Evidence map›Paper›PMID 16287859›Full record

ArticleMolecular and cellular biology2005

Altered integration of matrilin-3 into cartilage extracellular matrix in the absence of collagen IX.

Bastian Budde, Katrin Blumbach, Joni Ylöstalo, Frank Zaucke, Harald W A Ehlen, Raimund Wagener, Leena Ala-Kokko, Mats Paulsson, Peter Bruckner, Susanne Grässel

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

45 citing papers in PubMed, 143 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Matricellular proteins in cutaneous wound healing.Frontiers in cell and developmental biology · 2022
    Review
  5. Review
  6. Review
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Extracellular Distribution of Collagen II and Perifibrillar Adapter Proteins in Healthy and Osteoarthritic Human Knee Joint Cartilage.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2017
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. 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

10 authors at 4 institutions in 2 countries.

Bastian BuddeInstitute for Physiological Chemistry and Pathobiochemistry, University of Münster, Münster, Germany.
Katrin Blumbach
Joni Ylöstalo
Frank Zaucke
Harald W A Ehlen
Raimund Wagener
Leena Ala-Kokko
Mats Paulsson
Peter Bruckner
Susanne Grässel
University of Münster · DEUniversity of Oulu · FIUniversity of Cologne · DEUniversity of Regensburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The matrilins are a family of four noncollagenous oligomeric extracellular matrix proteins with a modular structure. Matrilins can act as adapters which bridge different macromolecular networks. We therefore investigated the effect of collagen IX deficiency on matrilin-3 integration into cartilage tissues. Mice harboring a deleted Col9a1 gene lack synthesis of a functional protein and produce cartilage fibrils completely devoid of collagen IX. Newborn collagen IX knockout mice exhibited significantly decreased matrilin-3 and cartilage oligomeric matrix protein (COMP) signals, particularly in the cartilage primordium of vertebral bodies and ribs. In the absence of collagen IX, a substantial amount of matrilin-3 is released into the medium of cultured chondrocytes instead of being integrated into the cell layer as in wild-type and COMP-deficient cells. Gene expression of matrilin-3 is not affected in the absence of collagen IX, but protein extraction from cartilage is greatly facilitated. Matrilin-3 interacts with collagen IX-containing cartilage fibrils, while fibrils from collagen IX knockout mice lack matrilin-3, and COMP-deficient fibrils exhibit an intermediate integration. In summary, the integration of matrilin-3 into cartilage fibrils occurs both by a direct interaction with collagen IX and indirectly with COMP serving as an adapter. Matrilin-3 can be considered as an interface component, capable of interconnecting macromolecular networks and mediating interactions between cartilage fibrils and the extrafibrillar matrix.

Indexed as

AnimalsAnimals, NewbornAntibody SpecificityCells, CulturedChondrocytesCollagen Type IXExtracellular MatrixExtracellular Matrix ProteinsGene ExpressionGlycoproteinsImmune SeraImmunohistochemistryMatrilin ProteinsMiceMice, KnockoutMicroscopy, ElectronCollagen Type IXExtracellular Matrix ProteinsGlycoproteinsImmune SeraMatn1 protein, mouseMatn3 protein, mouseMatrilin Proteins

Identifiers

PMID16287859
PMCPMC1291247
OpenAlexW2157827546

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.