Evidence map›Paper›PMID 11389678›Full record

ArticleThe Biochemical journal2001

Characterization of matrix metalloproteinase-26, a novel metalloproteinase widely expressed in cancer cells of epithelial origin.

G N Marchenko, B I Ratnikov, D V Rozanov, A Godzik, E I Deryugina, A Y Strongin

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
6.1field-weighted citation impact, top 3% 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

43 citing papers in PubMed, 130 citations in OpenAlex.

  1. Review
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  9. Review
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  12. MMP26: A potential biomarker for prostate cancer.Journal of Huazhong University of Science and Technology. Medical sciences = Hua zhong ke ji da xue xue bao. Yi xue Ying De wen ban = Huazhong keji daxue xuebao. Yixue Yingdewen ban · 2017
    Article
  13. Biochemical and Biological Attributes of Matrix Metalloproteinases.Progress in molecular biology and translational science · 2017
    Review
  14. Article
  15. Article
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  17. Matrilysin-2 expression in colorectal cancer is associated with overall survival of patients.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2014
    Article
  18. Review
  19. Article
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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 at 1 institution in 1 country.

G N MarchenkoThe Burnham Institute, 10901 North Torrey Pines Road, La Jolla, CA 92037, USA.
B I Ratnikov
D V Rozanov
A Godzik
E I Deryugina
A Y Strongin
Sanford Burnham Prebys Medical Discovery Institute · US

Funding

METALLOPROTEINASES IN TUMOR NEOVASCULARIZATIONR01CA083017 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 1999 to 2014
$3.8M
MT1-MMP pericellular proteolysis in malignancyR01CA077470 · NCI · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI STRONGIN, ALEX Y · 1999 to 2009
$3.1M
NCI NIH HHS CA77470NCI NIH HHS CA83017
6 · The paper itself

Abstract

Identification of expanding roles for matrix metalloproteinases (MMPs) in complex regulatory processes of tissue remodelling has stimulated the search for genes encoding proteinases with unique functions, regulation and expression patterns. By using a novel cloning strategy, we identified three previously unknown human MMPs, i.e. MMP-21, MMP-26 and MMP-28, in comprehensive gene libraries. The present study is focused on the gene and the protein of a novel MMP, MMP-26. Our findings show that MMP-26 is specifically expressed in cancer cells of epithelial origin, including carcinomas of lung, prostate and breast. Several unique structural and regulatory features, including an unusual 'cysteine-switch' motif, discriminate broad-spectrum MMP-26 from most other MMPs. MMP-26 efficiently cleaves fibrinogen and extracellular matrix proteins, including fibronectin, vitronectin and denatured collagen. Protein sequence, minimal modular domain structure, exon-intron mapping and computer modelling demonstrate similarity between MMP-26 and MMP-7 (matrilysin). However, substrate specificity and transcriptional regulation, as well as the functional role of MMP-26 and MMP-7 in cancer, are likely to be distinct. Despite these differences, matrilysin-2 may be a suitable trivial name for MMP-26. Our observations suggest an important specific function for MMP-26 in tumour progression and angiogenesis, and confirm and extend the recent findings of other authors [Park, Ni, Gerkema, Liu, Belozerov and Sang (2000) J. Biol. Chem. 275, 20540--20544; Uría and López-Otín (2000) Cancer Res. 60, 4745--4751; de Coignac, Elson, Delneste, Magistrelli, Jeannin, Aubry, Berthier, Schmitt, Bonnefoy and Gauchat (2000) Eur. J. Biochem. 267, 3323--3329].

Indexed as

Amino Acid SequenceBase SequenceCatalytic DomainCloning, MolecularDNA PrimersEpithelial CellsHumansMatrix MetalloproteinasesMatrix Metalloproteinases, SecretedModels, MolecularMolecular Sequence DataNeoplasmsPromoter Regions, GeneticProtein ConformationRecombinant ProteinsSequence Homology, Amino AcidDNA PrimersMatrix MetalloproteinasesMatrix Metalloproteinases, SecretedMMP26 protein, humanRecombinant ProteinsTranscription Factors

Identifiers

PMID11389678
PMCPMC1221897
OpenAlexW2117821061

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.