Evidence map›Paper›PMID 14524536›Full record

ArticleClinical & experimental metastasis2003

Seprase, a membrane-bound protease, alleviates the serum growth requirement of human breast cancer cells.

Johnna D Goodman, Tricia L Rozypal, Thomas Kelly

Abstract read
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In one paragraph

Article in Clinical & experimental metastasis, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
1.0field-weighted citation impact, top 27% 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

17 citing papers in PubMed, 51 citations in OpenAlex.

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  6. Targeting of activated fibroblasts for imaging and therapy.EJNMMI radiopharmacy and chemistry · 2019
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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 2 institutions in 1 country.

Johnna D GoodmanDepartment of Pathology, Arkansas Cancer Research Center, University of Arkansas for Medical Sciences, Little Rock, Arkansas 72205-7199, USA.
Tricia L Rozypal
Thomas Kelly
Cancer Research Center · USUniversity of Arkansas for Medical Sciences · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Seprase is a cell surface serine protease that is expressed to high levels by infiltrating ductal carcinomas of the breast but its function in malignancy is unknown. MDA-MB-435 (WT435) and MDA-MB-436 (WT436) human breast cancer cells express high levels of seprase as do the carcinoma cells in tumors of human breast cancer patients. To investigate its role in the pathobiology of breast cancer, seprase was specifically reduced in WT436 and WT435 cells by expression of antisense seprase cDNA. Decreased expression of seprase was confirmed in the antisense transfectants by zymography, immunoblotting, and fluorescence-activated cell sorting of cells labeled with antibody to seprase. Control-transfectants continued to express high levels of seprase. Seprase-deficient cells growing on type I collagen gels reveal a markedly different morphology than the parental or control-transfected cells that express high levels of seprase. The seprase-deficient cells grow in islands and aggregates of tightly attached cells while cells with high seprase expression grow as groups of separate individual cells. Interestingly, the aggregated growth of the seprase-deficient cells was not correlated with increased expression of E-cadherin. Seprase-deficient breast cancer cells also exhibit altered growth properties. Seprase-deficient cells and those with high seprase levels proliferate in serum-containing media. However, in serum-free medium seprase-deficient cells proliferate much more slowly than their seprase-expressing counterparts. These findings indicate that seprase promotes the aberrant growth of breast cancer cells by reducing their dependence on exogenous growth factors. Seprase may contribute to the pathogenesis of breast cancer by promoting growth of the primary tumor and by facilitating the growth of breast cancer cells in metastases at other sites of the body.

Indexed as

Membrane ProteinsSerine EndopeptidasesBlotting, NorthernBreast NeoplasmsCadherinsCarcinomaCell DivisionCell MembraneCell SeparationCloning, MolecularCollagen Type IDNA, ComplementaryEndopeptidasesFibroblast Activation Protein AlphaFlow CytometryGelatinasesCadherinsCollagen Type IDNA, ComplementaryEndopeptidasesFibroblast Activation Protein AlphaGelatinasesGrowth SubstancesMembrane ProteinsOligonucleotides, AntisenseSerine Endopeptidases

Identifiers

PMID14524536
OpenAlexW1491102423

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.