Evidence map›Paper›PMID 26604323›Full record

ReviewBioscience reports2015

How, with whom and when: an overview of CD147-mediated regulatory networks influencing matrix metalloproteinase activity.

G Daniel Grass, Bryan P Toole

Open access · goldAbstract readReview
In one paragraph

Review in Bioscience reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers, 3 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
104citing papers in PubMed, 3 pooled it
4.5field-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

104 citing papers in PubMed, 3 syntheses or guidelines pooled it, 157 citations in OpenAlex.

  1. Pooled it
  2. Pooled it
  3. Pooled it
  4. Review
  5. A Novel CD147-Targeting Nanobody for Immuno-PET Imaging of Liver Cancer.Journal of nuclear medicine : official publication, Society of Nuclear Medicine · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Modulation of Redox Metabolism, CD147, and CD47 Expression with the Maturation of Hematopoietic Stem Cells in Bone Marrow.Indian journal of hematology & blood transfusion : an official journal of Indian Society of Hematology and Blood Transfusion · 2025
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Article
  20. Review

44 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

2 authors at 2 institutions in 1 country.

G Daniel GrassDepartment of Radiation Oncology, H. Lee Moffitt Cancer Center and Research Institute, Tampa, FL 33612, U.S.A. Daniel.Grass@moffitt.org toolebp@musc.edu.
Bryan P TooleDepartment of Regenerative Medicine & Cell Biology, Medical University of South Carolina, Charleston, SC 29425, U.S.A. Hollings Cancer Center, Medical University of South Carolina, Charleston, SC 29425, U.S.A. Daniel.Grass@moffitt.org toolebp@musc.edu.
Medical University of South Carolina · USMoffitt Cancer Center · US

Funding

PERTURBATION OF HYALURONAN FUNCTION IN CANCERR01CA082867 · NCI · TUFTS UNIVERSITY BOSTON · PI TOOLE, BRYAN P · 1999 to 2010
$2.1M
Inhibition of Tumor Progression by Hyaluronan OligomersR01CA073839 · NCI · TUFTS UNIVERSITY BOSTON · PI TOOLE, BRYAN P · 1997 to 2008
$1.8M
NCI NIH HHS R01 CA073839NCI NIH HHS R01 CA082867
6 · The paper itself

Abstract

Matrix metalloproteinases (MMPs) comprise a family of 23 zinc-dependent enzymes involved in various pathologic and physiologic processes. In cancer, MMPs contribute to processes from tumour initiation to establishment of distant metastases. Complex signalling and protein transport networks regulate MMP synthesis, cell surface presentation and release. Earlier attempts to disrupt MMP activity in patients have proven to be intolerable and with underwhelming clinical efficacy; thus targeting ancillary proteins that regulate MMP activity may be a useful therapeutic approach. Extracellular matrix metalloproteinase inducer (EMMPRIN) was originally characterized as a factor present on lung cancer cells, which stimulated collagenase (MMP-1) production in fibroblasts. Subsequent studies demonstrated that EMMPRIN was identical with several other protein factors, including basigin (Bsg), all of which are now commonly termed CD147. CD147 modulates the synthesis and activity of soluble and membrane-bound [membrane-type MMPs (MT-MMPs)] in various contexts via homophilic/heterophilic cell interactions, vesicular shedding or cell-autonomous processes. CD147 also participates in inflammation, nutrient and drug transporter activity, microbial pathology and developmental processes. Despite the hundreds of manuscripts demonstrating CD147-mediated MMP regulation, the molecular underpinnings governing this process have not been fully elucidated. The present review summarizes our present knowledge of the complex regulatory systems influencing CD147 biology and provides a framework to understand how CD147 may influence MMP activity.

Indexed as

AnimalsBasiginCell CommunicationCollagenasesHumansBasiginBSG protein, humanCollagenasesbasigincancerCD147EMMPRINmatrix metalloproteinaseprotein oligomerization

Identifiers

PMID26604323
PMCPMC4718507
OpenAlexW2280193287

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.