Evidence map›Paper›PMID 20138147›Full record

ArticleMatrix biology : journal of the International Society for Matrix Biology2010

Interaction between cartilage oligomeric matrix protein and extracellular matrix protein 1 mediates endochondral bone growth.

Li Kong, Qingyun Tian, Fengjin Guo, Maria T Mucignat, Roberto Perris, Sandy Sercu, Joseph Merregaert, Paul E Di Cesare, Chuan-Ju Liu

Open access · greenAbstract read
In one paragraph

Article in Matrix biology : journal of the International Society for Matrix Biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
1.7field-weighted citation impact, top 17% 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

27 citing papers in PubMed, 48 citations in OpenAlex.

  1. Trial
  2. Article
  3. Review
  4. Osteoblast-Derived ECM1 Promotes Anti-Androgen Resistance in Bone Metastatic Prostate Cancer.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025
    Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Label-free quantitative proteomics reveals molecular correlates of altered biomechanical properties in molar incisor hypomineralization (MIH): an in vitro study.European archives of paediatric dentistry : official journal of the European Academy of Paediatric Dentistry · 2022
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Serum level of cartilage oligomeric matrix protein is lower in children with idiopathic scoliosis than in non-scoliotic controls.European spine journal : official publication of the European Spine Society, the European Spinal Deformity Society, and the European Section of the Cervical Spine Research Society · 2015
    Article
  20. Invoking the power of thrombospondins: regulation of thrombospondins expression.Matrix biology : journal of the International Society for Matrix Biology · 2014
    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

9 authors at 4 institutions in 3 countries.

Li KongDepartment of Orthopaedic Surgery, New York University School of Medicine, New York, NY 10003, United States.
Qingyun Tian
Fengjin Guo
Maria T Mucignat
Roberto Perris
Sandy Sercu
Joseph Merregaert
Paul E Di Cesare
Chuan-Ju Liu
New York University · USUniversity of Antwerp · BEUniversity of Parma · ITUniversity of California Davis Medical Center · US

Funding

Degradative COMP Fragments as a Biomarker of ArthritisK01AR053210 · NIAMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI LIU, CHUANJU · 2007 to 2011
$638k
THE ROLE OF p204 IN OSTEOGENESISR21AR052676 · NIAMS · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI LIU, CHUANJU · 2006 to 2007
$404k
Role and Regulation of ADAMTS-12 in the Cartilage CatabolismR03AG029388 · NIA · NEW YORK UNIVERSITY SCHOOL OF MEDICINE · PI LIU, CHUANJU · 2007 to 2008
$137k
NIAMS NIH HHS AR050620NIAMS NIH HHS AR053210NIAMS NIH HHS K01 AR053210NIAMS NIH HHS R21 AR052676NIA NIH HHS AG029388NIA NIH HHS R03 AG029388
6 · The paper itself

Abstract

In an effort to define the biological functions of COMP, a functional genetic screen was performed. This led to the identification of extracellular matrix protein 1 (ECM1) as a novel COMP-associated partner. COMP directly binds to ECM1 both in vitro and in vivo. The EGF domain of COMP and the C-terminus of ECM1 mediate the interaction between them. COMP and ECM1 colocalize in the growth plates invivo. ECM1 inhibits chondrocyte hypertrophy, matrix mineralization, and endochondral bone formation, and COMP overcomes the inhibition by ECM1. In addition, COMP-mediated neutralization of ECM1 inhibition depends on their interaction, since COMP largely fails to overcome the ECM1 inhibition in the presence of the EGF domain of COMP, which disturbs the association of COMP and ECM1. These findings provide the first evidence linking the association of COMP and ECM1 and the biological significance underlying the interaction between them in regulating endochondral bone growth.

Indexed as

AnimalsBone and BonesBone DevelopmentChondrocytesEmbryo, MammalianExtracellular Matrix ProteinsFetusGlycoproteinsGrowthGrowth PlateMatrilin ProteinsMiceMice, Inbred C57BLOsteogenesisProtein BindingExtracellular Matrix ProteinsGlycoproteinsMatn1 protein, mouseMatrilin Proteins

Identifiers

PMID20138147
PMCPMC2862898
OpenAlexW2087580238

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.