Evidence map›Paper›PMID 10953033›Full record

ArticleThe Journal of clinical investigation2000

Thrombin activates a Y box-binding protein (DNA-binding protein B) in endothelial cells.

O I Stenina, E J Poptic, P E DiCorleto

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of clinical investigation, 2000. 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
2.1field-weighted citation impact, top 13% 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, 70 citations in OpenAlex.

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  9. The role of cold shock domain proteins in inflammatory diseases.Journal of molecular medicine (Berlin, Germany) · 2014
    Review
  10. Article
  11. Review
  12. Thrombin induces endothelial arginase through AP-1 activation.American journal of physiology. Cell physiology · 2010
    Article
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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

3 authors at 1 institution in 1 country.

O I SteninaDepartment of Cell Biology, Lerner Research Institute, The Cleveland Clinic Foundation, Cleveland, Ohio 44195, USA.
E J Poptic
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 RR00080NHLBI NIH HHS HL29582NHLBI NIH HHS P01 HL029582
6 · The paper itself

Abstract

Thrombin stimulates the expression of multiple genes in endothelial cells (ECs), but the trans-acting factors responsible for this induction remain undefined. We have previously described a thrombin-inducible nuclear factor (TINF), which binds to an element in the PDGF B promoter and is responsible for the thrombin inducibility of this gene. Inactive cytoplasmic TINF is rapidly activated and translocated to nuclei of ECs upon stimulation with thrombin. We have now purified TINF from thrombin-treated ECs. Amino acid sequencing revealed it to be a member of the Y-box protein family, and the sole Y-box protein-encoding cDNA we detected in human or bovine ECs corresponded to DNA-binding protein B (dbpB). DbpB translocated to the nucleus after thrombin stimulation of ECs as shown by FACS analysis of nuclei from ECs expressing GFP-dbpB fusion proteins. During thrombin activation, dbpB was found to be cleaved, yielding a 30-kDa NH(2)-terminal fragment that recognized the thrombin-response element sequence, but not the Y-box consensus sequence. Preincubation of ECs with protein tyrosine phosphatase inhibitors completely blocked dbpB activation by thrombin and blocked induction of endogenous PDGF B-chain mRNA and promoter activation by thrombin. Y-box proteins are known to act constitutively to regulate the expression of several genes. Activation of this class of transcription factors in response to thrombin or any other agonist represents a novel signaling pathway.

Indexed as

CCAAT-Enhancer-Binding ProteinsTranscription FactorsAmino Acid SequenceAnimalsBase SequenceCattleCells, CulturedDNA-Binding ProteinsDNA ProbesEndothelium, VascularGene ExpressionHumansNFI Transcription FactorsNuclear ProteinsRNA, MessengerThrombinCCAAT-Enhancer-Binding ProteinsDNA-Binding ProteinsDNA ProbesNFI Transcription FactorsNuclear ProteinsRNA, MessengerThrombinTranscription FactorsY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID10953033
PMCPMC380248
OpenAlexW2128968848

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.