Evidence map›Paper›PMID 22573329›Full record

ArticleThe Journal of biological chemistry2012

Collagen XII and XIV, new partners of cartilage oligomeric matrix protein in the skin extracellular matrix suprastructure.

Pallavi Agarwal, Daniela Zwolanek, Douglas R Keene, Jan-Niklas Schulz, Katrin Blumbach, Dick Heinegård, Frank Zaucke, Mats Paulsson, Thomas Krieg, Manuel Koch and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
5.5field-weighted citation impact, top 3% 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

68 citing papers in PubMed, 143 citations in OpenAlex.

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  12. Matricellular Proteins in the Homeostasis, Regeneration, and Aging of Skin.International journal of molecular sciences · 2023
    Review
  13. Collagen XII regulates stromal wound closure.Experimental eye research · 2023
    Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Tissue mechanics coevolves with fibrillar matrisomes in healthy and fibrotic tissues.Matrix biology : journal of the International Society for Matrix Biology · 2022
    Review
  19. Article
  20. Article

8 more citing papers are in PubMed but not listed here.

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 at 3 institutions in 3 countries.

Pallavi AgarwalDepartment of Dermatology, University of Cologne, Cologne 50937, Germany.
Daniela Zwolanek
Douglas R Keene
Jan-Niklas Schulz
Katrin Blumbach
Dick Heinegård
Frank Zaucke
Mats Paulsson
Thomas Krieg
Manuel Koch
Beate Eckes
University of Cologne · DELund University · SEShriners Hospitals for Children - Portland · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The tensile and scaffolding properties of skin rely on the complex extracellular matrix (ECM) that surrounds cells, vasculature, nerves, and adnexus structures and supports the epidermis. In the skin, collagen I fibrils are the major structural component of the dermal ECM, decorated by proteoglycans and by fibril-associated collagens with interrupted triple helices such as collagens XII and XIV. Here we show that the cartilage oligomeric matrix protein (COMP), an abundant component of cartilage ECM, is expressed in healthy human skin. COMP expression is detected in the dermal compartment of skin and in cultured fibroblasts, whereas epidermis and HaCaT cells are negative. In addition to binding collagen I, COMP binds to collagens XII and XIV via their C-terminal collagenous domains. All three proteins codistribute in a characteristic narrow zone in the superficial papillary dermis of healthy human skin. Ultrastructural analysis by immunogold labeling confirmed colocalization and further revealed the presence of COMP along with collagens XII and XIV in anchoring plaques. On the basis of these observations, we postulate that COMP functions as an adapter protein in human skin, similar to its function in cartilage ECM, by organizing collagen I fibrils into a suprastructure, mainly in the vicinity of anchoring plaques that stabilize the cohesion between the upper dermis and the basement membrane zone.

Indexed as

AnimalsBasement MembraneCartilage Oligomeric Matrix ProteinChild, PreschoolCollagenCollagen Type ICollagen Type XIIDermisExtracellular MatrixExtracellular Matrix ProteinsFibroblastsGlycoproteinsHEK293 CellsHumansInfantKeratinocytesCartilage Oligomeric Matrix ProteinCOL12A1 protein, humanCOL14A1 protein, humanCol14a1 protein, mouseCollagenCollagen Type ICollagen Type XIIExtracellular Matrix ProteinsGlycoproteinsMatn1 protein, mouseMatrilin ProteinsRecombinant ProteinsTSP5 protein, human

Identifiers

PMID22573329
PMCPMC3391150
OpenAlexW2080242496

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.