Evidence map›Paper›PMID 7565704›Full record

ArticleMolecular and cellular biology1995

Differential regulation of Raf-1 and B-Raf and Ras-dependent activation of mitogen-activated protein kinase by cyclic AMP in PC12 cells.

P Erhardt, J Troppmair, U R Rapp, G M Cooper

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.7field-weighted citation impact, top 6% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 141 citations in OpenAlex.

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  14. Differential regulation of mitogen-activated protein kinases ERK1/2 and ERK5 by neurotrophins, neuronal activity, and cAMP in neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2001
    Article
  15. Article
  16. Involvement of protein kinase A in fibroblast growth factor-2-activated transcription.Proceedings of the National Academy of Sciences of the United States of America · 2000
    Article
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  18. Review
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

4 authors at 2 institutions in 2 countries.

P ErhardtDana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115, USA.
J Troppmair
U R Rapp
G M Cooper
Harvard University · USUniversity of Würzburg · DE

Funding

Regulation of apoptosis by PI 3-kinase/Akt signalingR01CA018689 · NCI · DANA-FARBER CANCER INSTITUTE · PI COOPER, GEOFFREY M · 1985 to 2012
$6.2M
NCI NIH HHS CA18689
6 · The paper itself

Abstract

Growth factor stimulation of the mitogen-activated protein (MAP) kinase pathway in fibroblasts is inhibited by cyclic AMP (cAMP) as a result of inhibition of Raf-1. In contrast, cAMP inhibits neither nerve growth factor-induced MAP kinase activation nor differentiation in PC12 pheochromocytoma cells. Instead, in PC12 cells cAMP activates MAP kinase. Since one of the major differences between the Ras/Raf/MAP kinase cascades of these cell types is the expression of B-Raf in PC12 cells, we compared the effects of cAMP on Raf-1 and B-Raf. In PC12 cells maintained in serum-containing medium, B-Raf was refractory to inhibition by cAMP, whereas Raf-1 was effectively inhibited. In contrast, both B-Raf and Raf-1 were inhibited by cAMP in serum-starved PC12 cells. The effect of cAMP is thus dependent upon growth conditions, with B-Raf being resistant to cAMP inhibition in the presence of serum. These results were extended by studies of Rat-1 fibroblasts into which B-Raf had been introduced by transfection. As in PC12 cells, B-Raf was resistant to inhibition by cAMP in the presence of serum, whereas Raf-1 was effectively inhibited. In addition, the expression of B-Raf rendered Rat-1 cells resistant to the inhibitory effects of cAMP on both growth factor-induced activation of MAP kinase and mitogenesis. These results indicate that Raf-1 and B-Raf are differentially sensitive to inhibition by cAMP and that B-Raf expression can contribute to cell type-specific differences in the regulation of the MAP kinase pathway. In contrast to the situation in PC12 cells, cAMP by itself did not stimulate MAP kinase in B-Raf-expressing Rat-1 cells. The activation of MAP kinase by cAMP in PC12 cells was inhibited by the expression of a dominant negative Ras mutant, indicating that cAMP acts on a target upstream of Ras. Thus, it appears that a signaling component upstream of Ras is also require for cAMP stimulation of MAP kinase in PC12 cells.

Indexed as

AnimalsCalcium-Calmodulin-Dependent Protein KinasesCell LineCyclic AMPEnzyme ActivationEpidermal Growth FactorFibroblastsNerve Growth FactorsPC12 CellsProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-rafras ProteinsRatsSignal TransductionCalcium-Calmodulin-Dependent Protein KinasesCyclic AMPEpidermal Growth FactorNerve Growth FactorsProtein Serine-Threonine KinasesProto-Oncogene ProteinsProto-Oncogene Proteins c-rafras Proteins

Identifiers

PMID7565704
PMCPMC230803
OpenAlexW2136477311

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.