Evidence map›Paper›PMID 11390977›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Thrombin induces the release of the Y-box protein dbpB from mRNA: a mechanism of transcriptional activation.

O I Stenina, K M Shaneyfelt, P E DiCorleto

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.4field-weighted citation impact, top 19% 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

20 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. Review
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  4. Article
  5. Article
  6. The role of cold shock domain proteins in inflammatory diseases.Journal of molecular medicine (Berlin, Germany) · 2014
    Review
  7. Article
  8. Article
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  18. Y box-binding protein 1 induces resistance to oncogenic transformation by the phosphatidylinositol 3-kinase pathway.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  19. Article
  20. 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

3 authors at 1 institution in 1 country.

O I SteninaDepartment of Cell Biology, Lerner Research Institute of The Cleveland Clinic Foundation, Cleveland, OH 44195, USA.
K M Shaneyfelt
P E DiCorleto
Cleveland Clinic · US

Funding

Vascular Cell function and AtherosclerosisP01HL029582 · NHLBI · CLEVELAND CLINIC LERNER COM-CWRU · PI FOX, PAUL L · 1985 to 2019
$32.0M
Zosuquidar trihydrochloride for acute myeloid leukemia &refractory anemiaM01RR000080 · NCRR · UNIVERSITY HOSPITALS OF CLEVELAND · PI DAVIS, PAMELA B · 1985 to 2007
$22.2M
NCRR NIH HHS M01 RR000080NCRR NIH HHS RR-00080NHLBI NIH HHS HL 29582NHLBI NIH HHS P01 HL029582
6 · The paper itself

Abstract

We have recently demonstrated that thrombin induces expression of the platelet-derived growth factor B-chain gene in endothelial cells (EC) through activation of the Y-box binding protein DNA-binding protein B (dbpB). We now present evidence that dbpB is activated by a novel mechanism: proteolytic cleavage leading to release from mRNA, nuclear translocation, and induction of thrombin-responsive genes. Cytosolic, full-length dbpB (50 kDa) was rapidly cleaved to a 30-kDa species upon thrombin stimulation of EC. This truncated, "active" dbpB exhibited nuclear localization and binding affinity for the thrombin response element sequence, which is distinct from the Y-box sequence. Oligo(dT) affinity chromatography revealed that cytosolic dbpB from control EC, but not active dbpB from thrombin-treated EC, was bound to mRNA. Latent dbpB immunoprecipitated from cytosolic extracts of control EC was activated by ribonuclease treatment. Furthermore, when EC cytosolic extracts were subjected to Nycodenz gradient centrifugation, latent dbpB fractionated with mRNA, whereas active dbpB fractionated with free proteins. The cytosolic retention domain of dbpB, which we localized to the region 247-267, was proteolytically cleaved during its activation. In contrast to full-length dbpB, truncated dbpB stimulated platelet-derived growth factor B-chain and tissue factor promoter activity by over 5-fold when transiently cotransfected with reporter constructs. These results suggest a novel mode of transcription factor activation in which an agonist causes release from mRNA of a latent transcription factor leading to its transport to the nucleus and its regulation of target gene expression.

Indexed as

Transcriptional ActivationTranscription Factors3T3 CellsAmino Acid SequenceAnimalsAortaBinding SitesCattleCCAAT-Enhancer-Binding ProteinsCell NucleusCytosolDNA-Binding ProteinsEndothelium, VascularMiceMolecular Sequence DataNFI Transcription FactorsCCAAT-Enhancer-Binding ProteinsDNA-Binding ProteinsNFI Transcription FactorsNuclear ProteinsPlatelet-Derived Growth FactorRecombinant ProteinsRNA, MessengerRNA, Ribosomal, 5SThrombinTranscription FactorsY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID11390977
PMCPMC34659
OpenAlexW2164143213

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.