Evidence map›Paper›PMID 25205731›Full record

ArticleBiological chemistry2014

Membrane-type I matrix metalloproteinase-dependent ectodomain shedding of mucin16/ CA-125 on ovarian cancer cells modulates adhesion and invasion of peritoneal mesothelium.

Lana Bruney, Kaitlynn C Conley, Natalie M Moss, Yueying Liu, M Sharon Stack

Open access · greenAbstract read
In one paragraph

Article in Biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
37citing papers in PubMed, 1 pooled it
1.5field-weighted citation impact, top 19% 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

37 citing papers in PubMed, 1 synthesis or guideline pooled it, 50 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Excess shed mesothelin disrupts pancreatic cancer cell clustering to impair peritoneal colonization.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Review
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  16. Review
  17. Metalloproteinases in Ovarian Cancer.International journal of molecular sciences · 2021
    Review
  18. Review
  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

5 authors at 2 institutions in 1 country.

Lana Bruney
Kaitlynn C Conley
Natalie M Moss
Yueying Liu
M Sharon Stack
University of Notre Dame · USUnited States Patent and Trademark Office · US

Funding

Receptor Cross-Talk in Early Metastatic DisseminationR01CA109545 · NCI · UNIVERSITY OF NOTRE DAME · PI STACK, MARY SHARON · 2006 to 2022
$4.3M
REGULATION OF OVARIAN CARCINOMA PROTEINASESR01CA086984 · NCI · UNIVERSITY OF NOTRE DAME · PI STACK, MARY SHARON · 2000 to 2014
$3.8M
Integrin Linked Kinase and Ovarian Cancer MetastasisF31CA159804 · NCI · UNIVERSITY OF MISSOURI-COLUMBIA · PI BRUNEY, LANA Y · 2011 to 2013
$86k
NCI NIH HHS F31 CA159804NCI NIH HHS R01 CA086984NCI NIH HHS R01 CA109545
6 · The paper itself

Abstract

Mucin16 [MUC16/cancer antigen 125 (CA-125)], a high-molecular-weight glycoprotein expressed on the ovarian tumor cell surface, potentiates metastasis via selective binding to mesothelin on peritoneal mesothelial cells. Shed MUC16/CA-125 is detectable in sera from ovarian cancer patients. We investigated the potential role of membrane type 1 matrix metalloproteinase (MT1-MMP, MMP-14), a transmembrane collagenase highly expressed in ovarian cancer cells, in MUC16/CA-125 ectodomain shedding. An inverse correlation between MT1-MMP and MUC16 immunoreactivity was observed in human ovarian tumors and cells. Further, when MUC16-expressing OVCA433 cells were engineered to overexpress MT1-MMP, surface expression of MUC16/CA-125 was lost, whereas cells expressing the inactive E240A mutant retained surface MUC16/CA-125. As a functional consequence, decreased adhesion of cells expressing catalytically active MT1-MMP to three-dimensional meso-mimetic cultures and intact ex vivo peritoneal tissue explants was observed. Nevertheless, meso-mimetic invasion is enhanced in MT1-MMP-expressing cells. Together, these data support a model wherein acquisition of catalytically active MT1-MMP expression in ovarian cancer cells induces MUC16/CA-125 ectodomain shedding, reducing adhesion to meso-mimetic cultures and to intact peritoneal explants. However, proteolytic clearing of MUC16/CA-125, catalyzed by MT1-MMP, may then expose integrins for high-affinity cell binding to peritoneal tissues, thereby anchoring metastatic lesions for subsequent proliferation within the collagen-rich sub-mesothelial matrix.

Indexed as

AnimalsCA-125 AntigenCell AdhesionCell Line, TumorFemaleHumansMatrix Metalloproteinase 14Membrane ProteinsMesothelinMiceMice, Inbred C57BLNeoplasm InvasivenessNeoplasm MetastasisNeoplasms, MesothelialNeoplasm TransplantationOvarian NeoplasmsCA-125 AntigenMatrix Metalloproteinase 14Membrane ProteinsMesothelinMMP14 protein, humanMsln protein, mouseMUC16 protein, human

Identifiers

PMID25205731
PMCPMC5568695
OpenAlexW1966870353

What OpenQuestion holds

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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.