Evidence map›Paper›PMID 23798676›Full record

ArticleThe Journal of biological chemistry2013

Degradome products of the matricellular protein CCN1 as modulators of pathological angiogenesis in the retina.

Jinok Choi, Ann Lin, Eric Shrier, Lester F Lau, Maria B Grant, Brahim Chaqour

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

25 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. An overview of CCN4 (WISP1) role in human diseases.Journal of translational medicine · 2024
    Review
  3. Article
  4. Review
  5. Article
  6. LncRNAFrontiers in medicine · 2022
    Article
  7. Review
  8. Article
  9. Review
  10. Blocking CTGF/CCN2 reduces established skeletal muscle fibrosis in a rat model of overuse injury.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020
    Article
  11. Review
  12. Article
  13. Blocking CCN2 Reduces Progression of Sensorimotor Declines and Fibrosis in a Rat Model of Chronic Repetitive Overuse.Journal of orthopaedic research : official publication of the Orthopaedic Research Society · 2019
    Article
  14. Article
  15. The matricellular protein CCN1 in tissue injury repair.Journal of cell communication and signaling · 2018
    Review
  16. Review
  17. Article
  18. Regulating the regulators of angiogenesis by CCN1 and taking it up a Notch.Journal of cell communication and signaling · 2016
    Article
  19. Article
  20. Review
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

6 authors at 4 institutions in 2 countries.

Jinok ChoiDepartment of Cell Biology, State University of New York Eye Institute, Downstate Medical Center, Brooklyn, New York 11203, USA.
Ann Lin
Eric Shrier
Lester F Lau
Maria B Grant
Brahim Chaqour
Institute of Cell Biology · UASUNY Downstate Health Sciences University · USUniversity of Florida · USUniversity of Illinois Chicago · US

Funding

Targeting the IGF-1 System in Retinal AngiogenesisR01EY007739 · NEI · UNIVERSITY OF FLORIDA · PI ABCOUWER, STEVEN F, GRANT, MARIA BARTOLOMEO · 1995 to 2015
$5.4M
Regulation of TNF-alpha by Integrin-Mediated Matrix SignalingR01GM078492 · NIGMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LAU, LESTER F · 2007 to 2018
$4.3M
The Matricellular Protein CCN1 in Wound HealingR01AR061791 · NIAMS · UNIVERSITY OF ILLINOIS AT CHICAGO · PI LAU, LESTER F · 2011 to 2021
$3.8M
Regulation and Function of the Matricellular Protein CCN1 in Ischemic RetinopathyR01EY022091 · NEI · SUNY DOWNSTATE MEDICAL CENTER · PI CHAQOUR, BRAHIM · 2012 to 2017
$2.0M
Cyr61/CCN1-Induced Angiogenesis and Vasculogenesis in the RetinaR21EY019387 · NEI · SUNY DOWNSTATE MEDICAL CENTER · PI CHAQOUR, BRAHIM · 2009 to 2010
$472k
HORMONES &NEOVASCULARIZATION IN DIABETIC RETINOPATHYR29EY007739 · NEI · UNIVERSITY OF FLORIDA · PI GRANT, MARIA B · 1989 to 1993
–
NEI NIH HHS EY007739-23NEI NIH HHS EY01260-12NEI NIH HHS EY019387-01A1NEI NIH HHS EY022091-01NEI NIH HHS R01 EY007739NEI NIH HHS R01 EY022091NEI NIH HHS R21 EY019387NIAMS NIH HHS R01 AR061791NIGMS NIH HHS R01 GM078492
6 · The paper itself

Abstract

CCN1 is a matricellular protein involved in normal vascular development and tissue repair. CCN1 exhibits cell- and context-dependent activities that are reflective of its tetramodular structure phylogenetically linked to four domains found in various matrix proteins. Here, we show that vitreal fluids from patients with proliferative diabetic retinopathy (PDR) were enriched with a two-module form of CCN1 comprising completely or partially the insulin-like growth factor-binding protein (IGFBP) and von Willebrand factor type C (vWC) domains. The two- and three-module forms comprising, in addition to IGFBP and vWC, the thrombospondin type 1 (TSP1) repeats are CCN1 degradome products by matrix metalloproteinase-2 and -14. The functional significance of CCN1 and its truncated variants was determined in the mouse model of oxygen-induced retinopathy, which simulates neovascular growth associated with PDR and assesses treatment outcomes. In this model, lentivirus-mediated expression of either CCN1 or the IGFBP-vWC-TSP1 form reduced ischemia-induced neovascularization, whereas ectopic expression of the IGFBP-vWC variant exacerbated pathological angiogenesis. The IGFBP-vWC form has potent proangiogenic properties promoting retinal endothelial cell growth, migration, and three-dimensional tubular structure formation, whereas the IGFBP-vWC-TSP1 variant suppressed cell growth and angiogenic gene expression. Both IGFBP-vWC and IGFBP-vWC-TSP1 forms exhibited predictable variations of their domain folding that enhanced their functional potential. These data provide new insights into the formation and activities of CCN1-truncated variants and raise the predictive value of the form containing completely or partially the IGFBP and vWC domains as a surrogate marker of CCN1 activity in PDR distinguishing pathological from physiological angiogenesis.

Indexed as

ProteolysisAnimalsBiomarkersCell LineCysteine-Rich Protein 61Diabetic RetinopathyEndothelial CellsGene Expression RegulationHumansInsulin-Like Growth Factor Binding ProteinsMiceNeovascularization, PathologicProtein FoldingProtein Structure, TertiaryRatsThrombospondin 1BiomarkersCCN1 protein, humanCCN1 protein, mouseCCN1 protein, ratCysteine-Rich Protein 61Insulin-Like Growth Factor Binding ProteinsThbs1 protein, ratThrombospondin 1von Willebrand FactorAngiogenesisCysteine-rich Protein 61 (CCN1)Endothelial CellExtracellular Matrix ProteinsIschemiaMatricellular ProteinMatrix Metalloproteinase (MMP)Protein DegradationProtein DomainsRetina

Identifiers

PMID23798676
PMCPMC3743481
OpenAlexW2031493375

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.