Evidence map›Paper›PMID 8762055›Full record

ReviewThe Histochemical journal1996

Phagocytosis and intracellular digestion of collagen, its role in turnover and remodelling.

V Everts, E van der Zee, L Creemers, W Beertsen

Abstract readReview
PubMed Publisher
In one paragraph

Review in The Histochemical journal, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 89 papers.

0numbers the graph read from it
0cells of the map it votes in
89citing papers in PubMed
4.2field-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

89 citing papers in PubMed, 344 citations in OpenAlex.

  1. Review
  2. Review
  3. The life cycle of type IV collagen.Matrix biology : journal of the International Society for Matrix Biology · 2025
    Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Article
  9. Novel approaches for periodontal tissue engineering.Genesis (New York, N.Y. : 2000) · 2022
    Review
  10. Article
  11. Article
  12. Article
  13. Beclin 1, LC3 and P62 Expression in Equine Sarcoids.Animals : an open access journal from MDPI · 2021
    Article
  14. Review
  15. You Say You Want a Resolution (of Fibrosis).American journal of respiratory cell and molecular biology · 2020
    Review
  16. Article
  17. Review
  18. Article
  19. Article
  20. The Peculiar Pattern of Type IV Collagen Deposition in Epiretinal Membranes.The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society · 2020
    Article

29 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

4 authors at 1 institution in 1 country.

V EvertsDepartment of Periodontology, Academic Centre for Dentistry Amsterdam (ACTA), The Netherlands.
E van der Zee
L Creemers
W Beertsen
Academic Center for Dentistry Amsterdam · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Collagens of most connective tissues are subject to continuous remodelling and turnover, a phenomenon which occurs under both physiological and pathological conditions. Degradation of these proteins involves participation of a variety of proteolytic enzymes including members of the following proteinase classes: matrix metalloproteinases (e.g. collagenase, gelatinase and stromelysin), cysteine proteinases (e.g. cathepsin B and L) and serine proteinases (e.g. plasmin and plasminogen activator). Convincing evidence is available indicating a pivotal role for matrix metalloproteinases, in particular collagenase, in the degradation of collagen under conditions of rapid remodelling, e.g. inflammation and involution of the uterus. Under steady state conditions, such as during turnover of soft connective tissues, involvement of collagenase has yet to be demonstrated. Under these circumstances collagen degradation is likely to take place particularly within the lysosomal apparatus after phagocytosis of the fibrils. We propose that this process involves the following steps: (i) recognition of the fibril by membrane-bound receptors (integrins?), (ii) segregation of the fibril, (iii) partial digestion of the fibril and/or its surrounding non-collagenous proteins by matrix metalloproteinases (possibly gelatinase), and finally (iv) lysosomal digestion by cysteine proteinases, such as cathepsin B and/or L. Modulation of this pathway is carried out under the influence of growth factors and cytokines, including transforming growth factor beta and interleukin 1 alpha.

Indexed as

PhagocytosisAnimalsCollagenConnective TissueConnective Tissue CellsCysteine EndopeptidasesFibroblastsHumansMetalloendopeptidasesCollagenCysteine EndopeptidasesMetalloendopeptidases

Identifiers

PMID8762055
OpenAlexW2090842150

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.