Cited by 383Antimicrobial Peptides and ActivitiesGut microbiota and healthProbiotics and Fermented Foods

The DOI matches its Crossref record; 41 of the 41 references it cites were found in a registry or an index.

Expression of the cathelicidin LL-37 is modulated by short chain fatty acids in colonocytes: relevance of signalling pathways

Open access

Schauber, J·2003·Gut

Open this paper in CoChat — free account Open PDF

Abstract

BACKGROUND AND AIMS: Short chain fatty acids (SCFA) exert profound effects on the colonic mucosa. In particular, SCFA modulate mucosal immune functions. The antimicrobial cathelicidin LL-37 is expressed by colon epithelial cells. In the present study the effect of SCFA on LL-37 expression was investigated. METHODS: LL-37 expression in vivo was assessed by immunohistochemistry. Real time quantitative reverse transcription-polymerase chain reaction was employed to determine LL-37 expression in colonocytes in vitro after treatment with various cytokines, SCFA, or flavone. LL-37 levels were correlated to cell differentiation which was determined by alkaline phosphatase (AP) activity. In addition, intracellular signalling pathways such as MEK-ERK (mitogen/extracellular signal protein kinase (MEK)/extracellular signal regulated protein kinase (ERK)) and p38/mitogen activated protein (MAP) kinase were explored. RESULTS: In vivo, LL-37 expression in healthy mucosa was restricted to differentiated epithelial cells in human colon and ileum. In colonocytes, increased LL-37 expression associated with cell differentiation was detected in vitro following treatment with butyrate, isobutyrate, propionate, and trichostatin A. Flavone induced LL-37 transcription but did not affect AP activity while cytokines had no effect. To dissect pathways mediating differentiation and LL-37 expression, specific inhibitors were applied. Inhibition of the protein kinase MEK enhanced butyrate induced AP activity while LL-37 expression in colon epithelial cells was blocked. In contrast, inhibition of p38/MAP kinase blocked cell differentiation without inhibiting LL-37 expression. CONCLUSIONS: Expression of the cathelicidin LL-37 in colonocytes and cellular differentiation are separately modulated by SCFA via distinct signalling pathways. These data may provide a rationale for dietary modulation of mucosal defence mechanisms.

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Integrity signals

Registry

Crossref · 10.1136/gut.52.5.735

Cites

41 of 41 references verified0 citation errors · 0 not checkable

Statistics

Claims the paper makes

The claims and statistics of this paper haven’t been checked yet.

Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Self-check

Percentages, sums and reported differences re-computed from the paper’s own numbers.

The self-check needs the paper’s full text.

A peptide antibiotic from human skin
Harder, J., Bartels, J., Christophers, E., & Schröder, J. ‐. (1997) · Nature · doi:10.1038/43088 · Cited by 1,365
Innate antimicrobial peptide protects the skin from invasive bacterial infection
Nizet, V., Ohtake, T., Lauth, X., Trowbridge, J., Rudisill, J., Dorschner, R. A., Pestonjamasp, V., Piraino, J., Huttner, K., & Gallo, R. L. (2001) · Nature · doi:10.1038/35106587 · Cited by 1,198
Human β-Defensin-1 Is a Salt-Sensitive Antibiotic in Lung That Is Inactivated in Cystic Fibrosis
Goldman, M. J., Anderson, G. M., Stolzenberg, E. D., Kari, U. P., ZASLOFF, M. A., & Wilson, J. M. (1997) · Cell · doi:10.1016/s0092-8674(00)81895-4 · Cited by 1,077
Regulation of Intestinal α-Defensin Activation by the Metalloproteinase Matrilysin in Innate Host Defense
Wilson, C. L., Ouellette, A. J., Satchell, D. P., Ayabe, T., López-Boado, Y. S., Stratman, J. L., Hultgren, S. J., Matrisian, L. M., & Parks, W. C. (1999) · Science · doi:10.1126/science.286.5437.113 · Cited by 1,076
The Expression of the Gene Coding for the Antibacterial Peptide LL-37 Is Induced in Human Keratinocytes during Inflammatory Disorders
Frohm, M., Agerberth, B., Ahangari, G., Ståhle‐Bäckdahl, M., Lidén, S., Wigzell, H., & Gudmundsson, G. H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.24.15258 · Cited by 803
The human antimicrobial and chemotactic peptides LL-37 and α-defensins are expressed by specific lymphocyte and monocyte populations
Agerberth, B., Charo, J., Werr, J., Olsson, B., Idali, F., Lindbom, L., Kiessling, R., Jörnvall, H., Wigzell, H., & Gudmundsson, G. H. (2000) · Blood · doi:10.1182/blood.v96.9.3086 · Cited by 758
Effects of short chain fatty acids on gut morphology and function
Scheppach, W. (1994) · Gut · doi:10.1136/gut.35.1_suppl.s35 · Cited by 756
The peptide antibiotic LL-37/hCAP-18 is expressed in epithelia of the human lung where it has broad antimicrobial activity at the airway surface
Bals, R., Wang, X., ZASLOFF, M. A., & Wilson, J. M. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.16.9541 · Cited by 745
Effect of butyrate enemas on the colonic mucosa in distal ulcerative colitis
Scheppach, W. M., Sommer, H., Kirchner, T., Paganelli, G.-M., Bartram, P., Christl, S. U., Richter, F., Dusel, G., & Kasper, H. (1992) · Gastroenterology · doi:10.1016/0016-5085(92)91094-k · Cited by 740
Conformation-dependent Antibacterial Activity of the Naturally Occurring Human Peptide LL-37
Johansson, J., Gudmundsson, G. H., Rottenberg, M. E., Berndt, K. D., & Agerberth, B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.6.3718 · Cited by 662

Show all 41 references

Sorted by citations

Items 101–200 of 382

Bacterial exotoxins downregulate cathelicidin (hCAP-18/LL-37) and human β-defensin 1 (HBD-1) expression in the intestinal epithelial cells
Chakraborty, K., Ghosh, S., Koley, H., Mukhopadhyay, A. K., Ramamurthy, T., Saha, D. R., Mukhopadhyay, D., Roychowdhury, S., Hamabata, T., Takeda, Y., et al. (2008) · Cellular Microbiology · doi:10.1111/j.1462-5822.2008.01227.x · Cited by 116
Histone-deacetylase inhibitors induce the cathelicidin LL-37 in gastrointestinal cells
Schauber, J., Iffland, K., Frisch, S., Kudlich, T., Schmausser, B., Eck, M., Menzel, T., Gostner, A., Lührs, H., & Scheppach, W. (2004) · Molecular Immunology · doi:10.1016/j.molimm.2004.05.005 · Cited by 109
Self-citation
Innate immune defence in the human gastrointestinal tract
Dommett, R. M., Zilbauer, M., George, J. T., & Bajaj‐Elliott, M. (2005) · Molecular Immunology · doi:10.1016/j.molimm.2004.12.004 · Cited by 109
α-Defensins in Enteric Innate Immunity
Mastroianni, J. R., & Ouellette, A. J. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.050773 · Cited by 109
Gut microbiota metabolite regulation of host defenses at mucosal surfaces: implication in precision medicine
Bilotta, A. J., & Cong, Y. (2019) · Precision Clinical Medicine · doi:10.1093/pcmedi/pbz008 · Cited by 113
The bacteriome–mycobiome interaction and antifungal host defense
ten Oever, J., & Netea, M. G. (2014) · European Journal of Immunology · doi:10.1002/eji.201344405 · Cited by 106
Innate immune defenses in the intestinal tract
Dann, S. M., & Eckmann, L. (2007) · Current Opinion in Gastroenterology · doi:10.1097/mog.0b013e32803cadf4 · Cited by 104
Antimicrobial Host Defence Peptides: Immunomodulatory Functions and Translational Prospects
van der Does, A. M., Hiemstra, P. S., & Mookherjee, N. (2019) · Advances in experimental medicine and biology · doi:10.1007/978-981-13-3588-4_10 · Cited by 105
LL-37 transports immunoreactive cGAMP to activate STING signaling and enhance interferon-mediated host antiviral immunity
Wei, X., Zhang, L., Yang, Y., Hou, Y., Xu, Y., Wang, Z., Su, H., Han, F., Han, J., Liu, P., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.110880 · Cited by 103
Review: Human antimicrobial proteins — effectors of innate immunity
Harder, J., Gläser, R., & Schröder, J. (2007) · Journal of Endotoxin Research · doi:10.1177/0968051907088275 · Cited by 101
Interspecies cathelicidin comparison reveals divergence in antimicrobial activity, TLR modulation, chemokine induction and regulation of phagocytosis
Coorens, M., Scheenstra, M. R., Veldhuizen, E. J. A., & Haagsman, H. P. (2017) · Scientific Reports · doi:10.1038/srep40874 · Cited by 103
Phenylbutyrate Counteracts Shigella Mediated Downregulation of Cathelicidin in Rabbit Lung and Intestinal Epithelia: A Potential Therapeutic Strategy
Sarker, P., Ahmed, S., Tiash, S., Rekha, R. S., Strömberg, R., Andersson, J., Bergman, P., Gudmundsson, G. H., Agerberth, B., & Raqib, R. (2011) · PLoS ONE · doi:10.1371/journal.pone.0020637 · Cited by 102
Short chain fatty acids (propionic and hexanoic) decrease Staphylococcus aureus internalization into bovine mammary epithelial cells and modulate antimicrobial peptide expression
Alva-Murillo, N., Ochoa‐Zarzosa, A., & López-Meza, J. E. (2011) · Veterinary Microbiology · doi:10.1016/j.vetmic.2011.08.025 · Cited by 99
Immune Response in the Barrier Epithelia: Lessons from the Fruit Fly Drosophila melanogaster
Davis, M. M., & Engström, Y. (2012) · Journal of Innate Immunity · doi:10.1159/000332947 · Cited by 97
Cathelicidins Inhibit Escherichia coli –Induced TLR2 and TLR4 Activation in a Viability-Dependent Manner
Coorens, M., Schneider, V. A. F., de Groot, A. M., van Dijk, A. I. J. M., Meijerink, M., Wells, J. M., Scheenstra, M. R., Veldhuizen, E. J. A., & Haagsman, H. P. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1602164 · Cited by 96
Effects of the cathelicidin LL-37 on intestinal epithelial barrier integrity
Otte, J., Zdebik, A., Brand, S., Chromik, A. M., Strauß, S., Schmitz, F., Steinstraesser, L., & Schmidt, W. E. (2009) · Regulatory Peptides · doi:10.1016/j.regpep.2009.03.009 · Cited by 94
PU.1 and bacterial metabolites regulate the human gene CAMP encoding antimicrobial peptide LL-37 in colon epithelial cells
Termén, S., Tollin, M., Rodrı́guez, E., Sveinsdóttir, S. H., Jóhannesson, B., Cederlund, A., Sjövall, J., Agerberth, B., & Gudmundsson, G. H. (2008) · Molecular Immunology · doi:10.1016/j.molimm.2008.06.020 · Cited by 96
The Antimicrobial Peptide Cathelicidin Protects Mice from Escherichia coli O157:H7-Mediated Disease
Chromek, M., Arvidsson, I., & Karpman, D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0046476 · Cited by 92
Human antimicrobial peptides in ocular surface defense
Mohammed, I., Said, D. G., & Dua, H. S. (2017) · Progress in Retinal and Eye Research · doi:10.1016/j.preteyeres.2017.03.004 · Cited by 94
Alternatives to antibiotics for farm animals.
Papatsiros, V. G., Katsoulos, P. D., Koutoulis, K. C., Karatzia, M. A., Dedousi, A., & Christodoulopoulos, G. (2014) · CABI Reviews · doi:10.1079/pavsnnr20138032 · Cited by 94
Heterogeneity across the murine small and large intestine
Bowcutt, R. (2014) · World Journal of Gastroenterology · doi:10.3748/wjg.v20.i41.15216 · Cited by 96
The human cathelicidin LL-37: a multifunctional peptide involved in infection and inflammation in the lung
Tjabringa, G. S., Rabe, K. F., & Hiemstra, P. S. (2005) · Pulmonary Pharmacology & Therapeutics · doi:10.1016/j.pupt.2005.01.001 · Cited by 93
Antimicrobial activity of essential oils and five terpenoid compounds against Campylobacter jejuni in pure and mixed culture experiments
Kürekçi, C., Padmanabha, J., Bishop‐Hurley, S. L., Hassan, E., Jassim, R. A. M. A., & McSweeney, C. S. (2013) · International Journal of Food Microbiology · doi:10.1016/j.ijfoodmicro.2013.08.014 · Cited by 88
Cathelicidins and Innate Defense Against Invasive Bacterial Infection
Nizet, V., & Gallo, R. L. (2003) · Scandinavian Journal of Infectious Diseases · doi:10.1080/00365540310015629 · Cited by 90
Host Antimicrobial Defence Peptides in Human Disease
Agerberth, B., & Gudmundsson, G. H. (2006) · Springer eBooks · doi:10.1007/3-540-29916-5_3 · Cited by 88
The bridge of the gut–joint axis: Gut microbial metabolites in rheumatoid arthritis
Xu, X., Wang, M., Wang, Z., Chen, Q., Chen, X., Xu, Y., Dai, M., Wu, B., & Li, Y. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1007610 · Cited by 87
Probiotics in the Intensive Care Unit
Morrow, L. E., Gogineni, V. K., & Malesker, M. A. (2012) · Nutrition in Clinical Practice · doi:10.1177/0884533612440290 · Cited by 84
Effects of probiotic and prebiotic on gastrointestinal motility in newborns.
Indrio, F., Riezzo, G., Raimondi, F., Bisceglia, M., Cavallo, L., & Francavilla, R. (2009) · PubMed · Cited by 82
The dietary histone deacetylase inhibitor sulforaphane induces human β‐defensin‐2 in intestinal epithelial cells
Schwab, M., Reynders, V., Loitsch, S., Steinhilber, D., Schröder, O., & Stein, J. (2008) · Immunology · doi:10.1111/j.1365-2567.2008.02834.x · Cited by 78
MUC2 Mucin and Butyrate Contribute to the Synthesis of the Antimicrobial Peptide Cathelicidin in Response to Entamoeba histolytica- and Dextran Sodium Sulfate-Induced Colitis
Cobo, E. R., Kissoon‐Singh, V., Moreau, F., Holani, R., & Chadee, K. (2017) · Infection and Immunity · doi:10.1128/iai.00905-16 · Cited by 83
Maintaining a Sterile Urinary Tract: The Role of Antimicrobial Peptides
Ali, A., Townes, C. L., Hall, J., & Pickard, R. S. (2009) · The Journal of Urology · doi:10.1016/j.juro.2009.02.124 · Cited by 80
Histone deacetylase inhibition enhances antimicrobial peptide but not inflammatory cytokine expression upon bacterial challenge
Fischer, N., Séchet, E., Friedman, R. C., Amiot, A., Sobhani, I., Nigro, G., Sansonetti, P. J., & Sperandio, B. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1605997113 · Cited by 83
Influences of the Gut Microbiota on DNA Methylation and Histone Modification
Ye, J., Wu, W., Li, Y., & Li, L. (2017) · Digestive Diseases and Sciences · doi:10.1007/s10620-017-4538-6 · Cited by 81
A complex relationship: the interaction among symbiotic microbes, invading pathogens, and their mammalian host
Curtis, M. M., & Sperandio, V. (2011) · Mucosal Immunology · doi:10.1038/mi.2010.89 · Cited by 79
Fecal Biomarkers of Intestinal Health and Disease in Children
Pang, T., Leach, S. T., Katz, T., Day, A. S., & Ooi, C. Y. (2014) · Frontiers in Pediatrics · doi:10.3389/fped.2014.00006 · Cited by 77
Role of Glial Cells in the Functional Expression of LL-37/Rat Cathelin-Related Antimicrobial Peptide in Meningitis
Brandenburg, L., Varoga, D. J., Nicolaeva, N., Leib, S. L., Wilms, H., Podschun, R., Wruck, C. J., Schröder, J., Pufe, T., & Lucius, R. (2008) · Journal of Neuropathology & Experimental Neurology · doi:10.1097/nen.0b013e31818b4801 · Cited by 74
Albumin and amino acids upregulate the expression of human beta-defensin 1
Sherman, H., Chapnik, N., & Froy, O. (2005) · Molecular Immunology · doi:10.1016/j.molimm.2005.09.013 · Cited by 73
Microbiota and gut neuropeptides: a dual action of antimicrobial activity and neuroimmune response
Sanz, J. A., & Aidy, S. E. (2019) · Psychopharmacology · doi:10.1007/s00213-019-05224-0 · Cited by 75
Intestinal colonization: How key microbial players become established in this dynamic process
Aidy, S. E., den Abbeele, P. V., de Wiele, T. V., Louis, P., & Kleerebezem, M. (2013) · BioEssays · doi:10.1002/bies.201300073 · Cited by 74
Immune-epithelial crosstalk at the intestinal surface
Wittkopf, N., Neurath, M. F., & Becker, C. (2014) · Journal of Gastroenterology · doi:10.1007/s00535-013-0929-4 · Cited by 72
Host Directed Therapy Against Infection by Boosting Innate Immunity
Bergman, P., Raqib, R., Rekha, R. S., Agerberth, B., & Gudmundsson, G. H. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.01209 · Cited by 72
Inducing endogenous antimicrobial peptides to battle infections
ZASLOFF, M. A. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0603508103 · Cited by 69
Role of the microbiome and its metabolites in ankylosing spondylitis
Song, Z., Yuan, D., & Zhang, S. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1010572 · Cited by 72
Modern Approaches in Probiotics Research to Control Foodborne Pathogens
Amalaradjou, M. A. R., & Bhunia, A. K. (2012) · Advances in food and nutrition research · doi:10.1016/b978-0-12-394598-3.00005-8 · Cited by 72
Microbiota-derived short-chain fatty acids and modulation of host-derived peptides formation: Focused on host defense peptides
Liu, T., Sun, Z., Yang, Z., & Qiao, X. (2023) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2023.114586 · Cited by 69
Mechanisms linking the human gut microbiome to prophylactic and treatment strategies for COVID-19
Walton, G., Gibson, G. R., & Hunter, K. A. (2020) · British Journal Of Nutrition · doi:10.1017/s0007114520003980 · Cited by 66
Sodium butyrate inhibits Staphylococcus aureus internalization in bovine mammary epithelial cells and induces the expression of antimicrobial peptide genes
Ochoa‐Zarzosa, A., Villarreal-Fernández, E., Cano-Camacho, H., & López-Meza, J. E. (2009) · Microbial Pathogenesis · doi:10.1016/j.micpath.2009.04.006 · Cited by 66
Do Antimicrobial Peptides and Complement Collaborate in the Intestinal Mucosa?
Kopp, Z. A., Jain, U., Limbergen, J. V., & Stadnyk, A. W. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00017 · Cited by 65
Enemies and brothers in arms:Candida albicansand gram-positive bacteria
Förster, T. M., Mogavero, S., Dräger, A., Graf, K., Polke, M., Jacobsen, I. D., & Hube, B. (2016) · Cellular Microbiology · doi:10.1111/cmi.12657 · Cited by 67
Anaerostipes butyraticus sp. nov., an anaerobic, butyrate-producing bacterium from Clostridium cluster XIVa isolated from broiler chicken caecal content, and emended description of the genus Anaerostipes
Eeckhaut, V., Immerseel, F. V., Pasmans, F., Brandt, E. D., Haesebrouck, F., Ducatelle, R., & Vandamme, P. A. R. (2009) · INTERNATIONAL JOURNAL OF SYSTEMATIC AND EVOLUTIONARY MICROBIOLOGY · doi:10.1099/ijs.0.015289-0 · Cited by 64
Different Lipopolysaccharide Branched-Chain Amino Acids Modulate Porcine Intestinal Endogenous β-Defensin Expression through the Sirt1/ERK/90RSK Pathway
Ren, M., Zhang, S., Liu, X., Li, S., Mao, X., Zeng, X., & Qiao, S. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b00968 · Cited by 63
Regulation of the CAMP gene by 1,25(OH)2D3 in various tissues
Gombart, A. F., O’Kelly, J., Saito, T., & Koeffler, H. P. (2006) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2006.12.095 · Cited by 63
Role of nuclear hormone receptors in butyrate-mediated up-regulation of the antimicrobial peptide cathelicidin in epithelial colorectal cells
Schwab, M., Reynders, V., Shastri, Y., Loitsch, S. M., Stein, J. M., & Schröder, O. (2006) · Molecular Immunology · doi:10.1016/j.molimm.2006.09.016 · Cited by 63
Enterohemorrhagic Escherichia coli Pathogenesis and the Host Response
Karpman, D., & Ståhl, A.-L. (2014) · Microbiology Spectrum · doi:10.1128/microbiolspec.ehec-0009-2013 · Cited by 65
Bacterial products increase expression of the human cathelicidin hCAP-18/LL-37 in cultured human sinus epithelial cells
Nell, M. J., Tjabringa, G. S., Vonk, M. J., Hiemstra, P. S., & Grote, J. J. (2004) · FEMS Immunology & Medical Microbiology · doi:10.1016/j.femsim.2004.05.013 · Cited by 61
Probiotic, prebiotic, and synbiotic use in critically ill patients
Morrow, L. E., Gogineni, V. K., & Malesker, M. A. (2012) · Current Opinion in Critical Care · doi:10.1097/mcc.0b013e3283514b17 · Cited by 61
The Anti-inflammatory Immune Regulation Induced by Butyrate Is Impaired in Inflamed Intestinal Mucosa from Patients with Ulcerative Colitis
Magnusson, M. K., Isaksson, S., & Öhman, L. (2019) · Inflammation · doi:10.1007/s10753-019-01133-8 · Cited by 59
Swine-Derived Probiotic Lactobacillus plantarum Modulates Porcine Intestinal Endogenous Host Defense Peptide Synthesis Through TLR2/MAPK/AP-1 Signaling Pathway
Wang, J., Zhang, W., Wang, S., Liu, H., Zhang, D., Wang, Y., & Ji, H. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.02691 · Cited by 59
Antimicrobial Components of the Neonatal Gut Affected Upon Colonization
Kai-Larsen, Y., Bergsson, G., Gudmundsson, G. H., Printz, G., Jörnvall, H., Marchini, G., & Agerberth, B. (2007) · Pediatric Research · doi:10.1203/pdr.0b013e318045be83 · Cited by 59
Antimicrobial Proteins in Intestine and Inflammatory Bowel Diseases
Kim, J. M. (2014) · Intestinal Research · doi:10.5217/ir.2014.12.1.20 · Cited by 57
Microbial Metabolite Dysbiosis and Colorectal Cancer
Niekamp, P., & Kim, C. H. (2023) · Gut and Liver · doi:10.5009/gnl220260 · Cited by 60
Immune and genetic gardening of the intestinal microbiome
Jacobs, J. P., & Braun, J. G. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.02.052 · Cited by 60
Dietary modulation of endogenous host defense peptide synthesis as an alternative approach to in-feed antibiotics
Robinson, K., Ma, X., Liu, Y., Qiao, S., Hou, Y., & Zhang, G. (2018) · Animal nutrition · doi:10.1016/j.aninu.2018.01.003 · Cited by 57
cAMP Stringently Regulates Human Cathelicidin Antimicrobial Peptide Expression in the Mucosal Epithelial Cells by Activating cAMP-response Element-binding Protein, AP-1, and Inducible cAMP Early Repressor
Chakraborty, K., Maity, P. C., Sil, A. K., Takeda, Y., & Das, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.001180 · Cited by 56
The Ussing Type Chamber Model to Study the Intestinal Transport and Modulation of Specific Tight-Junction Genes Using a Colonic Cell Line
Bergmann, H., Rogoll, D., Scheppach, W., Melcher, R., & Richling, E. (2009) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200800498 · Cited by 54
Upregulating Human Cathelicidin Antimicrobial Peptide LL-37 Expression May Prevent Severe COVID-19 Inflammatory Responses and Reduce Microthrombosis
Aloul, K. M., Nielsen, J. E., Defensor, E. B., Lin, J. S., Fortkort, J. A., Shamloo, M., Cirillo, J. D., Gombart, A. F., & Barron, A. E. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.880961 · Cited by 54
Differential regulation of human cathelicidin LL-37 by free fatty acids and their analogs
Jiang, W., Sunkara, L. T., Zeng, X., Deng, Z., Myers, S. M., & Zhang, G. (2013) · Peptides · doi:10.1016/j.peptides.2013.10.008 · Cited by 54
Advances in the mechanisms of polysaccharides in alleviating depression and its complications
Guo, Y., Chen, X., Gong, P., Li, Z., Wu, Y., Zhang, J., Wang, J., Yao, W., Yang, W., & Chen, F. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154566 · Cited by 55
ZBP-89 Regulates Expression of Tryptophan Hydroxylase I and Mucosal Defense Against Salmonella Typhimurium in Mice
Essien, B. E., Grasberger, H., Romain, R. D., Law, D., Veniaminova, N. A., Saqui–Salces, M., Zaatari, M. E., Tessier, A. J., Hayes, M. M., Yang, A. C., et al. (2013) · Gastroenterology · doi:10.1053/j.gastro.2013.01.057 · Cited by 53
The Network of Colonic Host Defense Peptides as an Innate Immune Defense Against Enteropathogenic Bacteria
Blyth, G. A. D., Connors, L. T., Fodor, C. C., & Cobo, E. R. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00965 · Cited by 59
Epithelial regulation of microbiota-immune cell dynamics
Didriksen, B. J., Eshleman, E. M., & Alenghat, T. (2024) · Mucosal Immunology · doi:10.1016/j.mucimm.2024.02.008 · Cited by 54
Topical treatment with the vitamin D analogue calcipotriol enhances the upregulation of the antimicrobial protein hCAP18/LL‐37 during wounding in human skin in vivo
Heilborn, J. D., Weber, G., Grönberg, A., Dieterich, C., & Ståhle, M. (2009) · Experimental Dermatology · doi:10.1111/j.1600-0625.2009.00997.x · Cited by 54
Drosophila as a Model for Human Diseases—Focus on Innate Immunity in Barrier Epithelia
Bergman, P., Esfahani, S. S., & Engström, Y. (2016) · Current topics in developmental biology/Current Topics in Developmental Biology · doi:10.1016/bs.ctdb.2016.07.002 · Cited by 56
Pharmaconutrition Review: Physiological Mechanisms
Pierre, J. F., Heneghan, A. F., Lawson, C. M., Wischmeyer, P. E., Kozar, R. A., & Kudsk, K. A. (2013) · Journal of Parenteral and Enteral Nutrition · doi:10.1177/0148607113493326 · Cited by 51
Fungal Dysbiosis and Intestinal Inflammation in Children With Beta-Cell Autoimmunity
Honkanen, J. K., Vuorela, A., Muthas, D., Orivuori, L., Luopajärvi, K., Tejesvi, M. V., Lavrinienko, A., Pirttilä, A. M., Fogarty, C. L., Härkönen, T., et al. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.00468 · Cited by 51
Cyclic AMP synergizes with butyrate in promoting β-defensin 9 expression in chickens
Sunkara, L. T., Zeng, X., Curtis, A. R., & Zhang, G. (2013) · Molecular Immunology · doi:10.1016/j.molimm.2013.09.003 · Cited by 51
Entinostat up-regulates the CAMP gene encoding LL-37 via activation of STAT3 and HIF-1α transcription factors
Miraglia, E., Nylén, F., Johansson, K., Arnér, E. S. J., Cebula, M., Farmand, S., Ottosson, H., Strömberg, R., Gudmundsson, G. H., Agerberth, B., et al. (2016) · Scientific Reports · doi:10.1038/srep33274 · Cited by 50
Antimicrobial and immune-modulatory effects of vitamin D provide promising antibiotics-independent approaches to tackle bacterial infections – lessons learnt from a literature survey
Golpour, A., Bereswill, S., & Heimesaat, M. M. (2019) · European Journal of Microbiology and Immunology · doi:10.1556/1886.2019.00014 · Cited by 52
Past, Present, and Future of Gastrointestinal Microbiota Research in Cats
Lyu, Y., Su, C., Verbrugghe, A., de Wiele, T. V., Martinez-Caja, A. M., & Hesta, M. (2020) · Frontiers in Microbiology · doi:10.3389/fmicb.2020.01661 · Cited by 55
Animal Health: Global Antibiotic Issues
Peng, M., Salaheen, S., & Biswas, D. (2014) · Elsevier eBooks · doi:10.1016/b978-0-444-52512-3.00187-x · Cited by 50
Controversies in the management of the critically ill: the role of probiotics
Θεοδωρακοπούλου, Μ., Perros, E., Giamarellos‐Bourboulis, E. J., & Dimοpoulos, G. (2013) · International Journal of Antimicrobial Agents · doi:10.1016/j.ijantimicag.2013.04.010 · Cited by 48
A review of the innate immune defence of the human foetus and newborn, with the emphasis on antimicrobial peptides
Kai-Larsen, Y., Gudmundsson, G. H., & Agerberth, B. (2014) · Acta Paediatrica · doi:10.1111/apa.12700 · Cited by 47
The potential for immunoglobulins and host defense peptides (HDPs) to reduce the use of antibiotics in animal production
van Dijk, A. I. J. M., Hedegaard, C. J., Haagsman, H. P., & Heegaard, P. M. H. (2018) · Veterinary Research · doi:10.1186/s13567-018-0558-2 · Cited by 47
First line of defense in early human life
Yoshio, H., Lagercrantz, H., Gudmundsson, G. H., & Agerberth, B. (2004) · Seminars in Perinatology · doi:10.1053/j.semperi.2004.08.008 · Cited by 48
The impact of gut microbiome-targeted therapy on liver enzymes in patients with nonalcoholic fatty liver disease: an umbrella meta-analysis
Amini-Salehi, E., Hassanipour, S., Keivanlou, M.-H., Shahdkar, M., Orang Goorabzarmakhi, M., Vakilpour, A., Joukar, F., Hashemi, M., Sattari, N., Javid, M., et al. (2024) · Nutrition Reviews · doi:10.1093/nutrit/nuad086 · Cited by 42
Expression of human cathelicidin peptide LL-37 in inflammatory bowel disease
Kusaka, S., Nishida, A., Takahashi, K., Bamba, S., Yasui, H., Kawahara, M., Inatomi, O., Sugimoto, M., & Andoh, A. (2017) · Clinical & Experimental Immunology · doi:10.1111/cei.13047 · Cited by 42
Amniotic Fluid Cathelicidin in PPROM Pregnancies: From Proteomic Discovery to Assessing Its Potential in Inflammatory Complications Diagnosis
Tambor, V., Kacerovský, M., Andrýs, C., Musilova, I. K., Hornychová, H., Plíšková, L., Link, M., Stulík, J., & Lenčo, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041164 · Cited by 40
Antimicrobial resistance in livestock: antimicrobial peptides provide a new solution for a growing challenge
Li, Z., Hu, Y., Yang, Y., Lu, Z., & Wang, Y. (2018) · Animal Frontiers · doi:10.1093/af/vfy005 · Cited by 40
A 21st century evaluation of the safety of oral vitamin D
Glade, M. J. (2012) · Nutrition · doi:10.1016/j.nut.2011.11.006 · Cited by 40
Contribution of microbiota to the intestinal physicochemical barrier
Malago, J. J. (2014) · Beneficial Microbes · doi:10.3920/bm2014.0041 · Cited by 40
Potent Inducers of Endogenous Antimicrobial Peptides for Host Directed Therapy of Infections
Ottosson, H., Nylén, F., Sarker, P., Miraglia, E., Bergman, P., Gudmundsson, G. H., Raqib, R., Agerberth, B., & Strömberg, R. (2016) · Scientific Reports · doi:10.1038/srep36692 · Cited by 38
Inducible expression of defensins and cathelicidins by nutrients and associated regulatory mechanisms
Chen, J., Zhai, Z., Long, H., Yang, G., Deng, B., & Deng, J. (2019) · Peptides · doi:10.1016/j.peptides.2019.170177 · Cited by 38
Effects of Probiotics Lactobacillus reuteri and Clostridium butyricum on the Expression of Toll-like Receptors, Pro- and Anti-inflammatory Cytokines, and Antimicrobial Peptides in Broiler Chick Intestine
Terada, T., Nii, T., Isobe, N., & Yoshimura, Y. (2019) · The Journal of Poultry Science · doi:10.2141/jpsa.0190098 · Cited by 38
Two intestinal microbiota-derived metabolites, deoxycholic acid and butyrate, synergize to enhance host defense peptide synthesis and alleviate necrotic enteritis
Kim, D. M., Liu, J., Whitmore, M. A., Tobin, I., Zhao, Z., & Zhang, G. (2024) · Journal of Animal Science and Biotechnology/Journal of animal science and biotechnology · doi:10.1186/s40104-024-00995-9 · Cited by 37
A literature survey on antimicrobial and immune-modulatory effects of butyrate revealing non-antibiotic approaches to tackle bacterial infections
Du, K., Bereswill, S., & Heimesaat, M. M. (2021) · European Journal of Microbiology and Immunology · doi:10.1556/1886.2021.00001 · Cited by 36
Rewiring host–microbe interactions and barrier function during gastrointestinal inflammation
Yang-Jensen, S. K., Pærregaard, S. I., Brandum, E. P., Jørgensen, A. S., Hjortø, G. M., & Jensen, B. A. H. (2022) · Gastroenterology report · doi:10.1093/gastro/goac008 · Cited by 38
The activation of the TLR2/p38 pathway by sodium butyrate in bovine mammary epithelial cells is involved in the reduction of Staphylococcus aureus internalization
Alva-Murillo, N., Medina-Estrada, I., Báez-Magaña, M., Ochoa‐Zarzosa, A., & López-Meza, J. E. (2015) · Molecular Immunology · doi:10.1016/j.molimm.2015.09.025 · Cited by 36
Trace metal zinc stimulates secretion of antimicrobial peptide LL-37 from Caco-2 cells through ERK and p38 MAP kinase
Talukder, P., Satho, T., Irie, K., Sharmin, T., Dieng, H., Nakashima, Y., Kashige, N., & Miake, F. (2010) · International Immunopharmacology · doi:10.1016/j.intimp.2010.10.010 · Cited by 35
The Effect of Lactobacillus casei 32G on the Mouse Cecum Microbiota and Innate Immune Response Is Dose and Time Dependent
Aktaş, B., Wolfe, T. J. D., Tandee, K., Safdar, N., Darien, B. J., & Steele, J. L. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145784 · Cited by 34
The Microbiome as a Potential Target for Therapeutic Manipulation in Pancreatic Cancer
Rahman, R. A., Lamarca, Á., Hubner, R. A., Valle, J. W., & McNamara, M. G. (2021) · Cancers · doi:10.3390/cancers13153779 · Cited by 35

Authors: Schauber, J.
Affiliations: University of Würzburg (DE)
Corresponding author: Schauber, J
Venue: Gut
Publisher: BMJ
Published: 2003-05-01
Volume: 52
Issue: 5
Pages: 735-741
ISSN: 0017-5749 (ISSN-L)
DOI: 10.1136/gut.52.5.735
PMC: PMC1773650
OpenAlex: W2130246343
Cited by: 383
References: 41
Citations by year: 2026: 10 · 2025: 11 · 2024: 15 · 2023: 21 · 2022: 27 · 2021: 15 · 2020: 24 · 2019: 25 · 2018: 23 · 2017: 17 · 2016: 21 · 2015: 12 · 2014: 20 · 2013: 17 · 2012: 19
FWCI: 8.91
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Gut (publishedVersion)
PubMed Central (publishedVersion)
PubMed (publishedVersion)
HighWire Press Open Archive (submittedVersion)
Funders: Boehringer Ingelheim Fonds
Deutsche Forschungsgemeinschaft
Stiftelsen för Strategisk Forskning
Karolinska Institutet
Julius-Maximilians-Universität Würzburg
Medical Research Council
Topics: Life Sciences › Immunology and Microbiology › Microbiology › Antimicrobial Peptides and Activities
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Gut microbiota and health
Life Sciences › Agricultural and Biological Sciences › Food Science › Probiotics and Fermented Foods
Keywords: cathelicidin LL-37, short-chain fatty acids, colonic epithelial cells, butyrate, MEK/ERK signaling, p38 MAPK, flavones, alkaline phosphatase activity, mucosal immunity
MeSH terms: Adult, Alkaline Phosphatase, Biopsy, Butyrates, Cell Differentiation, Cell Line, Colon, Epithelial Cells, Fatty Acids, Volatile, Flavonoids, Humans, Hydroxamic Acids, Immunohistochemistry, Intestinal Mucosa, Protein Kinases, Protein Synthesis Inhibitors, Signal Transduction, Apoptosis, Reverse Transcriptase Polymerase Chain Reaction, Antimicrobial Cationic Peptides, Flavones, Cathelicidins

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Expression of the cathelicidin LL-37 is modulated by short chain fatty acids in colonocytes: relevance of signalling pathways

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Self-check

Citations

Cites

Cited by

Related

Metadata

Record

About these checks