656800001418
- date added to LUP
- 2016-04-04 08:56:52
- date last changed
- 2022-01-29 08:01:11
@article{befa1161-f19f-4ad2-93b1-914834643c95,
abstract = {{The human neuroblastoma cell line SH-SY5Y/TrkA differentiates in vitro and acquires a sympathetic phenotype in response to phorbolester (activator of protein kinase C, PKC) in the presence of serum or growth factors, or nerve growth factor (NGF). We have now investigated to what extent phorbolester and NGF cause activation of Ras and Raf-1 and the involvement of PKC in this response in differentiating SH-SY5Y/TrkA cells. NGF stimulated increased accumulation of Ras-GTP and a threefold activation of Raf-1. In contrast, 12-O-tetradecanoylphorbol-13-acetate (TPA) had no effect on the amount of Ras-GTP but led to a smaller activation of Raf-1. NGF caused a limited increase in phosphorylation of Raf-1 compared with TPA, and NGF-induced Raf activity was independent of PKC. Analysis of phosphorylation of the endogenous PKC substrate myristoylated alanine-rich C-kinase substrate (MARCKS), and of subcellular distribution of PKC-alpha, -delta, and -epsilon revealed that NGF only caused a very small activation of PKC in SH-SY5Y/TrkA cells. The results identify Raf-1 as a target for both TPA- and NGF-induced signals in differentiating SH-SY5Y/TrkA cells and demonstrate that signalling to Raf-1 was mediated via distinct mechanisms.}},
author = {{Söderholm, H and Olsson, A and Lavenius, E and Rönnstrand, Lars and Nånberg, Eeva}},
issn = {{1873-3913}},
language = {{eng}},
number = {{2}},
pages = {{95--104}},
publisher = {{Elsevier}},
series = {{Cellular Signalling}},
title = {{Activation of Ras, Raf-1 and protein kinase C in differentiating human neuroblastoma cells after treatment with phorbolester and NGF}},
url = {{http://www.ncbi.nlm.nih.gov/pubmed/11257453}},
volume = {{13}},
year = {{2001}},
}