Evidence map›Paper›PMID 22403397›Full record

ArticleThe Journal of biological chemistry2012

NEU1 and NEU3 sialidase activity expressed in human lung microvascular endothelia: NEU1 restrains endothelial cell migration, whereas NEU3 does not.

Alan S Cross, Sang Won Hyun, Alba Miranda-Ribera, Chiguang Feng, Anguo Liu, Chinh Nguyen, Lei Zhang, Irina G Luzina, Sergei P Atamas, William S Twaddell and 7 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.6field-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

35 citing papers in PubMed, 61 citations in OpenAlex.

  1. Article
  2. Review
  3. iScience · 2024
    Article
  4. Review
  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Review
  11. The extracellular sialidase NEU3 primes neutrophils.Journal of leukocyte biology · 2022
    Article
  12. Article
  13. Article
  14. Review
  15. Review
  16. Article
  17. Article
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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

17 authors at 1 institution in 1 country.

Alan S CrossCenter for Vaccine Development, University of Maryland, School of Medicine, Baltimore, Maryland 21201, USA.
Sang Won Hyun
Alba Miranda-Ribera
Chiguang Feng
Anguo Liu
Chinh Nguyen
Lei Zhang
Irina G Luzina
Sergei P Atamas
William S Twaddell
Wei Guang
Erik P Lillehoj
Adam C Puché
Wei Huang
Lai-Xi Wang
Antonino Passaniti
Simeon E Goldblum
University of Maryland, Baltimore · US

Funding

Thrombospondin-1 Opens Endothelial Paracellular Pathway via EGFR/ErbB2 ActivationR01HL084223 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI GOLDBLUM, SIMEON EMANUEL · 2007 to 2011
$1.9M
Role of Sialidase in Pulmonary Host Defenses and Acute Lung InjuryR01HL086933 · NHLBI · UNIVERSITY OF MARYLAND BALTIMORE · PI CROSS, ALAN S. · 2007 to 2010
$1.8M
NEU1 Sialidase Disrupts CD31-Driven Angiogenesis in Human Lung EndotheliaI01BX002352 · VA · BALTIMORE VA MEDICAL CENTER · PI GOLDBLUM, SIMEON EMANUEL · 2015 to 2018
–
BLRD VA I01 BX002352NHLBI NIH HHS HL084223NHLBI NIH HHS HL086933NHLBI NIH HHS R01 HL084223NHLBI NIH HHS R01 HL086933
6 · The paper itself

Abstract

The microvascular endothelial surface expresses multiple molecules whose sialylation state regulates multiple aspects of endothelial function. To better regulate these sialoproteins, we asked whether endothelial cells (ECs) might express one or more catalytically active sialidases. Human lung microvascular EC lysates contained heat-labile sialidase activity for a fluorogenic substrate, 2'-(4-methylumbelliferyl)-α-D-N-acetylneuraminic acid (4-MU-NANA), that was dose-dependently inhibited by the competitive sialidase inhibitor, 2,3-dehydro-2-deoxy-N-acetylneuraminic acid but not its negative control. The EC lysates also contained sialidase activity for a ganglioside mixture. Using real time RT-PCR to detect mRNAs for the four known mammalian sialidases, NEU1, -2, -3, and -4, NEU1 mRNA was expressed at levels 2700-fold higher that those found for NEU2, -3, or -4. Western analyses indicated NEU1 and -3 protein expression. Using confocal microscopy and flow cytometry, NEU1 was immunolocalized to both the plasma membrane and the perinuclear region. NEU3 was detected both in the cytosol and nucleus. Prior siRNA-mediated knockdown of NEU1 and NEU3 each decreased EC sialidase activity for 4-MU-NANA by >65 and >17%, respectively, and for the ganglioside mixture by 0 and 40%, respectively. NEU1 overexpression in ECs reduced their migration into a wound by >40%, whereas NEU3 overexpression did not. Immunohistochemical studies of normal human tissues immunolocalized NEU1 and NEU3 proteins to both pulmonary and extrapulmonary vascular endothelia. These combined data indicate that human lung microvascular ECs as well as other endothelia express catalytically active NEU1 and NEU3. NEU1 restrains EC migration, whereas NEU3 does not.

Indexed as

Cell MovementAortaCarotid ArteriesCell LineCell MembraneCell NucleusCerebral ArteriesCytosolEndothelial CellsFlow CytometryGene Expression Regulation, EnzymologicHumansHymecromoneImmunoblottingKidneyLung2'-(4-methylumbelliferyl)-alpha-D-N-acetylneuraminic acid2-deoxy-2,3-dehydro-N-acetylneuraminic acidHymecromoneN-Acetylneuraminic AcidNEU1 protein, humanNEU2 protein, humanNeu3 protein, humanNEU4 protein, humanNeuraminidase

Identifiers

PMID22403397
PMCPMC3346112
OpenAlexW2079273426

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.