Evidence map›Paper›PMID 18783725›Full record

ReviewMolecular aspects of medicine2008

Meprins, membrane-bound and secreted astacin metalloproteinases.

Erwin E Sterchi, Walter Stöcker, Judith S Bond

Open access · greenAbstract readReview
In one paragraph

Review in Molecular aspects of medicine, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 101 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
101citing papers in PubMed, 2 pooled it
3.0field-weighted citation impact, top 8% 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

101 citing papers in PubMed, 2 syntheses or guidelines pooled it, 199 citations in OpenAlex.

  1. Pooled it
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  12. ThePolymers · 2024
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41 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

3 authors at 3 institutions in 3 countries.

Erwin E SterchiInstitute of Biochemistry and Molecular Biology, University of Berne, Buehlstrasse 28, CH-3012 Berne, Switzerland. erwin.sterchi@mci.unibe.ch
Walter Stöcker
Judith S Bond
Johannes Gutenberg University Mainz · DEPennsylvania State University · USUniversity of Bern · CH

Funding

MEPRINS-METALLOPROTEINSASES OF THE KIDNEY AND INTESTINER01DK019691 · NIDDK · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI BOND, JUDITH S · 1986 to 2010
$3.1M
MEPRINS - METALLOPROTEINASES OF THE KIDNEY AND INTESTINER56DK019691 · NIDDK · PENNSYLVANIA STATE UNIV HERSHEY MED CTR · PI BOND, JUDITH S · 2005 to 2005
$73k
INTRACELLULAR PROTEIN CATABOLISM IN DIABETES MELLITUSR37DK019691 · NIDDK · VIRGINIA POLYTECHNIC INST AND ST UNIV · PI BOND, JUDITH S · 1989 to 1996
–
NIDDK NIH HHS DK 19691NIDDK NIH HHS R01 DK019691NIDDK NIH HHS R56 DK019691
6 · The paper itself

Abstract

The astacins are a subfamily of the metzincin superfamily of metalloproteinases. The first to be characterized was the crayfish enzyme astacin. To date more than 200 members of this family have been identified in species ranging from bacteria to humans. Astacins are involved in developmental morphogenesis, matrix assembly, tissue differentiation and digestion. Family members include the procollagen C-proteinase (BMP1, bone morphogenetic protein 1), tolloid and mammalian tolloid-like, HMP (Hydra vulgaris metalloproteinase), sea urchin BP10 (blastula protein) and SPAN (Strongylocentrotus purpuratus astacin), the 'hatching' subfamily comprising alveolin, ovastacin, LCE, HCE ('low' and 'high' choriolytic enzymes), nephrosin (from carp head kidney), UVS.2 from frog, and the meprins. In the human and mouse genomes, there are six astacin family genes (two meprins, three BMP1/tolloid-like, one ovastacin), but in Caenorhabditis elegans there are 40. Meprins are the only astacin proteinases that function on the membrane and extracellularly by virtue of the fact that they can be membrane-bound or secreted. They are unique in their domain structure and covalent subunit dimerization, oligomerization propensities, and expression patterns. They are normally highly regulated at the transcriptional and post-translational levels, localize to specific membranes or extracellular spaces, and can hydrolyse biologically active peptides, cytokines, extracellular matrix (ECM) proteins and cell-surface proteins. The in vivo substrates of meprins are unknown, but the abundant expression of these proteinases in the epithelial cells of the intestine, kidney and skin provide clues to their functions.

Indexed as

Amino Acid SequenceAnimalsHumansIntestinal MucosaMetalloendopeptidasesModels, MolecularMolecular Sequence DataPhylogenyProtein ConformationProtein SubunitsSubstrate SpecificityTissue Distributionastacinmeprin AMetalloendopeptidasesProtein Subunits

Identifiers

PMID18783725
PMCPMC2650038
OpenAlexW1995518402

What OpenQuestion holds

Textmetadata
LicenceTDM
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.