Evidence map›Paper›PMID 30738042›Full record

ArticleLife sciences2019

Exchange protein directly activated by cAMP plays a critical role in regulation of vascular fibrinolysis.

Xi He, Aleksandra Drelich, Shangyi Yu, Qing Chang, Dejun Gong, Yixuan Zhou, Yue Qu, Yang Yuan, Zhengchen Su, Yuan Qiu and 9 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Life sciences, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
1.1field-weighted citation impact, top 23% 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

10 citing papers in PubMed, 19 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Annexin Animal Models-From Fundamental Principles to Translational Research.International journal of molecular sciences · 2021
    Review
  9. Article
  10. 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

19 authors at 6 institutions in 2 countries.

Xi HeDepartment of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA; Department of Cardiovascular Surgery, Changhai Hospital, Shanghai 200433, China.
Aleksandra DrelichDepartment of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Shangyi YuDepartment of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA; Department of Cardiovascular Surgery, Changhai Hospital, Shanghai 200433, China.
Qing ChangDepartment of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Dejun GongDepartment of Cardiovascular Surgery, Changhai Hospital, Shanghai 200433, China.
Yixuan ZhouDepartment of Cardiovascular Surgery, Changhai Hospital, Shanghai 200433, China.
Yue QuDepartment of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Yang YuanDepartment of Cardiovascular Surgery, Changhai Hospital, Shanghai 200433, China.
Zhengchen SuDepartment of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Yuan QiuDepartment of Mathematics and Statistics, Texas Tech University, Lubbock, TX 79409, USA.
Shao-Jun TangDepartment of Neuroscience and Cell Biology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Angelo GaitasDepartment of Neurology, Icahn School of Medicine at Mount Sinai, NY 10029, USA.
Thomas KsiazekDepartment of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Zhiyun XuDepartment of Cardiovascular Surgery, Changhai Hospital, Shanghai 200433, China.
Jia ZhouDepartment of Pharmacology and Toxicology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Zongdi FengCenter for Vaccines and Immunity, The Research Institute at Nationwide Children's Hospital, Columbus, OH 43205, USA.
Maki WakamiyaDepartment of Neurology, University of Texas Medical Branch, Galveston, TX 77555, USA.
Fanglin LuDepartment of Cardiovascular Surgery, Changhai Hospital, Shanghai 200433, China. Electronic address: lufanglin@smmu.edu.cn.
Bin GongDepartment of Pathology, University of Texas Medical Branch, Galveston, TX 77555, USA. Electronic address: bigong@utmb.edu.
The University of Texas Medical Branch at Galveston · USSecond Military Medical University · CNChanghai Hospital · CNIcahn School of Medicine at Mount Sinai · USNationwide Children's Hospital · USTexas Tech University · US

Funding

Wnt signaling in glial activation during HIV-associated chronic pain pathogenesisR01NS079166 · NINDS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI TANG, SHAO-JUN · 2012 to 2021
$5.5M
Antiretroviral Therapy and Neuroinflammation in the CNSR01NS095747 · NINDS · UNIVERSITY OF TEXAS MED BR GALVESTON · PI CHUNG, JIN M · 2016 to 2020
$2.6M
Epac1 Plays a Critical Role in Bacterial Adhesion during RickettsiosesR01AI121012 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI GONG, BIN · 2016 to 2020
$1.9M
Targeting the Host Adenosine A2A Receptor to Protect Against Fatal Rickettsiosis Using an Approved Parkinson's Disease DrugR21AI137785 · NIAID · UNIVERSITY OF TEXAS MED BR GALVESTON · PI GONG, BIN · 2018 to 2019
$440k
NIAID NIH HHS R01 AI121012NIAID NIH HHS R21 AI137785NINDS NIH HHS R01 NS079166NINDS NIH HHS R01 NS095747
6 · The paper itself

Abstract

Plasmin-mediated fibrinolysis at the surface of vascular endothelial cells (SVEC) plays a key role in maintaining vascular hemostasis, in which the cAMP pathway participates. After externalization to the SVEC, annexin A2 (ANXA2) serves as a platform for conversion of plasminogen to plasmin. Here we describe a regulatory role of the exchange protein directly activated by cAMP (EPAC) in ANXA2 externalization and vascular fibrinolysis. Knockout of EPAC1 in mice results in a decreased ANXA2 expression on the SVEC associated with increased fibrin deposition and fibrinolytic dysfunction. Reduced levels of EPAC1 are also found in endocardial tissues beneath atrial mural thrombi in patients. Notably, administration of recombinant ANXA2 ameliorates fibrinolytic dysfunction in the EPAC1-null mice. Mechanistically, EPAC1 regulates the SVEC plasminogen conversion depended on ANXA2. EPAC1 promotes tyrosine-23 phosphorylation of ANXA2, a prerequisite for its recruitment to the SVEC. Our data thus reveal a novel regulatory role for EPAC1 in vascular fibrinolysis.

Indexed as

AnimalsAnnexin A2Cell MembraneCyclic AMPEndothelial CellsEndothelium, VascularFibrinolysinFibrinolysisGuanine Nucleotide Exchange FactorsHomeostasisHumansMiceMice, KnockoutPhosphorylationPlasminogenProteolysisAnnexin A2ANXA2 protein, humanCyclic AMPEpac protein, mouseFibrinolysinGuanine Nucleotide Exchange FactorsPlasminogenRAPGEF3 protein, humanAnnexin A2Atomic force microscopyEPAC1ThrombosisVascular endothelial fibrinolysis

Identifiers

PMID30738042
PMCPMC6918504
OpenAlexW2951853551

What OpenQuestion holds

Textmetadata
LicenceTDM
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.