Evidence map›Paper›PMID 21626280›Full record

ArticleAngiogenesis2011

TM4SF1: a tetraspanin-like protein necessary for nanopodia formation and endothelial cell migration.

Andrew Zukauskas, Anne Merley, Dan Li, Lay-Hong Ang, Tracey E Sciuto, Samantha Salman, Ann M Dvorak, Harold F Dvorak, Shou-Ching Shih Jaminet

Abstract read
In one paragraph

Article in Angiogenesis, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
1.9field-weighted citation impact, top 17% 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

34 citing papers in PubMed, 62 citations in OpenAlex.

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  14. Active perception during angiogenesis: filopodia speed up Notch selection of tip cellsPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2021
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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

9 authors at 3 institutions in 1 country.

Andrew ZukauskasCenter for Vascular Biology Research, Department of Pathology, Beth Israel Deaconess Medical Center, Boston, MA 02215, USA.
Anne Merley
Dan Li
Lay-Hong Ang
Tracey E Sciuto
Samantha Salman
Ann M Dvorak
Harold F Dvorak
Shou-Ching Shih Jaminet
Beth Israel Deaconess Medical Center · USHarvard University · USCenter for Vascular Biology Research · US

Funding

The Role of PlGF in Normal and Neoplastic AngiogenesisP01CA092644 · NCI · BETH ISRAEL DEACONESS MEDICAL CENTER · PI DVORAK, HAROLD FISHER · 2002 to 2013
$17.2M
NCI NIH HHS P01 CA092644NCI NIH HHS P01 CA92644
6 · The paper itself

Abstract

Transmembrane-4-L-six-family-1 (TM4SF1) is a tetraspanin-like membrane protein that is highly and selectively expressed by cultured endothelial cells (EC) and, in vivo, by EC lining angiogenic tumor blood vessels. TM4SF1 is necessary for the formation of unusually long (up to a 50 μm), thin (~100-300 nm wide), F-actin-poor EC cell projections that we term 'nanopodia'. Immunostaining of nanopodia at both the light and electron microsopic levels localized TM4SF1 in a regularly spaced, banded pattern, forming TM4FS1-enriched domains. Live cell imaging of GFP-transduced HUVEC demonstrated that EC project nanopodia as they migrate and interact with neighboring cells. When TM4SF1 mRNA levels in EC were increased from the normal ~90 mRNA copies/cell to ~400 copies/cell through adenoviral transduction, EC projected more and longer nanopodia from the entire cell circumference but were unable to polarize or migrate effectively. When fibroblasts, which normally express TM4SF1 at ~5 copies/cell, were transduced to express TM4SF1 at EC-like levels, they formed typical TM4SF1-banded nanopodia, and broadened, EC-like lamellipodia. Mass-spectrometry demonstrated that TM4SF1 interacted with myosin-10 and β-actin, proteins involved in filopodia formation and cell migration. In summary, TM4SF1, like genuine tetraspanins, serves as a molecular organizer that interacts with membrane and cytoskeleton-associated proteins and uniquely initiates the formation of nanopodia and facilitates cell polarization and migration.

Indexed as

Antigens, SurfaceCell Membrane StructuresCell MovementCell PolarityCells, CulturedCytoskeletonEndothelial CellsFibroblastsHumansNeoplasm ProteinsPseudopodiaAntigens, SurfaceNeoplasm ProteinsTM4SF1 protein, human

Identifiers

PMID21626280
PMCPMC3298766
OpenAlexW1966766084

What OpenQuestion holds

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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.