Evidence map›Paper›PMID 19679556›Full record

ArticleCancer research2009

Osteoclast-derived matrix metalloproteinase-7, but not matrix metalloproteinase-9, contributes to tumor-induced osteolysis.

Sophie Thiolloy, Jennifer Halpern, Ginger E Holt, Herbert S Schwartz, Gregory R Mundy, Lynn M Matrisian, Conor C Lynch

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 10% 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

34 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
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  14. Regulation of Bone Metabolism.Reports of biochemistry & molecular biology · 2017
    Article
  15. Article
  16. Article
  17. Liensinine and Nuciferine, Bioactive Components ofEvidence-based complementary and alternative medicine : eCAM · 2017
    Article
  18. Article
  19. Article
  20. Matrix metalloproteinases and genetic mouse models in cancer research: a mini-review.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2015
    Review
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 1 institution in 1 country.

Sophie ThiolloyDepartment of Cancer Biology, Vanderbilt University, Nashville, Tennessee, USA.
Jennifer Halpern
Ginger E Holt
Herbert S Schwartz
Gregory R Mundy
Lynn M Matrisian
Conor C Lynch
Vanderbilt University · US

Funding

Tumor and Stromal Metalloproteinases in Breast CancerR01CA084360 · NCI · VANDERBILT UNIVERSITY · PI FINGLETON, BARBARA · 2000 to 2014
$5.7M
NCI NIH HHS 1 R01 CA84360NCI NIH HHS R01 CA084360
6 · The paper itself

Abstract

The matrix metalloproteinases MMP-2, MMP-3, MMP-7, MMP-9, and MMP-13 are highly expressed in the tumor-bone microenvironment, and, of these, MMP-7 and MMP-9 were found to be localized to bone-resorbing osteoclasts in human breast-to-bone metastases. In a bid to define the roles of host-derived MMP-7 and MMP-9 in the tumor-bone microenvironment, the tibias of MMP-7 and MMP-9 null mice were injected with osteolytic luciferase-tagged mammary tumor cell lines. Our data show that osteoclast-derived MMP-7 significantly contributes to tumor growth and tumor-induced osteolysis whereas osteoclast-derived MMP-9 had no effect on these processes. MMP-7 is capable of processing a number of nonmatrix molecules to soluble active forms that have profound effects on cell-cell communication, such as RANKL, a crucial mediator of osteoclast precursor recruitment and maturation. Therefore, the ability of osteoclast-derived MMP-7 to promote RANKL solubilization in the tumor-bone microenvironment was explored. Results revealed that levels of soluble RANKL were significantly lower in the MMP-7 null mice compared with wild-type (WT) controls. In keeping with this observation, MMP-7 null mice had significantly fewer osteoclast numbers at the tumor-bone interface compared with the WT controls. In summary, we propose that the solubilization of RANKL by MMP-7 is a potential mechanism through which MMP-7 mediates mammary tumor-induced osteolysis. Our studies indicate that the selective inhibition of MMP-7 in the tumor-bone microenvironment may be of benefit for the treatment of lytic breast-to-bone metastases.

Indexed as

AnimalsBone DensityBone NeoplasmsBreast NeoplasmsCell ProliferationCells, CulturedFemaleHumansMatrix Metalloproteinase 7Matrix Metalloproteinase 9MiceMice, KnockoutOsteoclastsOsteolysisRANK LigandTumor BurdenMatrix Metalloproteinase 7Matrix Metalloproteinase 9RANK Ligand

Identifiers

PMID19679556
PMCPMC2745595
OpenAlexW2041252138

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.