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Lysosomal destabilization activates the NLRP3 inflammasome in human umbilical vein endothelial cells (HUVECs).

Abstract：

:Inflammation is a crucial component in the pathogenesis of many vascular diseases, such as atherosclerosis and diabetes. Inflammasomes are intracellular signalling complexes whose activation promotes inflammation. Nucleotide-binding domain and Leucine-rich repeat Receptor containing a Pyrin domain 3 (NLRP3) is a pattern recognition receptor (PRR) forming the best-known inflammasome. Disturbances in NLRP3 have been associated with multiple diseases. The purpose of this study was to explore the lysosomal destabilization-related NLRP3 inflammasome signaling pathway in human endothelial cells. In order to prime and activate NLRP3, human umbilical vein cells (HUVECs) were exposed to TNF-α and the lysosomal destructive agent Leusine-Leusine-O-Methylesther (Leu-Leu-OMe), respectively. A caspase-1 inhibitor was used to block caspase-1's enzymatic function and an interleukin 1 receptor antagonist (IL-1RA) to prevent any possible secondary effects of IL-1β. Leu-Leu-OMe increased the expression of NLRP3, IL-1β, and IL-18 in HUVECs. Exposure to Leu-Leu-OMe significantly promoted the production of IL-6 and IL-8 in primed HUVECs; this effect was prevented by the pre-treatment of cells with an IL-1RA. Our results suggest that lysosomal destabilization activates the NLRP3 inflammasome pathway that promotes the production of IL-6 and IL-8 in an autocrine manner in HUVEC cells.

journal_name

J Cell Commun Signal

journal_title

Journal of cell communication and signaling

authors

Kinnunen K,Piippo N,Loukovaara S,Hytti M,Kaarniranta K,Kauppinen A

doi

10.1007/s12079-017-0396-4

subject

Has Abstract

pub_date

2017-09-01 00:00:00

pages

275-279

issue

3

eissn

1873-9601

issn

1873-961X

pii

10.1007/s12079-017-0396-4

journal_volume

11

pub_type

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