Evidence map›Paper›PMID 8246947›Full record

ArticleMolecular and cellular biology1993

Epidermal growth factor induces phosphorylation of extracellular signal-regulated kinase 2 via multiple pathways.

B M Burgering, A M de Vries-Smits, R H Medema, P C van Weeren, L G Tertoolen, J L Bos

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In one paragraph

Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed
8.4field-weighted citation impact, top 2% 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

37 citing papers in PubMed, 158 citations in OpenAlex.

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  5. Extracellular matrix composition determines the transcriptional response to epidermal growth factor receptor activation.Proceedings of the National Academy of Sciences of the United States of America · 2001
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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

6 authors at 1 institution in 1 country.

B M BurgeringLaboratory of Physiological Chemistry, Utrecht University, The Netherlands.
A M de Vries-Smits
R H Medema
P C van Weeren
L G Tertoolen
J L Bos
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Expression of p21rasAsn-17, a dominant negative mutant of p21ras that blocks p21ras activation by growth factors, inhibits activation of extracellular signal-regulated kinase 2 (ERK2) by insulin and platelet-derived growth factor in rat-1 cells [A. M. M. de Vries-Smits, B. M. T. Burgering, S. J. Leevers, C. J. Marshall, and J. L. Bos, Nature (London) 357:602-604, 1992]. Here we report that expression of p21rasAsn-17 does not abolish epidermal growth factor (EGF)-induced phosphorylation of ERK2 in fibroblasts. Since EGF activates p21ras in these cells, this indicates that EGF induces a p21ras-independent pathway for the phosphorylation of ERK2 as well. We investigated whether activation of protein kinase C (PKC) or increase in intracellular calcium could be involved in p21ras-independent signaling. In rat-1 cells, inhibition of either PKC, by prolonged 12-O-tetradecanoylphorbol-13-acetate (TPA) pretreatment, or calcium influx, by ethylene glycol-bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) pretreatment, did not abolish EGF-induced ERK2 phosphorylation. However, a combined inhibition of both p21ras and calcium influx, but not PKC, resulted in a complete inhibition of EGF-induced ERK2 phosphorylation. In contrast, in Swiss 3T3 cells, inhibition of both p21ras activation and TPA-sensitive PKC, but not calcium influx, inhibited EGF-induced ERK2 phosphorylation. These results demonstrate that in fibroblasts, EGF induces alternative pathways of ERK2 phosphorylation in a cell-type-specific manner.

Indexed as

AnimalsCalciumCalcium-Calmodulin-Dependent Protein KinasesCell LineEgtazic AcidEpidermal Growth FactorMiceMitogen-Activated Protein Kinase 1PhosphorylationPlatelet-Derived Growth FactorProto-Oncogene Proteins p21(ras)RatsSignal TransductionTetradecanoylphorbol AcetateCalciumCalcium-Calmodulin-Dependent Protein KinasesEgtazic AcidEpidermal Growth FactorMitogen-Activated Protein Kinase 1Platelet-Derived Growth FactorProto-Oncogene Proteins p21(ras)Tetradecanoylphorbol Acetate

Identifiers

PMID8246947
PMCPMC364795
OpenAlexW2126653581

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.