Evidence map›Paper›PMID 21688302›Full record

ArticleJournal of cellular biochemistry2011

Proteolysis of the matricellular protein hevin by matrix metalloproteinase-3 produces a SPARC-like fragment (SLF) associated with neovasculature in a murine glioma model.

Matt Weaver, Gail Workman, Chad R Schultz, Nancy Lemke, Sandra A Rempel, E Helene Sage

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.1field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 24 citations in OpenAlex.

  1. Article
  2. Article
  3. Alpha-neurexins in health and disease.Frontiers in molecular neuroscience · 2025
    Review
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Revisiting the matricellular concept.Matrix biology : journal of the International Society for Matrix Biology · 2014
    Review
  13. Review
  14. Diverse biological functions of the SPARC family of proteins.The international journal of biochemistry & cell biology · 2012
    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

6 authors at 2 institutions in 1 country.

Matt WeaverBenaroya Research Institute, 1201 Ninth Avenue, Seattle, Washington 98101, USA.
Gail Workman
Chad R Schultz
Nancy Lemke
Sandra A Rempel
E Helene Sage
Henry Ford Hospital · USBenaroya Research Institute

Funding

EXTRACELLULAR PROTEINS AS SIGNALS IN ENDOTHELIAL GROWTHR01GM040711 · NIGMS · UNIVERSITY OF WASHINGTON · PI SAGE, EMILY HELENE · 1988 to 2009
$2.7M
THE ROLE OF SPARC IN GLIOMA INVASIONR01CA086997 · NCI · HENRY FORD HEALTH SYSTEM · PI REMPEL, SANDRA ANN · 2001 to 2007
$1.8M
NCI NIH HHS CA86997NCI NIH HHS R01 CA086997NIGMS 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. Based on sequence similarity, we hypothesized that proteolytic digestion of hevin would result in SPARC-like fragments (SLF) that affect the activity and/or location of these proteins. Incubation of hevin with matrix metalloproteinase-3 (MMP-3), a protease known to cleave SPARC, produced a limited number of peptides. Sequencing revealed the major proteolytic products to be SPARC-like in primary structure. In gliomas implanted into murine brain, a SLF was associated with SPARC in the neovasculature but not with hevin, the latter prominent in the astrocytes encompassed by infiltrating tumor. In this model of invasive glioma that involves MMP-3 activity, host-derived SLF was not observed in the extracellular matrix adjacent to tumor cells. In contrast, it occurred with its homolog SPARC in the angiogenic response to the tumor. We conclude that MMP-3-derived SLF is a marker of neovessels in glioma, where it could influence the activity of SPARC.

Indexed as

Neovascularization, PathologicAmino Acid SequenceAnimalsBrain NeoplasmsCalcium-Binding ProteinsCell Line, TumorCHO CellsCricetinaeCricetulusDisease Models, AnimalExtracellular Matrix ProteinsGliomaHumansImmunohistochemistryMatrix Metalloproteinase 3MiceCalcium-Binding ProteinsExtracellular Matrix ProteinsMatrix Metalloproteinase 3OsteonectinSparcl1 protein, mouse

Identifiers

PMID21688302
PMCPMC3188378
OpenAlexW1992675622

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.