Lysozyme-Induced Transcriptional Regulation of TNF-α Pathway Genes in Cells of the Monocyte Lineage
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Lysozyme is one of the most important anti-bacterial effectors in the innate immune system of animals. Besides its direct antibacterial enzymatic activity, lysozyme displays other biological properties, pointing toward a significant anti-inflammatory effect, many aspects of which are still elusive. Here we investigate the perturbation of gene expression profiles induced by lysozyme in a monocyte cell line in vitro considering a perspective as broad as the whole transcriptome profiling. The results of the RNA-seq experiment show that lysozyme induces transcriptional modulation of the TNF-α/IL-1β pathway genes in U937 monocytes. The analysis of transcriptomic profiles with IPA® identified a simple but robust molecular network of genes, in which the regulation trends are fully consistent with the anti-inflammatory activity of lysozyme. This study provides the first evidence in support of the anti-inflammatory action of lysozyme on the basis of transcriptomic regulation data resulting from the broad perspective of a whole-transcriptome profiling. Such important effects can be achieved with the supplementation of relatively low concentrations of lysozyme, for a short time of exposure. These new insights allow the potential of lysozyme in pharmacological applications to be better exploited.
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The significant up-regulation of S100A8 and LYZ suggests an enhanced inflammatory response in AD monocytes.
“Given their major roles in the immune response and inflammation (54, 55), the significant up-regulation of S100A8 and LYZ suggested an enhanced inflammatory response in AD monocytes.”
From Understanding monocyte-driven neuroinflammation in Alzheimer’s disease using human cortical organoid microphysiological systems (2025) · cites this paper as [55]
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Cites
Cox, J., & Mann, M. (2008) · Nature Biotechnology · doi:10.1038/nbt.1511 · Cited by 14,855 · see citing works
Universal sample preparation method for proteome analysis
Wiśniewski, J. R., Zougman, A., Nagaraj, N., & Mann, M. (2009) · Nature Methods · doi:10.1038/nmeth.1322 · Cited by 8,352 · see citing works
The Perseus computational platform for comprehensive analysis of (prote)omics data
Tyanova, S., Temu, T., Sinitcyn, P. G., Carlson, A., Hein, M. Y., Geiger, T., Mann, M., & Cox, J. (2016) · Nature Methods · doi:10.1038/nmeth.3901 · Cited by 7,977 · see citing works
Global quantification of mammalian gene expression control
Schwanhäusser, B., Busse, D., Li, N., Dittmar, G., Schuchhardt, J., Wolf, J., Chen, W., & Selbach, M. (2011) · Nature · doi:10.1038/nature10098 · Cited by 6,566 · cited 1× · see citing works
“The biological uncoupling between the levels of mRNA and proteins may be the consequence of half-life difference between proteins and mRNAs, these latter being five-times less stable than proteins in mammalian cells [54].”
BackgroundCox, J., Hein, M. Y., Luber, C. A., Paron, I., Nagaraj, N., & Mann, M. (2014) · Molecular & Cellular Proteomics · doi:10.1074/mcp.m113.031591 · Cited by 5,180 · see citing works
Rappsilber, J., Mann, M., & Ishihama, Y. (2007) · Nature Protocols · doi:10.1038/nprot.2007.261 · Cited by 4,641 · see citing works
Correlation between Protein and mRNA Abundance in Yeast
Gygi, S. P., Rochon, Y., Franza, B. R., & Aebersold, R. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.3.1720 · Cited by 3,819 · see citing works
Establishment and characterization of a human histiocytic lymphoma cell line (U‐937)
Sundström, C., & Nilsson, K. (1976) · International Journal of Cancer · doi:10.1002/ijc.2910170504 · Cited by 2,409 · see citing works
Expansion of the eukaryotic proteome by alternative splicing
Nilsen, T. W., & Graveley, B. R. (2010) · Nature · doi:10.1038/nature08909 · Cited by 2,172 · see citing works
Correlation of mRNA and protein in complex biological samples
Maier, T., Güell, M., & Serrano, L. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.10.036 · Cited by 1,802 · see citing works
Kulak, N. A., Pichler, G., Paron, I., Nagaraj, N., & Mann, M. (2014) · Nature Methods · doi:10.1038/nmeth.2834 · Cited by 1,719 · see citing works
On a remarkable bacteriolytic element found in tissues and secretions
Fleming, A. (1922) · Proceedings of the Royal Society of London Series B Containing Papers of a Biological Character · doi:10.1098/rspb.1922.0023 · Cited by 1,156 · see citing works
From bacterial killing to immune modulation: Recent insights into the functions of lysozyme
Ragland, S. A., & Criss, A. K. (2017) · PLoS Pathogens · doi:10.1371/journal.ppat.1006512 · Cited by 873 · see citing works
Lysozymes in the animal kingdom
Callewaert, L., & Michiels, C. W. (2010) · Journal of Biosciences · doi:10.1007/s12038-010-0015-5 · Cited by 763 · see citing works
Protein kinase cascades activated by stress and inflammatory cytokines
Kyriakis, J. M., & Avruch, J. (1996) · BioEssays · doi:10.1002/bies.950180708 · Cited by 709 · see citing works
Wolpe, S. D., Davatelis, G., Sherry, B. A., Beutler, B., HESSE, D. G., Nguyen, H. T., Moldawer, L. L., Nathan, C. F., Lowry, S. F., & Cerami, A. (1988) · The Journal of Experimental Medicine · doi:10.1084/jem.167.2.570 · Cited by 571 · see citing works
Quantitative proteomics combined with BAC TransgeneOmics reveals in vivo protein interactions
Hubner, N. C., Bird, A. W., Cox, J., Splettstoesser, B., Bandilla, P., Poser, I., Hyman, A., & Mann, M. (2010) · Journal of Cell Biology · doi:10.1083/jcb.200911091 · Cited by 440 · see citing works
The chemistry of lysozyme and its use as a food preservative and a pharmaceutical
PROCTOR, V. A., Cunningham, F. E., & Fung, D. Y. C. (1988) · C R C Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398809527473 · Cited by 439 · see citing works
IEX -1L, an Apoptosis Inhibitor Involved in NF-κB-Mediated Cell Survival
Wu, M. X., Ao, Z., Prasad, K. V. S., Wu, R., & Schlossman, S. F. (1998) · Science · doi:10.1126/science.281.5379.998 · Cited by 414 · see citing works
Lysozyme and RNases as anti-HIV components in β-core preparations of human chorionic gonadotropin
Lee‐Huang, S., Huang, P. L., Sun, Y., Huang, P. L., Kung, H., Blithe, D., & Chen, H. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.6.2678 · Cited by 354 · see citing works
Genetic evidence that antibacterial activity of lysozyme is independent of its catalytic function
Ibrahim, H. R., Matsuzaki, T., & Aoki, T. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02872-1 · Cited by 348 · see citing works
What is new in lysozyme research and its application in food industry? A review
Wu, T., Jiang, Q., Wu, D., Hu, Y., Chen, S., Ding, T., Ye, X., Liu, D., & Chen, J. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.09.017 · Cited by 281 · see citing works
Novel Natural Food Antimicrobials
Juneja, V. K., Dwivedi, H. P., & Yan, X. (2012) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-022811-101241 · Cited by 266 · see citing works
Advances in targeted proteomics and applications to biomedical research
Shi, T., Song, E., Nie, S., Rodland, K., Liu, T., Qian, W., & Smith, R. D. (2016) · PROTEOMICS · doi:10.1002/pmic.201500449 · Cited by 259 · see citing works
Bacterial Wall as Target for Attack
Koch, A. L. (2003) · Clinical Microbiology Reviews · doi:10.1128/cmr.16.4.673-687.2003 · Cited by 232 · see citing works
Tenovuo, J. O. (2002) · Oral Diseases · doi:10.1034/j.1601-0825.2002.1o781.x · Cited by 216 · see citing works
Integrating transcriptome and proteome profiling: Strategies and applications
Kumar, D., Bansal, G., Narang, A., Basak, T., Abbas, T., & Dash, D. (2016) · PROTEOMICS · doi:10.1002/pmic.201600140 · Cited by 186 · see citing works
c-Jun NH 2 -Terminal Kinase Is Essential for the Regulation of AP-1 by Tumor Necrosis Factor
Ventura, J., Kennedy, N. J., Lamb, J. A., Flavell, R. A., & Davis, R. J. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.8.2871-2882.2003 · Cited by 156 · see citing works
The Peptidoglycan-Degrading Property of Lysozyme Is Not Required for Bactericidal Activity In Vivo
Nash, J. A., Ballard, T. N. S., Weaver, T. E., & Akinbi, H. T. (2006) · The Journal of Immunology · doi:10.4049/jimmunol.177.1.519 · Cited by 154 · see citing works
Lee, M., Kovacs-Nolan, J., Yang, C., Archbold, T. L., Fan, M. Z., & Mine, Y. (2009) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf803133b · Cited by 153 · see citing works
Opdenakker, G., Froyen, G., Fiten, P., Proost, P., & Vandamme, J. (1993) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1993.1251 · Cited by 117 · see citing works
A cDNA Clone Used to Study mRNA Inducible in Human Tonsillar Lymphocytes by a Tumor Promoter1
Obaru, K., FUKUDA, M., Maeda, S., & 島田, 和. (1986) · The Journal of Biochemistry · doi:10.1093/oxfordjournals.jbchem.a135549 · Cited by 116 · see citing works
Structures of Human Genes Coding for Cytokine LD78 and Their Expression
Nakao, M., Nomiyama, H., & 島田, 和. (1990) · Molecular and Cellular Biology · doi:10.1128/mcb.10.7.3646 · Cited by 113 · see citing works
Identification of a ubiquitin family protein as a novel neutrophil chemotactic factor
Owhashi, M., Taoka, Y., Ishii, K., Nakazawa, S., Uemura, H., & Kambara, H. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2003.08.038 · Cited by 104 · see citing works
A novel anti‐inflammatory activity of lysozyme: modulation of serum complement activation
Ogundele, M. O. (1998) · Mediators of Inflammation · doi:10.1080/09629359890893 · Cited by 99 · see citing works
Lysozyme Transgenic Goats’ Milk Influences Gastrointestinal Morphology in Young Pigs ,
Brundige, D. R., Maga, E. A., Klasing, K. C., & Murray, J. D. (2008) · Journal of Nutrition · doi:10.1093/jn/138.5.921 · Cited by 97 · see citing works
Maga, E. A., Walker, R. L., Anderson, G. B., & Murray, J. D. (2006) · Transgenic Research · doi:10.1007/s11248-006-0014-3 · Cited by 74 · see citing works
Zheng, F., Cai, W., Mitsuhashi, T., Vlassara, H., & Bucala, R. (2001) · Molecular Medicine · doi:10.1007/bf03401963 · Cited by 71 · see citing works
Inhibitory effects of oroxylin A on endothelial protein C receptor shedding in vitro and in vivo
Ku, S., Han, M. S., Lee, M. Y., Lee, Y. M., & Bae, J. (2014) · BMB Reports · doi:10.5483/bmbrep.2014.47.6.198 · Cited by 70 · see citing works
Mitsuhashi, T., Li, Y. M., Fishbane, S., & Vlassara, H. (1997) · Journal of Clinical Investigation · doi:10.1172/jci119600 · Cited by 68 · see citing works
Binding of lysozyme to lipopolysaccharide suppresses tumor necrosis factor production in vivo
Takada, K., Ohno, N., & Yadomae, T. (1994) · Infection and Immunity · doi:10.1128/iai.62.4.1171-1175.1994 · Cited by 67 · see citing works
Nakimbugwe, D., Masschalck, B., Deckers, D., Callewaert, L., Aertsen, A., & Michiels, C. W. (2006) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2006.00240.x · Cited by 67 · see citing works
Anti-inflammatory effect of lysozyme from hen egg white on mouse peritoneal macrophages
Tagashira, A., Nishi, K., Matsumoto, S., & Sugahara, T. (2018) · Cytotechnology · doi:10.1007/s10616-017-0184-2 · Cited by 53 · see citing works
Lysozyme Association with Nucleic Acids
Steinrauf, L. K., Shiuan, D., Yang, W.-J., & Chiang, M. Y. (1999) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1999.1804 · Cited by 47 · see citing works
Lin, K., Wey, M., Kan, L., & Shiuan, D. (2008) · Applied Biochemistry and Biotechnology · doi:10.1007/s12010-008-8348-3 · Cited by 38 · see citing works
Asakura, K., Kojima, T., Shirasaki, H., & Kataura, A. (1990) · Auris Nasus Larynx · doi:10.1016/s0385-8146(12)80018-6 · Cited by 35 · see citing works
Inhibitory effects of lysozyme on endothelial protein C 1receptor shedding in vitro and in vivo
Ku, S., Yoon, E.-K., Lee, H. G., Han, M. S., Lee, T., & Bae, J. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.11.038 · Cited by 32 · see citing works
Tenebäck, C. C., Scanlon, T. C., Wargo, M. J., Bement, J. L., Griswold, K. E., & Leclair, L. W. (2013) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.00500-13 · Cited by 29 · see citing works
Lysozyme association with circulating RNA, extracellular vesicles, and chronic stress
Abey, S. K., Yuana, Y., Joseph, P. V., Kenea, N. D., Fourie, N. H., Sherwin, L. B., Gonye, G. E., Smyser, P. A., Stempinski, E., Boulineaux, C. M., et al. (2016) · BBA Clinical · doi:10.1016/j.bbacli.2016.12.003 · Cited by 27 · see citing works
Ibrahim, H. R., Hamasaki, K., & Miyata, T. (2017) · European Journal of Pharmaceutical Sciences · doi:10.1016/j.ejps.2017.07.005 · Cited by 26 · see citing works
Lysozyme-rich mucus metaplasia in duodenal crypts supersedes Paneth cells in celiac disease
Rubio‐Terres, C. (2011) · Archiv für Pathologische Anatomie und Physiologie und für Klinische Medicin · doi:10.1007/s00428-011-1129-3 · Cited by 23 · see citing works
Cocchietto, M., Zorzin, L., Toffoli, B., Candido, R., Fabris, B., Stebel, M., & Sava, G. (2008) · Diabetes & Metabolism · doi:10.1016/j.diabet.2008.05.009 · Cited by 22 · see citing works
Self-citationLysozyme from hen egg white ameliorates lipopolysaccharide-induced systemic inflammation in mice
Tagashira, A., Nishi, K., & Sugahara, T. (2019) · Cytotechnology · doi:10.1007/s10616-019-00296-4 · Cited by 21 · see citing works
Suppressive effects of lysozyme on polyphosphate-mediated vascular inflammatory responses
Chung, J., Ku, S., Lee, S., & Bae, J. (2016) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2016.05.016 · Cited by 20 · see citing works
Lysozyme regulates LPS-induced interleukin-6 release in mice.
Takada, K., Ohno, N., & Yadomae, T. (1994) · PubMed · Cited by 19 · see citing works
Gallo, D., Cocchietto, M., Masat, E., Agostinis, C., Harei, E., Veronesi, P., & Sava, G. (2014) · Experimental Biology and Medicine · doi:10.1177/1535370213518281 · Cited by 18 · see citing works
Self-citationOhbayashi, H., Setoguchi, Y., Fukuchi, Y., Shibata, K., Sakata, Y., & Arai, T. (2016) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2016.03.001 · Cited by 18 · see citing works
Rubio‐Terres, C., & Befrits, R. (2009) · PubMed Central · Cited by 14 · see citing works
Recovery of Lymphocyte CD4+: CD8+ Ratio in Patients Treated with Lysozyme
Cartel, F., Cartei, G., Ceschia, V., Pacor, S., & Sava, G. (1992) · Clinical Drug Investigation · doi:10.1007/bf03258379 · Cited by 14 · see citing works
Self-citationLysozyme expression in microscopic colitis
Rubio‐Terres, C. (2011) · Journal of Clinical Pathology · doi:10.1136/jcp.2010.086850 · Cited by 13 · see citing works
Inhibitory effects of epi-sesamin on endothelial protein C receptor shedding in vitro and in vivo
Ku, S., Lee, W., Yoo, H., Han, C.-K., & Bae, J. (2013) · Inflammation Research · doi:10.1007/s00011-013-0648-6 · Cited by 11 · see citing works
PEGylated lysozymes with anti-septic effects in human endothelial cells and in mice
Lee, W., Park, E. J., Kwak, S., Kim, Y., Na, D. H., & Bae, J. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.02.167 · Cited by 8 · see citing works
Lysozyme is up-regulated in Barrett’s mucosa
Rubio‐Terres, C., & Lörinc, E. (2011) · Histopathology · doi:10.1111/j.1365-2559.2011.03830.x · Cited by 7 · see citing works
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Applications of Lysozyme, an Innate Immune Defense Factor, as an Alternative Antibiotic
Ferraboschi, P., Ciceri, S., & Grisenti, P. (2021) · Antibiotics · doi:10.3390/antibiotics10121534 · Cited by 455 · see citing works
Coulton, A., Murai, J., Qian, D., Thakkar, K., Lewis, C. E., & Litchfield, K. (2024) · Nature Communications · doi:10.1038/s41467-024-49885-8 · Cited by 114 · see citing works
Zhou, N., Zhao, Y., Yao, Y., Wu, N., Xu, M., Du, H., Wu, J., & Tu, Y. (2021) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.1c04742 · Cited by 75 · see citing works
Lysozyme: A Natural Product with Multiple and Useful Antiviral Properties
Bergamo, A., & Sava, G. (2024) · Molecules · doi:10.3390/molecules29030652 · Cited by 52 · see citing works
Self-citationWang, Y., Li, S., Jin, M., Han, Q., Liu, S., Chen, X., & Han, Y. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21051635 · Cited by 49 · see citing works
Zhang, Q., Zhao, Y., Yao, Y., Wu, N., Chen, S., Xu, L., & Tu, Y. (2024) · Food Research International · doi:10.1016/j.foodres.2024.114114 · Cited by 37 · see citing works
Mikkelsen, K., Dargahi, N., Fraser, S., & Apostolopoulos, V. (2023) · Biomedicines · doi:10.3390/biomedicines11092578 · Cited by 34 · see citing works
Enzyme-Based Anti-Inflammatory Therapeutics for Inflammatory Diseases
Narayanan, K. B. (2025) · Pharmaceutics · doi:10.3390/pharmaceutics17050606 · Cited by 33 · see citing works
Wang, Q., Huang, T., Zheng, Z., Su, Y., Wu, Z., Zeng, C., Yu, G., Liu, Y., Wang, X., Li, H., et al. (2025) · Science Translational Medicine · doi:10.1126/scitranslmed.adn9980 · Cited by 32 · see citing works
Pharmacological Modulation of Host Immunity with Hen Egg White Lysozyme (HEWL)—A Review
Bergamo, A., & Sava, G. (2023) · Molecules · doi:10.3390/molecules28135027 · Cited by 24 · see citing works
Self-citationBastamy, M., Raheel, I. A., Elbestawy, A. R., Diab, M., Hammad, E., El-Ebeedy, L. A., EL-Barbary, A. M., Albadrani, G. M., Abdel‐Daim, M. M., Abdel-Latif, M. A., et al. (2024) · Animal Biotechnology · doi:10.1080/10495398.2024.2309955 · Cited by 23 · see citing works
Natnan, M. E., Low, C. F., Chong, C. M., Daud, N. I. N. A. A., Om, A. D., & Baharum, S. N. (2022) · Biology · doi:10.3390/biology11091288 · Cited by 22 · see citing works
Roy, S., Srinivasan, V. R., Arunagiri, S., Mishra, N., Bhatia, A., Shejale, K. P., Prajapati, K. P., Kar, K., & Anand, B. G. (2024) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2024.103205 · Cited by 21 · see citing works
Tarahi, M., Kalita, P., Deka, H., Oladzadabbasabadi, N., Ghaderi, S., Tavassoli, M., & Roy, S. (2025) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2025.105267 · Cited by 13 · see citing works
The Deletion of IL-17A Enhances Helicobacter hepaticus Colonization and Triggers Colitis
Zhu, L., Wu, Z., Zhu, C. X., Yin, J., Huang, Y., Feng, J., & Zhang, Q. (2022) · Journal of Inflammation Research · doi:10.2147/jir.s359100 · Cited by 13 · see citing works
RetractedShen, L., Cao, S., Wang, Y., Zhou, P., Wang, S., Zhao, Y., Meng, L., Zhang, Q., Li, Y., Xu, X., et al. (2022) · ACS Applied Materials & Interfaces · doi:10.1021/acsami.2c19026 · Cited by 13 · see citing works
Lysozyme promotes renal fibrosis through the JAK/STAT3 signal pathway in diabetic nephropathy
Ren, Y., Yu, M., Zheng, D., He, W., & Jin, J. (2023) · Archives of Medical Science · doi:10.5114/aoms/170160 · Cited by 12 · see citing works
Zhou, N., Yao, Y., Wu, N., Du, H., Xu, M., Zhao, Y., & Tu, Y. (2021) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.202100682 · Cited by 11 · see citing works
Tian, C., Ao, Z., Cerneckis, J., Cai, H., Chen, L., Niu, H., Takayama, K., Kim, J., Shi, Y., Gu, M., et al. (2025) · Science Advances · doi:10.1126/sciadv.adu2708 · Cited by 9 · see citing works
“Given their major roles in the immune response and inflammation ( 54 , 55 ), the significant up-regulation of S100A8 and LYZ suggested an enhanced inflammatory response in AD monocytes.”
Soveral, L. D. F., de Almeida, P. A., Kreutz, Y., Ribeiro, V. A., Frandoloso, R., & Kreutz, L. C. (2022) · Fish and Shellfish Immunology Reports · doi:10.1016/j.fsirep.2022.100053 · Cited by 9 · see citing works
Lysozyme in the treatment of non-infectious sore throat
Glamočlija, U., Mehić, M., Šukalo, A., Avdić, A. T., & Jaganjac, J. D. (2020) · Biomolecules and Biomedicine · doi:10.17305/bjbms.2019.4619 · Cited by 8 · see citing works
Regulation of Lysozyme Activity by Human Hormones
Панкратов, Т. А., Gannesen, A. V., & Nikolaev, Y. A. (2023) · Iranian Biomedical Journal · doi:10.52547/ibj.3614 · Cited by 7 · see citing works
Dai, L., Lou, N., Huang, L., Li, L., Tang, L. M., Shi, Y., & Han, X. (2025) · Cancer Immunology Immunotherapy · doi:10.1007/s00262-025-03968-7 · Cited by 6 · see citing works
Zhang, Y., Zhang, Q., Li, S., Zhao, Y., Lv, X., & Xu, X. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.143297 · Cited by 6 · see citing works
Yubolphan, R., Phongsiri, K., Mongkhammee, N., Pidech, J., Roytrakul, S., Suwattanasophon, C., Choowongkomon, K., Daduang, S., Khunkitti, W., & Jangpromma, N. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.70713 · Cited by 6 · see citing works
Zhang, P., Bi, Y., Zhao, X., Chen, K., Chen, E., & Xiao, C. (2025) · Frontiers in Immunology · doi:10.3389/fimmu.2025.1574783 · Cited by 5 · see citing works
Han, N.-C., de Souza, L. C., Johnson, C. D., Klein, J. R., Kirkpatrick, T., Silva, R., & Letra, A. (2023) · Journal of Endodontics · doi:10.1016/j.joen.2023.05.002 · Cited by 5 · see citing works
IFN‐γ stimulates Paneth cell secretion through necroptosis mTORC1 dependent
Encarnacion‐Garcia, M. R., la Torre‐Baez, R. D., Hernandez‐Cueto, M. A., Velázquez‐Villegas, L. A., Candelario‐Martínez, A., Sánchez-Argáez, A. B., Horta‐López, P. H., Montoya‐García, A., Jaimes‐Ortega, G. A., Lopez-Bailon, L. U., et al. (2024) · European Journal of Immunology · doi:10.1002/eji.202350716 · Cited by 4 · see citing works
Tian, C., Ao, Z., Cerneckis, J., Cai, H., Chen, L., Niu, H., Takayama, K., Kim, J., Shi, Y., Gu, M., et al. (2025) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2025.02.16.638539 · Cited by 3 · see citing works
Wang, Q., Huang, T., Zheng, Z., Su, Y., Wu, Z., Yu, G., Liu, Y., Wang, X., Li, H., Chen, X., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.10.10.561804 · Cited by 2 · see citing works
Karakaš, S., Huduti, D., Mehić, M., Šukalo, A., Jaganjac, J. D., Avdić, A. T., Skopljak, A., Dupovac, A., Sarajlić, Z., & Glamočlija, U. (2022) · Acta Medica Academica · doi:10.5644/ama2006-124.364 · Cited by 1 · see citing works
Joshua, P. E., Ilo, C. C., Ukachukwu, U. G., Odimegwu, D. C., Asomadu, R. O., & Ezeorba, T. P. C. (2023) · Future Journal of Pharmaceutical Sciences · doi:10.1186/s43094-023-00481-5 · Cited by 1 · see citing works
Encarnacion‐Garcia, M. R., la Torre‐Baez, R. D., Hernandez‐Cueto, M. A., Velázquez‐Villegas, L. A., Candelario‐Martínez, A., Horta‐López, P. H., Montoya‐García, A., Jaimes‐Ortega, G. A., Lopez-Bailon, L. U., Piedra-Quintero, Z. L., et al. (2023) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2023.05.13.540666
Sun, J., Wang, Y., Zhang, Y., Peng, Y., Liu, W., Li, X., Cai, Z., Huang, X., Lu, Y., & Sheng, L. (2025) · Food, Nutrition and Health. · doi:10.1007/s44403-025-00023-2
Causal link between mental disorders and gastrointestinal diseases: a Mendelian randomization study
Ding, W., Chen, L., Pei, B., Gao, D., Xia, J., Li, X., & Wang, Y. (2025) · Frontiers in Endocrinology · doi:10.3389/fendo.2025.1288619
Jia, J., lin, H., Chen, Z., He, K., Cao, H., Li, Z., Cao, J., Li, Y., & Yin, M. (2025) · Research Square · doi:10.21203/rs.3.rs-7605804/v1
Joshua, P. E., Ilo, C. C., Ukachukwu, U. G., Odimegwu, D. C., Asomadu, R. O., & Ezeorba, T. P. C. (2024) · Figshare · doi:10.6084/m9.figshare.26580533
Zantioti, C., & Malandrakis, E. E. (2026) · Probiotics and Antimicrobial Proteins · doi:10.1007/s12602-026-10933-y
Ivanova, E. V., Н., Ч. И., Nb, P., Bekpergenova, A. V., & Bondarenko, T. A. (2026) · Russian Journal of Immunology · doi:10.46235/1028-7221-17082-teo
Valete, E. J., Espiritu, H. M., & Cho, Y.-I. (2026) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2026.111129
Urbańska, D. M., Pawlik, M. J., Korwin‐Kossakowska, A., Rutkowska, K., Kawecka-Grochocka, E., Czopowicz, M., Mickiewicz, M., Kaba, J., & Bagnicka, E. (2026) · Animal Science Papers and Reports · doi:10.2478/aspr-2026-0019
- Authors
- Bergamo, A., Gerdol, M., Pallavicini, A., Greco, S., Schepens, I., Hamelin, R., Armand, F., Dyson, P. J., & Sava, G.
- Affiliations
- Callerio Foundation Onlus, 34127 Trieste, Italy
- University of Trieste (IT)
- École Polytechnique Fédérale de Lausanne (CH)
- Corresponding author
- Bergamo, Alberta
- ORCID
- Venue
- International Journal of Molecular Sciences
- Publisher
- MDPI AG
- Published
- 2019-11-05
- Volume
- 20
- Issue
- 21
- Pages
- 5502
- ISSN
- 1422-0067 (ISSN-L)
- PMC
- PMC6862675
- OpenAlex
- W2984064714
- Cited by
- 42
- References
- 65
- Citations by year
- 2026: 4 · 2025: 12 · 2024: 7 · 2023: 8 · 2022: 5 · 2021: 4 · 2020: 2
- FWCI
- 1.10
- Type
- journal article
- Language
- en
- Open access
- gold
- dx.doi.org
- Licence
- Locations
- International Journal of Molecular Sciences (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- ArTS Archivio della ricerca di Trieste (University of Trieste https://www.units.it/) (submittedVersion, cc-by)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Infoscience (Ecole Polytechnique Fédérale de Lausanne) (submittedVersion, cc-by-nc-nd)
- Funders
- École Polytechnique Fédérale de Lausanne
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Immune Response and Inflammation
- Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
- Keywords
- lysozyme, anti-inflammatory activity, transcriptional regulation, monocytes, U937 cells, gene expression profiling, innate immunity, transcriptome, molecular networks
- MeSH terms
- Cell Line, Humans, Inflammation, Monocytes, Muramidase, Tumor Necrosis Factor-alpha, Signal Transduction, Transcriptional Activation, Interleukin-1beta, Transcriptome
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