ArticlePulmonary circulation
Group V phospholipase A(2) increases pulmonary endothelial permeability through direct hydrolysis of the cell membrane.
Article in Pulmonary circulation. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Alveolar macrophage-derived gVPLA2 promotes ventilator-induced lung injury via the cPLA2/PGE2 pathway.BMC pulmonary medicine · 2023Article
- Suilyin Disrupts the Blood-Brain Barrier by Activating Group III Secretory Phospholipase A2.Life (Basel, Switzerland) · 2022Article
- Secretory Phospholipase ACell biochemistry and biophysics · 2021Review
- Group V Phospholipase ACells · 2021Article
- Degradation of group V secretory phospholipase AMicrovascular research · 2020Article
- Elevated truncated oxidized phospholipids as a factor exacerbating ALI in the aging lungs.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2019Article
- Prostaglandin E receptor-4 receptor mediates endothelial barrier-enhancing and anti-inflammatory effects of oxidized phospholipids.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Epigenetic control of group V phospholipase A2 expression in human malignant cells.Tumour biology : the journal of the International Society for Oncodevelopmental Biology and Medicine · 2016Article
- Mechanical induction of group V phospholipase A(2) causes lung inflammation and acute lung injury.American journal of physiology. Lung cellular and molecular physiology · 2013Article
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Authors and funding
7 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Acute lung injury (ALI) is characterized by inflammatory disruption of the alveolar-vascular barrier, resulting in severe respiratory compromise. Inhibition of the intercellular messenger protein, Group V phospholipase A(2) (gVPLA(2)), blocks vascular permeability caused by LPS both in vivo and in vitro. In this investigation we studied the mechanism by which recombinant gVPLA(2) increases permeability of cultured human pulmonary endothelial cells (EC). Exogenous gVPLA(2) (500 nM), a highly hydrolytic enzyme, caused a significant increase in EC permeability that began within minutes and persisted for >10 hours. However, the major hydrolysis products of gVPLA(2) (Lyso-PC, Lyso-PG, LPA, arachidonic acid) did not cause EC structural rearrangement or loss of barrier function at concentrations <10 μM. Higher concentrations (≥ 30 μM) of these membrane hydrolysis products caused some increased permeability but were associated with EC toxicity (measured by propidium iodide incorporation) that did not occur with barrier disruption by gVPLA(2) (500 nM). Pharmacologic inhibition of multiple intracellular signaling pathways induced by gVPLA(2) activity (ERK, p38, PI3K, cytosolic gIVPLA(2)) also did not prevent EC barrier disruption by gVPLA(2). Finally, pretreatment with heparinase to prevent internalization of gVPLA(2) did not inhibit EC barrier disruption by gVPLA(2). Our data thus indicate that gVPLA(2) increases pulmonary EC permeability directly through action as a membrane hydrolytic agent. Disruption of EC barrier function does not depend upon membrane hydrolysis products, gVPLA(2) internalization, or upregulation of downstream intracellular signaling.
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Registered trials
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