Evidence map›Paper›PMID 24319267›Full record

ArticleJournal of immunology (Baltimore, Md. : 1950)2014

Soluble gC1qR is an autocrine signal that induces B1R expression on endothelial cells.

Berhane Ghebrehiwet, Yan Ji, Alisa Valentino, Lina Pednekar, Mahalakshmi Ramadass, David Habiel, Richard R Kew, Kinga H Hosszu, Dennis K Galanakis, Uday Kishore and 1 more

Abstract read
In one paragraph

Article in Journal of immunology (Baltimore, Md. : 1950), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. Article
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  16. Soluble gC1qR in Blood and Body Fluids: Examination in a Pancreatic Cancer Patient Cohort.International journal of cancer research and molecular mechanisms · 2015
    Article
  17. 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

11 authors.

Berhane GhebrehiwetDepartment of Medicine, Stony Brook University, Stony Brook, NY 11794;
Yan Ji
Alisa Valentino
Lina Pednekar
Mahalakshmi Ramadass
David Habiel
Richard R Kew
Kinga H Hosszu
Dennis K Galanakis
Uday Kishore
Ellinor I B Peerschke

Funding

Mechanisms of a Novel Chemotactic Cofactor for C5aR01GM063769 · NIGMS · STATE UNIVERSITY NEW YORK STONY BROOK · PI KEW, RICHARD R · 2001 to 2011
$2.6M
gC1q-R/p33: structure function and role on inflammation.R01AI060866 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI GHEBREHIWET, BERHANE · 2006 to 2009
$1.2M
The role of C1q in regulation of monocyte to dendritic cell transitionR01AI084178 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI GHEBREHIWET, BERHANE · 2009 to 2010
$602k
gC1q-R/P33: Structure-function and role in inflammationR56AI060866 · NIAID · STATE UNIVERSITY NEW YORK STONY BROOK · PI GHEBREHIWET, BERHANE · 2012 to 2012
$377k
NIAID NIH HHS R01 AI 060866NIAID NIH HHS R01 AI060866NIAID NIH HHS R01 AI-084178NIAID NIH HHS R01 AI084178NIAID NIH HHS R56 AI060866NIGMS NIH HHS R01 GM-063769NIGMS NIH HHS R01 GM063769
6 · The paper itself

Abstract

Bradykinin (BK) is one of the most potent vasodilator agonists known and belongs to the kinin family of proinflammatory peptides. BK induces its activity via two G protein-coupled receptors: BK receptor 1 (B1R) and BK receptor 2. Although BK receptor 2 is constitutively expressed on endothelial cells (ECs), B1R is induced by IL-1β. The C1q receptor, receptor for the globular heads of C1q (gC1qR), which plays a role in BK generation, is expressed on activated ECs and is also secreted as soluble gC1qR (sgC1qR). Because sgC1qR can bind to ECs, we hypothesized that it may also serve as an autocrine/paracrine signal for the induction of B1R expression. In this study, we show that gC1qR binds to ECs via a highly conserved domain consisting of residues 174-180, as assessed by solid-phase binding assay and deconvolution fluorescence microscopy. Incubation of ECs (24 h, 37 °C) with sgC1qR resulted in enhancement of B1R expression, whereas incubation with gC1qR lacking aa 174-180 and 154-162 had a diminished effect. Binding of sgC1qR to ECs was through surface-bound fibrinogen and was inhibited by anti-fibrinogen. In summary, our data suggest that, at sites of inflammation, sgC1qR can enhance vascular permeability by upregulation of B1R expression through de novo synthesis, as well as rapid translocation of preformed B1R.

Indexed as

Autocrine CommunicationSignal TransductionBinding SitesCarrier ProteinsCell LineCell MembraneEndothelial CellsFibrinogenGene Expression RegulationHumansMitochondrial ProteinsProtein BindingProtein Interaction Domains and MotifsProtein TransportReceptor, Bradykinin B1C1QBP protein, humanCarrier ProteinsFibrinogenMitochondrial ProteinsReceptor, Bradykinin B1

Identifiers

PMID24319267
PMCPMC3876932

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.