Evidence map›Paper›PMID 23737137›Full record

ArticleMolecular and cellular biochemistry2013

Matrix metalloproteinase-2 (MMP-2) generates soluble HLA-G1 by cell surface proteolytic shedding.

Roberta Rizzo, Alessandro Trentini, Daria Bortolotti, Maria C Manfrinato, Antonella Rotola, Massimiliano Castellazzi, Loredana Melchiorri, Dario Di Luca, Franco Dallocchio, Enrico Fainardi and 1 more

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In one paragraph

Article in Molecular and cellular biochemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 41 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed, 1 pooled it
4.0field-weighted citation impact, top 6% 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

41 citing papers in PubMed, 1 synthesis or guideline pooled it, 76 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Article
  6. Review
  7. Article
  8. Induction of pulmonary HLA-G expression by SARS-CoV-2 infection.Cellular and molecular life sciences : CMLS · 2022
    Article
  9. ADAM17 cleaves the insulin receptor ectodomain on endothelial cells and causes vascular insulin resistance.American journal of physiology. Heart and circulatory physiology · 2022
    Article
  10. Review
  11. Article
  12. Downregulated cytotoxic CD8Cellular & molecular immunology · 2022
    Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Review
  18. Article
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4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

11 authors at 2 institutions in 1 country.

Roberta RizzoSection of Microbiology and Medical Genetics, Department of Medical Sciences, University of Ferrara, Ferrara, Italy. rbr@unife.it
Alessandro Trentini
Daria Bortolotti
Maria C Manfrinato
Antonella Rotola
Massimiliano Castellazzi
Loredana Melchiorri
Dario Di Luca
Franco Dallocchio
Enrico Fainardi
Tiziana Bellini
University of Ferrara · ITArcispedale Sant'Anna · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Human leukocyte antigen-G (HLA-G) molecules are non-classical HLA class I antigens with an important role in pregnancy immune regulation and inflammation control. Soluble HLA-G proteins can be generated through two mechanisms: alternative splicing and proteolytic release, which is known to be metalloprotease mediated. Among this class of enzymes, matrix metalloproteinases (MMPs) might be involved in the HLA-G1 membrane cleavage. Of particular interest are MMP-2 and MMP-9, which regulate the inflammatory process by cytokine and chemokine modulation. We evaluated the effect of MMP-9 and MMP-2 on HLA-G1 membrane shedding. In particular, we analyzed the in vitro effect of these two gelatinases on the secretion of HLA-G1 via proteolytic cleavage in 221-G1-transfected cell line, in JEG3 cell line, and in peripheral blood mononuclear cells. The results obtained by both cell lines showed the role of MMP-2 in HLA-G1 shedding. On the contrary, MMP-9 was not involved in this process. In addition, we identified three possible highly specific cleavage sites for MMP-2, whereas none were detected for MMP-9. This study suggests an effective link between MMP-2 and HLA-G1 shedding, increasing our knowledge on the regulatory machinery beyond HLA-G regulation in physiological and pathological conditions.

Indexed as

ProteolysisAmino Acid SequenceAntibodies, BlockingCell Line, TumorCell MembraneCycloheximideEdetic AcidHLA-G AntigensHumansLeukocytes, MononuclearMatrix Metalloproteinase 2Matrix Metalloproteinase 9Molecular Sequence DataAntibodies, BlockingCycloheximideEdetic AcidHLA-G AntigensMatrix Metalloproteinase 2Matrix Metalloproteinase 9MMP2 protein, humanMMP9 protein, human

Identifiers

PMID23737137
OpenAlexW1981158549

What OpenQuestion holds

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Read underepoch 390

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.