Evidence map›Paper›PMID 18286233›Full record

ReviewCancer metastasis reviews2008

MT4-(MMP17) and MT6-MMP (MMP25), A unique set of membrane-anchored matrix metalloproteinases: properties and expression in cancer.

Anjum Sohail, Qing Sun, Huiren Zhao, M Margarida Bernardo, Jin-Ah Cho, Rafael Fridman

Abstract readReview
In one paragraph

Review in Cancer metastasis reviews, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
–field-weighted citation impact
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

74 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Matrix metalloproteinases in kidney homeostasis and diseases: an update.American journal of physiology. Renal physiology · 2024
    Review
  8. Review
  9. Article
  10. Article
  11. Molecular Mechanisms Driven by MT4-MMP in Cancer Progression.International journal of molecular sciences · 2023
    Review
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

14 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

6 authors.

Anjum SohailDepartment of Pathology, School of Medicine, and Proteases and Cancer Program, Barbara Ann Karmanos Cancer Institute, Wayne State University, Detroit, MI 48201, USA.
Qing Sun
Huiren Zhao
M Margarida Bernardo
Jin-Ah Cho
Rafael Fridman

Funding

REGULATION OF MATRIX METALLOPROTEINASE ACTIVATIONR01CA061986 · NCI · WAYNE STATE UNIVERSITY · PI FRIDMAN, RAFAEL A. · 1995 to 2015
$3.9M
NCI NIH HHS CA 61986NCI NIH HHS R01 CA061986
6 · The paper itself

Abstract

The process of cancer progression involves the action of multiple proteolytic systems, among which the family of matrix metalloproteinases (MMPs) play a pivotal role. The MMPs evolved to accomplish their proteolytic tasks in multiple cellular and tissue microenvironments including lipid rafts by incorporation and deletions of specific structural domains. The membrane type-MMPs (MT-MMPs) incorporated membrane anchoring domains that display these proteases at the cell surface, and thus they are optimal pericellular proteolytic machines. Two members of the MT-MMP subfamily, MMP-17 (MT4-MMP) and MMP-25 (MT6-MMP), are anchored to the plasma membrane via a glycosyl-phosphatidyl inositol (GPI) anchor, which confers these enzymes a unique set of regulatory and functional mechanisms that separates them from the rest of the MMP family. Discovered almost a decade ago, the body of work on GPI-MT-MMPs today is still surprisingly limited when compared to other MT-MMPs. However, new evidence shows that the GPI-MT-MMPs are highly expressed in human cancer, where they are associated with progression. Accumulating biochemical and functional evidence also highlights their distinct properties. In this review, we summarize the structural, biochemical, and biological properties of GPI-MT-MMPs and present an overview of their expression and role in cancer. We further discuss the potential implications of GPI-anchoring for enzyme function. Finally, we comment on the new scientific challenges that lie ahead to better understand the function and role in cancer of these intriguing but yet unique MMPs.

Indexed as

AnimalsCell MembraneGPI-Linked ProteinsHumansMatrix Metalloproteinase 17Matrix Metalloproteinases, Membrane-AssociatedNeoplasmsGPI-Linked ProteinsMatrix Metalloproteinase 17matrix metalloproteinase 25Matrix Metalloproteinases, Membrane-Associated

Identifiers

PMID18286233
PMCPMC3903121

What OpenQuestion holds

Textmetadata
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Registered trials

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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.