Evidence map›Paper›PMID 20018883›Full record

ArticleThe Journal of biological chemistry2010

Processing of the matricellular protein hevin in mouse brain is dependent on ADAMTS4.

Matt S Weaver, Gail Workman, Marina Cardo-Vila, Wadih Arap, Renata Pasqualini, E Helene Sage

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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Article
  3. Alpha-neurexins in health and disease.Frontiers in molecular neuroscience · 2025
    Review
  4. GEARBOCS: An Adeno Associated Virus Tool forbioRxiv : the preprint server for biology · 2024
    Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. SPARCL1 Promotes Excitatory But Not Inhibitory Synapse Formation and Function Independent of Neurexins and Neuroligins.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2020
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Diverse biological functions of the SPARC family of proteins.The international journal of biochemistry & cell biology · 2012
    Review
  19. Article
  20. Article
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 2 institutions in 1 country.

Matt S WeaverHope Heart Program, Benaroya Research Institute at Virginia Mason, Seattle, Washington 98101-2795, USA.
Gail Workman
Marina Cardo-Vila
Wadih Arap
Renata Pasqualini
E Helene Sage
Benaroya Research InstituteThe University of Texas MD Anderson Cancer Center · US

Funding

EXTRACELLULAR PROTEINS AS SIGNALS IN ENDOTHELIAL GROWTHR01GM040711 · NIGMS · UNIVERSITY OF WASHINGTON · PI SAGE, EMILY HELENE · 1988 to 2009
$2.7M
Regulation of Cell Function by Matricellular HevinR01CA109559 · NCI · BENAROYA RESEARCH INST AT VIRGINIA MASON · PI WIGHT, THOMAS N · 2004 to 2008
$1.8M
NCI NIH HHS CA109559NCI NIH HHS R01 CA109559NIGMS NIH HHS GM40711NIGMS NIH HHS R01 GM040711
6 · The paper itself

Abstract

The matricellular SPARC family member hevin (SPARC-like 1/SPARCL-1/SC1/Mast9) contributes to neural development and alters tumor progression in a range of mammalian models. The distribution of hevin in mouse tissues was reexamined with a novel monoclonal antibody that discriminates between hevin and its ortholog SPARC. We now report proteolysis of hevin in many tissues, with the most extensive processing in the brain. We demonstrate a cleavage site within the hevin sequence for the neural tissue proteinase ADAMTS4. Digestion of hevin by ADAMTS4 in vitro produced fragments similar to those present in brain lysates. Monoclonal antibodies revealed a SPARC-like fragment generated from hevin that was co-localized with ADAMTS4 in vivo. We show that proteolysis of hevin by ADAMTS4 in the mouse cerebellum is important for the normal development of this tissue. In conclusion, we have identified the fragmentation of hevin by ADAMTS4 in the mouse brain and propose that this specific proteolysis is integral to cell morphology and extracellular matrix deposition in the developing brain.

Indexed as

ADAM ProteinsADAMTS4 ProteinAnimalsBrain ChemistryCalcium-Binding ProteinsCerebellumExtracellular Matrix ProteinsHumansMiceMice, Mutant StrainsNerve Tissue ProteinsProcollagen N-EndopeptidaseADAM ProteinsADAMTS4 ProteinADAMTS4 protein, humanAdamts4 protein, mouseCalcium-Binding ProteinsExtracellular Matrix ProteinsNerve Tissue ProteinsProcollagen N-EndopeptidaseSPARCL1 protein, humanSparcl1 protein, mouse

Identifiers

PMID20018883
PMCPMC2820812
OpenAlexW1997956950

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.