Evidence map›Paper›PMID 17254565›Full record

ArticleExperimental cell research2007

Activated protein C promotes breast cancer cell migration through interactions with EPCR and PAR-1.

Lea M Beaulieu, Frank C Church

Abstract read
In one paragraph

Article in Experimental cell research, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed, 1 pooled it
1.9field-weighted citation impact, top 14% 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

36 citing papers in PubMed, 1 synthesis or guideline pooled it, 66 citations in OpenAlex.

  1. Pooled it
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  19. AMPK Activators as a Drug for Diabetes, Cancer and Cardiovascular Disease.Pharmaceutical regulatory affairs : open access · 2014
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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

2 authors at 1 institution in 1 country.

Lea M BeaulieuDepartment of Pathology and Laboratory Medicine, University of North Carolina, School of Medicine, Chapel Hill, NC 27599, USA.
Frank C Church
University of North Carolina at Chapel Hill · US

Funding

Pre-doctoral Training Program in Integrative Vascular BiologyT32HL069768 · NHLBI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Christopher P. Mack · 2002 to 2026
$9.7M
INHIBITION OF FACTOR X ACTIVATION BY HEPARIN-ATR01HL032656 · NHLBI · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI CHURCH, FRANK C · 1985 to 2004
$1.0M
Role of the Protein C System in Blood Vessel RepairF31NS054590 · NINDS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BEAULIEU, LEA M · 2006 to 2006
$26k
NHLBI NIH HHS HL-32656NHLBI NIH HHS R01 HL032656NHLBI NIH HHS T32 HL069768NHLBI NIH HHS T32 HL69768NINDS NIH HHS F31 NS054590NINDS NIH HHS F31 NS054590-01A1
6 · The paper itself

Abstract

Activated protein C (APC) is a serine protease that regulates thrombin (IIa) production through inactivation of blood coagulation factors Va and VIIIa. APC also has non-hemostatic functions related to inflammation, proliferation, and apoptosis through various mechanisms. Using two breast cancer cell lines, MDA-MB-231 and MDA-MB-435, we investigated the role of APC in cell chemotaxis and invasion. Treatment of cells with increasing APC concentrations (1-50 microg/ml) increased invasion and chemotaxis in a concentration-dependent manner. Only the active form of APC increased invasion and chemotaxis of the MDA-MB-231 cells when compared to 3 inactive APC derivatives. Using a modified "checkerboard" analysis, APC was shown to only affect migration when plated with the cells; therefore, APC is not a chemoattractant. Blocking antibodies to endothelial protein C receptor (EPCR) and protease-activated receptor-1 (PAR-1) attenuated the effects of APC on chemotaxis in the MDA-MB-231 cells. Finally, treatment of the MDA-MB-231 cells with the proliferation inhibitor, Na butyrate, showed that APC did not increase migration by increasing cell number. Therefore, APC increases invasion and chemotaxis of cells by binding to the cell surface and activating specific signaling pathways through EPCR and PAR-1.

Indexed as

Cell MovementAntigens, CDBreast NeoplasmsCell Line, TumorCell ProliferationChemotaxisEndothelial Protein C ReceptorEnzyme ActivationHumansNeoplasm InvasivenessProtein BindingProtein CReceptor, PAR-1Receptors, Cell SurfaceAntigens, CDEndothelial Protein C ReceptorPROCR protein, humanProtein CReceptor, PAR-1Receptors, Cell Surface

Identifiers

PMID17254565
PMCPMC4055951
OpenAlexW2063754581

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.