Evidence map›Paper›PMID 15855654›Full record

ArticleThe American journal of pathology2005

Matrix metalloproteinase-1 associates with intracellular organelles and confers resistance to lamin A/C degradation during apoptosis.

G Astrid Limb, Karl Matter, Gillian Murphy, Alison D Cambrey, Paul N Bishop, Glenn E Morris, Peng T Khaw

Open access · bronzeAbstract read
In one paragraph

Article in The American journal of pathology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
3.0field-weighted citation impact, top 7% 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

54 citing papers in PubMed, 118 citations in OpenAlex.

  1. Trial
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Matrix metalloproteinases in kidney homeostasis and diseases: an update.American journal of physiology. Renal physiology · 2024
    Review
  11. The effect of cellular nuclear function alteration on the pathogenesis of shoulder adhesive capsulitis: an immunohistochemical study on lamin A/C expression.Journal of orthopaedics and traumatology : official journal of the Italian Society of Orthopaedics and Traumatology · 2024
    Article
  12. Article
  13. Review
  14. Article
  15. Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu.International journal of molecular sciences · 2022
    Review
  16. Article
  17. Frontiers in neuroscience · 2022
    Review
  18. Article
  19. Review
  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

7 authors at 5 institutions in 3 countries.

G Astrid LimbDepartment of Pathology, Institute of Ophthalmology, University College London and Moorfields Eye Hospital, 11 Bath St., London EC1V 9EL. g.limb@ucl.ac.uk
Karl Matter
Gillian Murphy
Alison D Cambrey
Paul N Bishop
Glenn E Morris
Peng T Khaw
Moorfields Eye Hospital NHS Foundation Trust · GBInstitute for Medical Research · MYUniversity College London · GBUniversity of Manchester · GBWrexham University · GB

Funding

Wellcome Trust
6 · The paper itself

Abstract

Since the first description of matrix metalloproteinase (MMP)-1 as an interstitial collagenase, great importance has been ascribed to this enzyme in extracellular matrix remodeling during tumoral, inflammatory, and angiogenic processes. As more evidence for the role of MMPs in targeting nonmatrix substrates emerges, casual observations that intracellular MMP-1 is found in vitro and in vivo prompt investigation of the role that MMP-1 may play on basic cell functions such as cell division and apoptosis. Here we show for the first time that MMP-1 not only has extracellular functions but that it is strongly associated with mitochondria and nuclei and accumulates within the cells during the mitotic phase of the cell cycle. On induction of apoptosis, MMP-1 co-localized with aggregated mitochondria and accumulated around fragmented nuclei. Inhibition of this enzyme by RNA interference or treatment with a broad MMP inhibitor caused faster degradation of lamin A, activation of caspases, and fragmentation of DNA when compared with untreated cells. These observations strongly suggest that intracellular association of MMP-1 to mitochondria and nuclei confers resistance to apoptosis and may explain the well-known association of this enzyme with tumor cell survival and spreading.

Indexed as

ApoptosisCaspasesCell CycleCell NucleusCells, CulturedDNA FragmentationEnzyme ActivationFibroblastsGene SilencingHumansLamin Type AMatrix Metalloproteinase 1Matrix Metalloproteinase InhibitorsMitochondriaMitosisOrganellesCaspaseslamin CLamin Type AMatrix Metalloproteinase 1Matrix Metalloproteinase InhibitorsStaurosporine

Identifiers

PMID15855654
PMCPMC1606407
OpenAlexW2164122188

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.