Evidence map›Paper›PMID 38762714›Full record

ArticleCell biochemistry and biophysics2024

Pseudomonas aeruginosa N-3-Oxododecanoyl Homoserine Lactone Disrupts Endothelial Integrity by Activating the Angiopoietin-Tie System.

Jungho Shin, Sun Hee Ahn, Dong-Jin Oh

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Article in Cell biochemistry and biophysics, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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1 · What the graph read from it

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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

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3 · Its place in the literature

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0 citing papers in PubMed.

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4 · The record

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5 · Who and what money

Authors and funding

3 authors.

Jungho ShinDepartment of Internal Medicine, Chung-Ang University College of Medicine, Seoul, South Korea.
Sun Hee AhnDepartment of Internal Medicine, Chung-Ang University College of Medicine, Seoul, South Korea.
Dong-Jin OhDepartment of Internal Medicine, Myongji Hospital, Hanyang University College of Medicine, Goyang, South Korea. intmdoh@hanmail.net.

Funding

National Research Foundation of Korea 2020R1F1A1072498
6 · The paper itself

Abstract

The activation of the angiopoietin (Angpt)-Tie system is linked to endothelial dysfunction during sepsis. Bacterial quorum-sensing molecules function as pathogen-associated molecular patterns. However, their impact on the endothelium and the Angpt-Tie system remains unclear. Therefore, this study investigated whether treatment with N-3-oxododecanoyl homoserine lactone (3OC12-HSL), a quorum-sensing molecule derived from Pseudomonas aeruginosa, impaired endothelial function in human umbilical vein endothelial cells. 3OC12-HSL treatment impaired tube formation even at sublethal concentrations, and immunocytochemistry analysis revealed that it seemed to reduce vascular endothelial-cadherin expression at the cell-cell interface. Upon assessing the mRNA expression patterns of genes associated with the Angpt-Tie axis, the expressions of Angpt2, Forkhead box protein O1, Tie1, and vascular endothelial growth factor 2 were found to be upregulated in the 3OC12-HSL-treated cells. Moreover, western blot analysis revealed that 3OC12-HSL treatment increased Angpt2 expression. A co-immunoprecipitation assay was conducted to assess the effect of 3OC12-HSL on the IQ motif containing GTPase activating protein 1 (IQGAP1) and Rac1 complex and the interaction between these proteins was consistently maintained regardless of 3OC12-HSL treatment. Next, recombinant human (rh)-Angpt1 was added to assess whether it modulated the effects of 3OC12-HSL treatment. rh-Angpt1 addition increased cellular viability, improved endothelial function, and reversed the overall patterns of mRNA and protein expression in endothelial cells treated with 3OC12-HSL. Additionally, it was related to the increased expression of phospho-Akt and the IQGAP1 and Rac1 complex. Collectively, our findings indicated that 3OC12-HSL from Pseudomonas aeruginosa can impair endothelial integrity via the activation of the Angpt-Tie axis, which appeared to be reversed by rh-Angpt1 treatment.

Indexed as

4-ButyrolactoneAngiopoietin-2HomoserineHuman Umbilical Vein Endothelial CellsPseudomonas aeruginosaAngiopoietin-1Antigens, CDCadherin 5CadherinsForkhead Box Protein O1Humansrac1 GTP-Binding Proteinras GTPase-Activating ProteinsSignal Transduction4-ButyrolactoneAngiopoietin-1Angiopoietin-2ANGPT2 protein, humanAntigens, CDCadherin 5CadherinsForkhead Box Protein O1FOXO1 protein, humanHomoserineIQ motif containing GTPase activating protein 1N-(3-oxododecanoyl)homoserine lactonerac1 GTP-Binding Proteinras GTPase-Activating ProteinsAngiopoietinEndothelial cellN-3-oxododecanoyl homoserine lactoneQuorum-sensing moleculeSepsis

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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.