Evidence map›Paper›PMID 16611630›Full record

ArticleThe Journal of biological chemistry2006

ADAMTS-12 associates with and degrades cartilage oligomeric matrix protein.

Chuan-ju Liu, Wei Kong, Ke Xu, Yi Luan, Kiril Ilalov, Bantoo Sehgal, Shuang Yu, Ronald D Howell, Paul E Di Cesare

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
2.8field-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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 111 citations in OpenAlex.

  1. Pooled it
  2. Trial
  3. An Overview of ADAMTS Proteases.Methods in molecular biology (Clifton, N.J.) · 2026
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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

9 authors at 3 institutions in 2 countries.

Chuan-ju LiuDepartment of Orthopaedic Surgery, Musculoskeletal Research Center, New York University Hospital for Joint Diseases, New York, New York 10003, USA. chuanju.liu@med.nyu.edu
Wei Kong
Ke Xu
Yi Luan
Kiril Ilalov
Bantoo Sehgal
Shuang Yu
Ronald D Howell
Paul E Di Cesare
New York University Langone Orthopedic Hospital · USThe Orthopaedic Institute · USYale University · US

Funding

Physiological Role of ADAMTS-7B in ArthritisR03AR052022 · NIAMS · HOSPITAL FOR JOINT DISEASES ORTHO INST · PI LIU, CHUANJU · 2005 to 2007
$261k
NIAMS NIH HHS AR052022NIAMS NIH HHS R03 AR052022
6 · The paper itself

Abstract

Loss of articular cartilage because of extracellular matrix breakdown is the hallmark of arthritis. Degradative fragments of cartilage oligomeric matrix protein (COMP), a prominent noncollagenous matrix component in articular cartilage, have been observed in the cartilage, synovial fluid, and serum of arthritis patients. The molecular mechanism of COMP degradation and the enzyme(s) responsible for it, however, remain largely unknown. ADAMTS-12 (a disintegrin and metalloprotease with thrombospondin motifs) was shown to associate with COMP both in vitro and in vivo. ADAMTS-12 selectively binds to only the epidermal growth factor-like repeat domain of COMP of the four functional domains tested. The four C-terminal TSP-1-like repeats of ADAMTS-12 are shown to be necessary and sufficient for its interaction with COMP. Recombinant ADAMTS-12 is capable of digesting COMP in vitro. The COMP-degrading activity of ADAMTS-12 requires the presence of Zn2+ and appropriate pH (7.5-9.5), and the level of ADAMTS-12 in the cartilage and synovium of patients with both osteoarthritis and rheumatoid arthritis is significantly higher than in normal cartilage and synovium. Together, these findings indicate that ADAMTS-12 is a new COMP-interacting and -degrading enzyme and thus may play an important role in the COMP degradation in the initiation and progression of arthritis.

Indexed as

ADAM ProteinsADAMTS ProteinsBone and BonesCartilage Oligomeric Matrix ProteinExtracellular Matrix ProteinsGlycoproteinsHumansHydrolysisImmunoprecipitationMatrilin ProteinsPolymerase Chain ReactionProtein BindingADAM ProteinsADAMTS12 protein, humanADAMTS ProteinsCartilage Oligomeric Matrix ProteinExtracellular Matrix ProteinsGlycoproteinsMatrilin ProteinsTSP5 protein, human

Identifiers

PMID16611630
PMCPMC1483932
OpenAlexW2018029080

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.