Evidence map›Paper›PMID 27798230›Full record

ArticleMolecular biology of the cell2016

The role of HYAL2 in LSS-induced glycocalyx impairment and the PKA-mediated decrease in eNOS-Ser-633 phosphorylation and nitric oxide production.

Xiangquan Kong, Liang Chen, Peng Ye, Zhimei Wang, Junjie Zhang, Fei Ye, Shaoliang Chen

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

21 citing papers in PubMed, 32 citations in OpenAlex.

  1. Article
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  5. Mechanisms of triple-negative breast cancer extravasation: Impact of the physical environment and endothelial glycocalyx.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2024
    Review
  6. Review
  7. Review
  8. Vascular mechanotransduction.Physiological reviews · 2023
    Review
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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

7 authors at 2 institutions in 1 country.

Xiangquan KongDepartment of Cardiology, Nanjing First Hospital, Nanjing Medical University, Nanjing 210001, China.
Liang ChenDepartment of Cardiology, Nanjing First Hospital, Nanjing Medical University, Nanjing 210001, China.
Peng YeDepartment of Cardiology, Nanjing First Hospital, Nanjing Medical University, Nanjing 210001, China.
Zhimei WangDepartment of Cardiology, Nanjing First Hospital, Nanjing Medical University, Nanjing 210001, China.
Junjie ZhangDepartment of Cardiology, Nanjing First Hospital, Nanjing Medical University, Nanjing 210001, China.
Fei YeDepartment of Cardiology, Nanjing First Hospital, Nanjing Medical University, Nanjing 210001, China.
Shaoliang ChenDepartment of Cardiology, Nanjing First Hospital, Nanjing Medical University, Nanjing 210001, China; chmengx@126.com.
Nanjing Medical University · CNWannan Medical College · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Hyaluronan (HA) in the endothelial glycocalyx serves as a mechanotransducer for high-shear-stress-stimulated endothelial nitric oxide synthase (eNOS) phosphorylation and nitric oxide (NO) production. Low shear stress (LSS) has been shown to contribute to endothelial inflammation and atherosclerosis by impairing the barrier and mechanotransduction properties of the glycocalyx. Here we focus on the possible role of hyaluronidase 2 (HYAL2) in LSS-induced glycocalyx impairment and the resulting alterations in eNOS phosphorylation and NO production in human umbilical vein endothelial cells (HUVECs). We show that LSS strongly activates HYAL2 to degrade HA in the glycocalyx. The dephosphorylation of eNOS-Ser-633 under LSS was triggered after HA degradation by hyaluronidase and prevented by repairing the glycocalyx with high-molecular weight hyaluronan. Knocking down HYAL2 in HUVECs protected against HA degradation in the glycocalyx by inhibiting the expression and activity of HYAL2 and further blocked the dephosphorylation of eNOS-Ser-633 and the decrease in NO production in response to LSS. The LSS-induced dephosphorylation of PKA was completely abrogated in HYAL2 siRNA-transfected HUVECs. The LSS-induced dephosphorylation of eNOS-Ser-633 was also reversed by the PKA activator 8-Br-cAMP. We thus suggest that LSS inhibits eNOS-Ser-633 phosphorylation and, at least partially, NO production by activating HYAL2 to degrade HA in the glycocalyx.

Indexed as

Cell Adhesion MoleculesCells, CulturedCyclic AMP-Dependent Protein KinasesEndothelium, VascularGlycocalyxGPI-Linked ProteinsHumansHuman Umbilical Vein Endothelial CellsHyaluronoglucosaminidaseMechanotransduction, CellularNitric OxideNitric Oxide Synthase Type IIIPhosphorylationShear StrengthSignal TransductionStress, MechanicalCell Adhesion MoleculesCyclic AMP-Dependent Protein KinasesGPI-Linked ProteinsHyal2 protein, humanHyaluronoglucosaminidaseNitric OxideNitric Oxide Synthase Type IIINOS3 protein, human

Identifiers

PMID27798230
PMCPMC5156538
OpenAlexW2541964038

What OpenQuestion holds

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LicenceCC BY-NC-SA
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Registered trials

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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.