Evidence map›Paper›PMID 20937842›Full record

ArticleThe Journal of biological chemistry2010

Matriptase-2- and proprotein convertase-cleaved forms of hemojuvelin have different roles in the down-regulation of hepcidin expression.

Julia E Maxson, Juxing Chen, Caroline A Enns, An-Sheng Zhang

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

32 citing papers in PubMed, 60 citations in OpenAlex.

  1. Article
  2. Novel compound heterozygous mutations in theWorld journal of clinical cases · 2024
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  4. Review
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  12. Article
  13. Article
  14. Article
  15. Article
  16. Identification of TMPRSS6 cleavage sites of hemojuvelin.Journal of cellular and molecular medicine · 2015
    Article
  17. Review
  18. Low intracellular iron increases the stability of matriptase-2.The Journal of biological chemistry · 2015
    Article
  19. Article
  20. Review
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

4 authors at 1 institution in 1 country.

Julia E MaxsonDepartment of Cell and Developmental Biology, Oregon Health and Science University, Portland, Oregon 97239, USA.
Juxing Chen
Caroline A Enns
An-Sheng Zhang
Oregon Health & Science University · US

Funding

Regulation and function of transferrin receptor 2R01DK072166 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI ENNS, CAROLINE · 2005 to 2017
$3.7M
Basic research training in embryonic developmentT32HD049309 · NICHD · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARR-GILLESPIE, PETER GORDON · 2006 to 2010
$1.8M
Functional investigation of hemojuvelin in regulation of hepcidin expressionR01DK080765 · NIDDK · OREGON HEALTH & SCIENCE UNIVERSITY · PI ZHANG, AN-SHENG · 2008 to 2011
$913k
NICHD NIH HHS T32 HD049309NIDDK NIH HHS DK080765NIDDK NIH HHS DK72166NIDDK NIH HHS R01 DK072166NIDDK NIH HHS R01 DK080765
6 · The paper itself

Abstract

Hemojuvelin (HJV) is an important regulator of iron metabolism. Membrane-anchored HJV up-regulates expression of the iron regulatory hormone, hepcidin, through the bone morphogenic protein (BMP) signaling pathway by acting as a BMP co-receptor. HJV can be cleaved by the furin family of proprotein convertases, which releases a soluble form of HJV that suppresses BMP signaling and hepcidin expression by acting as a decoy that competes with membrane HJV for BMP ligands. Recent studies indicate that matriptase-2 binds and degrades HJV, leading to a decrease in cell surface HJV. In the present work, we show that matriptase-2 cleaves HJV at Arg(288), which produces one major soluble form of HJV. This shed form of HJV has decreased ability to bind BMP6 and does not suppress BMP6-induced hepcidin expression. These results suggest that the matriptase-2 and proprotein convertase-cleavage products have different roles in the regulation of hepcidin expression.

Indexed as

Gene Expression Regulation, EnzymologicAnimalsAntimicrobial Cationic PeptidesArginineGPI-Linked ProteinsHemochromatosisHemochromatosis ProteinHepcidinsHumansIronMembrane ProteinsMutationProprotein ConvertasesProtein BindingRatsRNA, Small InterferingAntimicrobial Cationic PeptidesArginineGPI-Linked ProteinsHAMP protein, humanHamp protein, ratHemochromatosis ProteinHepcidinsHJV protein, humanIronmatriptase 2Membrane ProteinsProprotein ConvertasesRNA, Small InterferingSerine Endopeptidases

Identifiers

PMID20937842
PMCPMC2998150
OpenAlexW2027924212

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.