Evidence map›Paper›PMID 24860093›Full record

ArticleThe Journal of biological chemistry2014

Platelet-derived growth factor β-receptor, transforming growth factor β type I receptor, and CD44 protein modulate each other's signaling and stability.

Helena Porsch, Merima Mehić, Berit Olofsson, Paraskevi Heldin, Carl-Henrik Heldin

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
–field-weighted citation impact
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

45 citing papers in PubMed.

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  19. Smad2 inhibition ofAtherosclerosis plus · 2021
    Article
  20. Regenerative cross talk between cardiac cells and macrophages.American journal of physiology. Heart and circulatory physiology · 2021
    Article
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

5 authors.

Helena PorschFrom the Ludwig Institute for Cancer Research, Science for Life Laboratory, Uppsala University, Biomedical Center, Box 595, SE-75124 Uppsala, Sweden.
Merima MehićFrom the Ludwig Institute for Cancer Research, Science for Life Laboratory, Uppsala University, Biomedical Center, Box 595, SE-75124 Uppsala, Sweden.
Berit OlofssonFrom the Ludwig Institute for Cancer Research, Science for Life Laboratory, Uppsala University, Biomedical Center, Box 595, SE-75124 Uppsala, Sweden.
Paraskevi HeldinFrom the Ludwig Institute for Cancer Research, Science for Life Laboratory, Uppsala University, Biomedical Center, Box 595, SE-75124 Uppsala, Sweden Evi.Heldin@LICR.uu.se.
Carl-Henrik HeldinFrom the Ludwig Institute for Cancer Research, Science for Life Laboratory, Uppsala University, Biomedical Center, Box 595, SE-75124 Uppsala, Sweden C-H.Heldin@LICR.uu.se.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Growth factors, such as platelet-derived growth factor BB (PDGF-BB) and transforming growth factor β (TGFβ), are key regulators of cellular functions, including proliferation, migration, and differentiation. Growth factor signaling is modulated by context-dependent cross-talk between different signaling pathways. We demonstrate in this study that PDGF-BB induces phosphorylation of Smad2, a downstream mediator of the canonical TGFβ pathway, in primary dermal fibroblasts. The PDGF-BB-mediated Smad2 phosphorylation was dependent on the kinase activities of both TGFβ type I receptor (TβRI) and PDGF β-receptor (PDGFRβ), and it was prevented by inhibitory antibodies against TGFβ. Inhibition of the activity of the TβRI kinase greatly reduced the PDGF-BB-dependent migration in dermal fibroblasts. Moreover, we demonstrate that the receptors for PDGF-BB and TGFβ interact physically in primary dermal fibroblasts and that stimulation with PDGF-BB induces internalization not only of PDGFRβ but also of TβRI. In addition, silencing of PDGFRβ by siRNA decreased the stability of TβRI and delayed TGFβ-induced signaling. We further show that the hyaluronan receptor CD44 interacts with both PDGFRβ and TβRI. Depletion of CD44 by siRNA increased signaling via PDGFRβ and TβRI by stabilizing the receptor proteins. Our data suggest that cross-talk between PDGFRβ and TβRI occurs in dermal fibroblasts and that CD44 negatively modulates signaling via these receptors.

Indexed as

AnimalsBecaplerminChlorocebus aethiopsCOS CellsHumansHyaluronan ReceptorsProtein BindingProtein Serine-Threonine KinasesProtein StabilityProto-Oncogene Proteins c-sisReceptor, Platelet-Derived Growth Factor betaReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type ISignal TransductionTransforming Growth Factor betaBecaplerminCD44 protein, humanHyaluronan ReceptorsProtein Serine-Threonine KinasesProto-Oncogene Proteins c-sisReceptor, Platelet-Derived Growth Factor betaReceptors, Transforming Growth Factor betaReceptor, Transforming Growth Factor-beta Type ITransforming Growth Factor betaCD44Cell SignalingCell Surface ReceptorCellular RegulationPDGFTransforming Growth Factor β (TGF-β)

Identifiers

PMID24860093
PMCPMC4094084

What OpenQuestion holds

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Registered trials

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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.