An immune-adrenergic pathway induces lethal levels of platelet-activating factor in mice.


Journal

Communications biology
ISSN: 2399-3642
Titre abrégé: Commun Biol
Pays: England
ID NLM: 101719179

Informations de publication

Date de publication:
29 Jun 2024
Historique:
received: 12 08 2023
accepted: 24 06 2024
medline: 2 7 2024
pubmed: 2 7 2024
entrez: 1 7 2024
Statut: epublish

Résumé

Acute immune responses with excess production of cytokines, lipid/chemical mediators, or coagulation factors, often result in lethal damage. In addition, the innate immune system utilizes multiple types of receptors that recognize neurotransmitters as well as pathogen-associated molecular patterns, making immune responses complex and clinically unpredictable. We here report an innate immune and adrenergic link inducing lethal levels of platelet-activating factor. Injecting mice with toll-like receptor (TLR) 4 ligand lipopolysaccharide (LPS), cell wall N-glycans of Candida albicans, and the α

Identifiants

pubmed: 38951147
doi: 10.1038/s42003-024-06498-7
pii: 10.1038/s42003-024-06498-7
doi:

Substances chimiques

Platelet Activating Factor 0
Lipopolysaccharides 0
1-Acylglycerophosphocholine O-Acyltransferase EC 2.3.1.23
Toll-Like Receptor 4 0
Adrenergic alpha-2 Receptor Agonists 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

782

Informations de copyright

© 2024. The Author(s).

Références

Shaker, M. S. et al. Anaphylaxis-a 2020 practice parameter update, systematic review, and Grading of Recommendations, Assessment, Development and Evaluation (GRADE) analysis. J. Allergy Clin. Immunol. 145, 1082–1123 (2020).
pubmed: 32001253 doi: 10.1016/j.jaci.2020.01.017
Stone, K. D., Prussin, C. & Metcalfe, D. D. IgE, mast cells, basophils, and eosinophils. J. Allergy Clin. Immunol. 125, S73–S80 (2010).
pubmed: 20176269 pmcid: 2847274 doi: 10.1016/j.jaci.2009.11.017
Cianferoni, A. Non-IgE-mediated anaphylaxis. J. Allergy Clin. Immunol. 147, 1123–1131 (2021).
pubmed: 33832694 doi: 10.1016/j.jaci.2021.02.012
Finkelman, F. D., Khodoun, M. V. & Strait, R. Human IgE-independent systemic anaphylaxis. J. Allergy Clin. Immunol. 137, 1674–1680 (2016).
pubmed: 27130857 pmcid: 7607869 doi: 10.1016/j.jaci.2016.02.015
Schiller, M., Ben-Shaanan, T. L. & Rolls, A. Neuronal regulation of immunity: why, how and where? Nat. Rev. Immunol. 21, 20–36 (2021).
pubmed: 32811994 doi: 10.1038/s41577-020-0387-1
Hodo, T. W., de Aquino, M. T. P., Shimamoto, A. & Shanker, A. Critical neurotransmitters in the neuroimmune network. Front Immunol. 11, 1869 (2020).
pubmed: 32973771 pmcid: 7472989 doi: 10.3389/fimmu.2020.01869
Li, D. & Wu, M. Pattern recognition receptors in health and diseases. Signal Transduct. Target Ther. 6, 291 (2021).
pubmed: 34344870 pmcid: 8333067 doi: 10.1038/s41392-021-00687-0
Tan, P. H., Ji, J., Yeh, C. C. & Ji, R. R. Interferons in pain and infections: emerging roles in neuro-immune and neuro-glial interactions. Front Immunol. 12, 783725 (2021).
pubmed: 34804074 pmcid: 8602180 doi: 10.3389/fimmu.2021.783725
Donnelly, C. R., Chen, O. & Ji, R. R. How do sensory neurons sense danger signals? Trends Neurosci. 43, 822–838 (2020).
pubmed: 32839001 pmcid: 7530006 doi: 10.1016/j.tins.2020.07.008
Iqbal, F. et al. Anesthetics: from modes of action to unconsciousness and neurotoxicity. J. Neurophysiol. 122, 760–787 (2019).
pubmed: 31242059 doi: 10.1152/jn.00210.2019
Jafarzadeh, A., Hadavi, M., Hassanshahi, G., Rezaeian, M. & Vazirinejad, R. General anesthetics on immune system cytokines: a narrative review article. Anesth. Pain. Med. 10, e103033 (2020).
pubmed: 33134146 pmcid: 7539048 doi: 10.5812/aapm.103033
Weiser, T. G. et al. An estimation of the global volume of surgery: a modelling strategy based on available data. Lancet 372, 139–144 (2008).
pubmed: 18582931 doi: 10.1016/S0140-6736(08)60878-8
Derrington, M. C. & Smith, G. A review of studies of anaesthetic risk, morbidity and mortality. Br. J. Anaesth. 59, 815–833 (1987).
pubmed: 3304374 doi: 10.1093/bja/59.7.815
Narani, K. K. Deep vein thrombosis and pulmonary embolism - Prevention, management, and anaesthetic considerations. Indian J. Anaesth. 54, 8–17 (2010).
pubmed: 20532065 pmcid: 2876903 doi: 10.4103/0019-5049.60490
Fischer, A., Ballet, J. J. & Griscelli, C. Specific inhibition of in vitro Candida-induced lymphocyte proliferation by polysaccharidic antigens present in the serum of patients with chronic mucocutaneous candidiasis. J. Clin. Invest. 62, 1005–1013 (1978).
pubmed: 361754 pmcid: 371859 doi: 10.1172/JCI109204
Kawakita, M. et al. Cell wall N-glycan of Candida albicans ameliorates early hyper- and late hypo-immunoreactivity in sepsis. Commun. Biol. 4, 342 (2021).
pubmed: 33727664 pmcid: 7966402 doi: 10.1038/s42003-021-01870-3
Gomez-Gaviria, M., Vargas-Macias, A. P., Garcia-Carnero, L. C., Martinez-Duncker, I. & Mora-Montes, H. M. Role of protein glycosylation in interactions of medically relevant fungi with the host. J. Fungi (Basel) 7, 875 (2021).
pubmed: 34682296 doi: 10.3390/jof7100875
Kamibayashi, T. & Maze, M. Clinical uses of α
pubmed: 11046225 doi: 10.1097/00000542-200011000-00030
Brown, G. D. et al. Dectin-1 is a major β-glucan receptor on macrophages. J. Exp. Med. 196, 407–412 (2002).
pubmed: 12163569 pmcid: 2193936 doi: 10.1084/jem.20020470
Shibata, N., Suzuki, A., Kobayashi, H. & Okawa, Y. Chemical structure of the cell-wall mannan of Candida albicans serotype A and its difference in yeast and hyphal forms. Biochem. J. 404, 365–372 (2007).
pubmed: 17331070 pmcid: 1896289 doi: 10.1042/BJ20070081
Shibata, N., Kobayashi, H., Okawa, Y. & Suzuki, S. Existence of novel β-1,2 linkage-containing side chain in the mannan of Candida lusitaniae, antigenically related to Candida albicans serotype A. Eur. J. Biochem. 270, 2565–2575 (2003).
pubmed: 12787022 doi: 10.1046/j.1432-1033.2003.03622.x
Shibata, N. et al. Demonstration of the presence of α-1,6-branched side chains in the mannan of Candida stellatoidea. Eur. J. Biochem. 246, 477–485 (1997).
pubmed: 9208941 doi: 10.1111/j.1432-1033.1997.00477.x
Shibata, N. et al. Existence of branched side chains in the cell wall mannan of pathogenic yeast, Candida albicans. Structure-antigenicity relationship between the cell wall mannans of Candida albicans and Candida parapsilosis. J. Biol. Chem. 270, 1113–1122 (1995).
pubmed: 7836369 doi: 10.1074/jbc.270.3.1113
Raschke, W. C., Kern, K. A., Antalis, C. & Ballou, C. E. Genetic control of yeast mannan structure. Isolation and characterization of mannan mutants. J. Biol. Chem. 248, 4660–4666 (1973).
pubmed: 4578088 doi: 10.1016/S0021-9258(19)43714-9
Graham, L. M. & Brown, G. D. The Dectin-2 family of C-type lectins in immunity and homeostasis. Cytokine 48, 148–155 (2009).
pubmed: 19665392 pmcid: 2756403 doi: 10.1016/j.cyto.2009.07.010
Saijo, S. et al. Dectin-2 recognition of α-mannans and induction of Th17 cell differentiation Is essential for host defense against Candida albicans. Immunity 32, 681–691 (2010).
pubmed: 20493731 doi: 10.1016/j.immuni.2010.05.001
Bi, L. et al. CARD9 mediates dectin-2-induced IκBα kinase ubiquitination leading to activation of NF-κB in response to stimulation by the hyphal form of Candida albicans. J. Biol. Chem. 285, 25969–25977 (2010).
pubmed: 20538615 pmcid: 2923990 doi: 10.1074/jbc.M110.131300
Hara, H. et al. Cell type-specific regulation of ITAM-mediated NF-κB activation by the adaptors, CARMA1 and CARD9. J. Immunol. 181, 918–930 (2008).
pubmed: 18606643 doi: 10.4049/jimmunol.181.2.918
Rodriguez, M. et al. Pharmacological inhibition of eicosanoids and platelet-activating factor signaling impairs zymosan-induced release of IL-23 by dendritic cells. Biochem. Pharmacol. 102, 78–96 (2016).
pubmed: 26673542 doi: 10.1016/j.bcp.2015.12.001
Robinson, M. J. et al. Dectin-2 is a Syk-coupled pattern recognition receptor crucial for Th17 responses to fungal infection. J. Exp. Med. 206, 2037–2051 (2009).
pubmed: 19703985 pmcid: 2737172 doi: 10.1084/jem.20082818
Eason, M. G., Kurose, H., Holt, B. D., Raymond, J. R. & Liggett, S. B. Simultaneous coupling of α
pubmed: 1322406 doi: 10.1016/S0021-9258(19)49605-1
Wu, Y. & Yoder, A. Chemokine coreceptor signaling in HIV-1 infection and pathogenesis. PLoS Pathog. 5, e1000520 (2009).
pubmed: 20041213 pmcid: 2790611 doi: 10.1371/journal.ppat.1000520
Barrett, N. A., Maekawa, A., Rahman, O. M., Austen, K. F. & Kanaoka, Y. Dectin-2 recognition of house dust mite triggers cysteinyl leukotriene generation by dendritic cells. J. Immunol. 182, 1119–1128 (2009).
pubmed: 19124755 doi: 10.4049/jimmunol.182.2.1119
Finkelman, F. D., Rothenberg, M. E., Brandt, E. B., Morris, S. C. & Strait, R. T. Molecular mechanisms of anaphylaxis: lessons from studies with murine models. J. Allergy Clin. Immunol. 115, 449–457 (2005). quiz 458.
pubmed: 15753886 doi: 10.1016/j.jaci.2004.12.1125
Shindou, H. et al. Relief from neuropathic pain by blocking of the platelet-activating factor-pain loop. FASEB J. 31, 2973–2980 (2017).
pubmed: 28341636 pmcid: 5471516 doi: 10.1096/fj.201601183R
Shimizu, T. Lipid mediators in health and disease: enzymes and receptors as therapeutic targets for the regulation of immunity and inflammation. Annu. Rev. Pharmacol. Toxicol. 49, 123–150 (2009).
pubmed: 18834304 doi: 10.1146/annurev.pharmtox.011008.145616
Ishii, S. & Shimizu, T. Platelet-activating factor (PAF) receptor and genetically engineered PAF receptor mutant mice. Prog. Lipid Res. 39, 41–82 (2000).
pubmed: 10729607 doi: 10.1016/S0163-7827(99)00016-8
Kita, Y., Takahashi, T., Uozumi, N. & Shimizu, T. A multiplex quantitation method for eicosanoids and platelet-activating factor using column-switching reversed-phase liquid chromatography-tandem mass spectrometry. Anal. Biochem. 342, 134–143 (2005).
pubmed: 15958190 doi: 10.1016/j.ab.2005.03.048
Yamada, M. et al. A comprehensive quantification method for eicosanoids and related compounds by using liquid chromatography/mass spectrometry with high speed continuous ionization polarity switching. J. Chromatogr. B Anal. Technol. Biomed. Life Sci. 995-996, 74–84 (2015).
doi: 10.1016/j.jchromb.2015.05.015
Honda, Z. et al. Cloning by functional expression of platelet-activating factor receptor from guinea-pig lung. Nature 349, 342–346 (1991).
pubmed: 1846231 doi: 10.1038/349342a0
Lordan, R., Tsoupras, A., Zabetakis, I. & Demopoulos, C. A. Forty years since the structural elucidation of platelet-activating Factor (PAF): historical, current, and future research perspectives. Molecules 24, 4414 (2019).
pubmed: 31816871 pmcid: 6930554 doi: 10.3390/molecules24234414
Abate, W., Alrammah, H., Kiernan, M., Tonks, A. J. & Jackson, S. K. Lysophosphatidylcholine acyltransferase 2 (LPCAT2) co-localises with TLR4 and regulates macrophage inflammatory gene expression in response to LPS. Sci. Rep. 10, 10355 (2020).
pubmed: 32587324 pmcid: 7316826 doi: 10.1038/s41598-020-67000-x
Deng, M. et al. Platelet-activating factor (PAF) mediates NLRP3-NEK7 inflammasome induction independently of PAFR. J. Exp. Med 216, 2838–2853 (2019).
pubmed: 31558613 pmcid: 6888982 doi: 10.1084/jem.20190111
Stack, J. et al. TRAM is required for TLR2 endosomal signaling to type I IFN induction. J. Immunol. 193, 6090–6102 (2014).
pubmed: 25385819 doi: 10.4049/jimmunol.1401605
Barbalat, R., Lau, L., Locksley, R. M. & Barton, G. M. Toll-like receptor 2 on inflammatory monocytes induces type I interferon in response to viral but not bacterial ligands. Nat. Immunol. 10, 1200–1207 (2009).
pubmed: 19801985 pmcid: 2821672 doi: 10.1038/ni.1792
Kawai, T. & Akira, S. Toll-like receptors and their crosstalk with other innate receptors in infection and immunity. Immunity 34, 637–650 (2011).
pubmed: 21616434 doi: 10.1016/j.immuni.2011.05.006
Dewachter, P., Mouton-Faivre, C. & Emala, C. W. Anaphylaxis and anesthesia: controversies and new insights. Anesthesiology 111, 1141–1150 (2009).
pubmed: 19858877 doi: 10.1097/ALN.0b013e3181bbd443
Caballero, M. L., Krantz, M. S., Quirce, S., Phillips, E. J. & Stone, C. A. Jr. Hidden dangers: recognizing excipients as potential causes of drug and vaccine hypersensitivity reactions. J. Allergy Clin. Immunol. Pract. 9, 2968–2982 (2021).
pubmed: 33737254 pmcid: 8355062 doi: 10.1016/j.jaip.2021.03.002
Morimoto, R., Shindou, H., Tarui, M. & Shimizu, T. Rapid production of platelet-activating factor is induced by protein kinase Ca-mediated phosphorylation of lysophosphatidylcholine acyltransferase 2 protein. J. Biol. Chem. 289, 15566–15576 (2014).
pubmed: 24742674 pmcid: 4140912 doi: 10.1074/jbc.M114.558874
Morimoto, R., Shindou, H., Oda, Y. & Shimizu, T. Phosphorylation of lysophosphatidylcholine acyltransferase 2 at Ser34 enhances platelet-activating factor production in endotoxin-stimulated macrophages. J. Biol. Chem. 285, 29857–29862 (2010).
pubmed: 20663880 pmcid: 2943291 doi: 10.1074/jbc.M110.147025
Kawai, T. & Akira, S. TLR signaling. Semin Immunol. 19, 24–32 (2007).
pubmed: 17275323 doi: 10.1016/j.smim.2006.12.004
Fischer, A., Ballet, J. J. & Griscelli, C. Specific inhibition of in vitro candida-induced lymphocyte-proliferation by polysaccharidic antigens present in serum of patients with chronic mucocutaneous candidiasis. J. Clin. Invest. 62, 1005–1013 (1978).
pubmed: 361754 pmcid: 371859 doi: 10.1172/JCI109204
Lands, W. E. Metabolism of glycerolipides; a comparison of lecithin and triglyceride synthesis. J. Biol. Chem. 231, 883–888 (1958).
pubmed: 13539023 doi: 10.1016/S0021-9258(18)70453-5
Kita, Y., Shindou, H. & Shimizu, T. Cytosolic phospholipase A(2) and lysophospholipid acyltransferases. Biochim. Biophys. Acta Mol. Cell Biol. Lipids 1864, 838–845 (2019).
pubmed: 30905348 doi: 10.1016/j.bbalip.2018.08.006
Pfeil, E. M. et al. Heterotrimeric G protein subunit Gαq is a master switch for Gβγ-mediated calcium mobilization by Gi-coupled GPCRs. Mol. Cell 80, 940–954 e946 (2020).
pubmed: 33202251 doi: 10.1016/j.molcel.2020.10.027
Jeong, Y. I. et al. The novel role of platelet-activating factor in protecting mice against lipopolysaccharide-induced endotoxic shock. PLoS One 4, e6503 (2009).
pubmed: 19652714 pmcid: 2714981 doi: 10.1371/journal.pone.0006503
Welch, E. J. et al. Opposing effects of platelet-activating factor and lyso-platelet-activating factor on neutrophil and platelet activation. Mol. Pharmacol. 75, 227–234 (2009).
pubmed: 18931035 doi: 10.1124/mol.108.051003
von Kanel, R., Mills, P. J., Ziegler, M. G. & Dimsdale, J. E. Effect of β
doi: 10.1067/mhj.2002.123146
Sandrini, L., Ieraci, A., Amadio, P., Zara, M. & Barbieri, S. S. Impact of acute and chronic stress on thrombosis in healthy individuals and cardiovascular disease patients. Int. J. Mol. Sci. 21, 7818 (2020).
pubmed: 33105629 pmcid: 7659944 doi: 10.3390/ijms21217818
Hara, H. et al. The adaptor protein CARD9 is essential for the activation of myeloid cells through ITAM-associated and Toll-like receptors. Nat. Immunol. 8, 619–629 (2007).
pubmed: 17486093 doi: 10.1038/ni1466
Kirihara, Y., Takechi, M., Kurosaki, K., Kobayashi, Y. & Kurosawa, T. Anesthetic effects of a mixture of medetomidine, midazolam and butorphanol in two strains of mice. Exp. Anim. 62, 173–180 (2013).
pubmed: 23903051 pmcid: 4160945 doi: 10.1538/expanim.62.173

Auteurs

Shuto Tanaka (S)

Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.

Masataka Kawakita (M)

Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.

Hikaru Yasui (H)

Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.

Koichi Sudo (K)

Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.

Fumie Itoh (F)

Division of Infection and Host Defense, Tohoku Medical and Pharmaceutical University, Sendai, Japan.

Masato Sasaki (M)

Division of Infection and Host Defense, Tohoku Medical and Pharmaceutical University, Sendai, Japan.

Nobuyuki Shibata (N)

Division of Infection and Host Defense, Tohoku Medical and Pharmaceutical University, Sendai, Japan.

Hiromitsu Hara (H)

Department of Immunology, Graduate School of Medical and Dental Sciences, Kagoshima University, Kagoshima, Japan.

Yoichiro Iwakura (Y)

Research Institute for Biomedical Sciences, Tokyo University of Science, Chiba, Japan.

Tomomi Hashidate-Yoshida (T)

Department of Lipid Life Science, National Center for Global Health and Medicine, Tokyo, Japan.

Hideo Shindou (H)

Department of Lipid Life Science, National Center for Global Health and Medicine, Tokyo, Japan.
Department of Medical Lipid Science, Graduate School of Medicine, University of Tokyo, Tokyo, Japan.

Takao Shimizu (T)

Department of Lipid Signaling, National Center for Global Health and Medicine, Tokyo, Japan.
Institute of Microbial Chemistry, Tokyo, Japan.

Taiki Oyama (T)

Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.

Himawari Matsunaga (H)

Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan.

Kazuhiko Takahara (K)

Department of Animal Development and Physiology, Graduate School of Biostudies, Kyoto University, Kyoto, Japan. ktakahar@zoo.zool.kyoto-u.ac.jp.

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