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Aquaporin-3 is involved in NLRP3-inflammasome activation contributing to the setting of inflammatory response

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Abstract

Inflammasomes are large immune multiprotein complexes that tightly regulate the production of the pro-inflammatory cytokines, being dependent on cell regulatory volume mechanisms. Aquaporins (AQPs) are protein channels that facilitate the transport of water and glycerol (aquaglyceroporins) through membranes, essential for cell volume regulation. Although these membrane proteins are highly expressed in monocytes and macrophages, their role in the inflammatory process is still unclear. Here, we investigated the role of aquaglyceroporin AQP3 in NLRP3-inflammasome activation by complementary approaches based either on shRNA silencing or on AQP3 selective inhibition. The latter has been achieved using a reported potent gold-based inhibitor, Auphen. AQP3 inhibition or silencing partially blocked LPS-priming and decreased production of IL-6, proIL-1β, and TNF-α, suggesting the possible involvement of AQP3 in macrophage priming by Toll-like receptor 4 engagement. Moreover, AQP3-dependent cell reswelling increased IL-1β release through caspase-1 activation. NLRP3-inflammasome activation induced by reswelling, nigericin, and ATP was also blocked when AQP3 was inhibited or silenced. Altogether, these data point towards AQPs as potential players in the setting of the inflammatory response.

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Abbreviations

AQP:

Aquaporin

ATP:

Adenosine triphosphate

Casp-1:

Caspase-1

GSDMD:

Gasdermin D

IL:

Interleukin

NF-κB:

Nuclear factor-κB

NLRP3:

Nucleotide-binding oligomerization domain-like receptors family pyrin domain containing 3

Pf :

Osmotic water permeability

Pgly :

Glycerol permeability

TNF-α:

Tumor necrosis factor alpha

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Acknowledgements

This research was funded by Fundação para a Ciência e Tecnologia (FCT), Portugal, through individual fellowship to IV da Silva (PD/BD/113634/2015), grant PTDC/BTM-SAL/28977/2017, and strategic projects UID/DTP/04138/2019, and by Ministerio de Economía, Industria y Competitividad, Spain (grant SAF2017‐88276‐R to P.P.), Fundación Séneca (grant 20859/PI/18 to P.P.), and the European Research Council (ERC‐2013‐CoG grant 614578 to P.P.). We appreciate Veit Hournung (Ludwig Maximilians Universitat Munchen, Germany) for THP-1 Casp-1 KO cells. We thank María Carmen Baños and Ana I. Gómez-Sánchez (IMIB-Arrixaca, Murcia, Spain) for technical assistance, and EU COST Action BM1406 for fruitful discussions and short-term scientific mission for I.V.S..

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  1. Pablo Pelegrín and Graça Soveral joint senior authors.

Authors and Affiliations

  1. Research Institute for Medicines (iMed.ULisboa), Faculty of Pharmacy, Universidade de Lisboa, Av. Prof. Gama Pinto, 1649-003, Lisboa, Portugal

    Inês Vieira da Silva & Graça Soveral

  2. Department of Biochemistry and Human Biology, Faculty of Pharmacy, Universidade de Lisboa, 1649-003, Lisboa, Portugal

    Inês Vieira da Silva, Carlos Cardoso & Graça Soveral

  3. Clinical Chemistry Laboratory, Dr. Joaquim Chaves, 1495-148, Algés, Portugal

    Carlos Cardoso

  4. Molecular Inflammation Group, Biomedical Research Institute of Murcia (IMIB-Arrixaca), Hospital Clínico Universitario Virgen de La Arrixaca, Carretera Buenavista, 30120, Murcia, Spain

    Helios Martínez-Banaclocha & Pablo Pelegrín

  5. Department of Chemistry, Technical University of Munich, Lichtenbergstr. 4, 85748, Garching b. München, Germany

    Angela Casini

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Contributions

IVS, PP, and GS contributed for the experimental planning; IVS, CC, and HM-B. performed the experiments; IVS analyzed the data; GS, PP, and AC contributed to reagents/materials/analysis tools; IVS wrote the main manuscript; PP and GS contributed to the intellectual input and scientific discussion, and edited the main manuscript; and, all authors read and approved the final manuscript.

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Correspondence to Pablo Pelegrín or Graça Soveral.

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da Silva, I.V., Cardoso, C., Martínez-Banaclocha, H. et al. Aquaporin-3 is involved in NLRP3-inflammasome activation contributing to the setting of inflammatory response. Cell. Mol. Life Sci. 78, 3073–3085 (2021). https://doi.org/10.1007/s00018-020-03708-3

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