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

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

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Schauber, J·2003·Gut

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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.

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A peptide antibiotic from human skin
Harder, J., Bartels, J., Christophers, E., & Schröder, J. ‐. (1997) · Nature · doi:10.1038/43088 · Cited by 1,365
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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
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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
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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

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Show all 41 references

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Sekirov, I., Russell, S. L., Antunes, L. C. M., & Finlay, B. B. (2010) · Physiological Reviews · doi:10.1152/physrev.00045.2009 · Cited by 4,182
The gut microbiota--masters of host development and physiology
Sommer, F., & Bäckhed, F. (2013) · Nature Reviews Microbiology · doi:10.1038/nrmicro2974 · Cited by 3,681
Role of the normal gut microbiota
Jandhyala, S. M. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i29.8787 · Cited by 3,001
Review article: the role of butyrate on colonic function
HAMER, H. M., JONKERS, D., VENEMA, K., VANHOUTVIN, S., TROOST, F. J., & BRUMMER, R. ‐. (2008) · Alimentary Pharmacology & Therapeutics · doi:10.1111/j.1365-2036.2007.03562.x · Cited by 2,721
Potential beneficial effects of butyrate in intestinal and extraintestinal diseases
Canani, R. B. (2011) · World Journal of Gastroenterology · doi:10.3748/wjg.v17.i12.1519 · Cited by 1,381
Regulation of immune cell function by short‐chain fatty acids
Corrêa‐Oliveira, R., Fachi, J. L., Vieira, A., Sato, F. T., & Vinolo, M. A. R. (2016) · Clinical & Translational Immunology · doi:10.1038/cti.2016.17 · Cited by 1,346
Butyrate: A Double-Edged Sword for Health?
Liu, H., Wang, J., He, T., Becker, S. R., Zhang, G., Li, D., & Ma, X. (2018) · Advances in Nutrition · doi:10.1093/advances/nmx009 · Cited by 1,185
Human cathelicidin antimicrobial peptide (CAMP) gene is a direct target of the vitamin D receptor and is strongly up‐regulated in myeloid cells by 1,25‐dihydroxyvitamin D 3
Gombart, A. F., Borregaard, N., & Koeffler, H. P. (2005) · The FASEB Journal · doi:10.1096/fj.04-3284com · Cited by 1,145
Diet, microorganisms and their metabolites, and colon cancer
O'Keefe, S. J. D. (2016) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/nrgastro.2016.165 · Cited by 1,100
LL-37, the only human member of the cathelicidin family of antimicrobial peptides
Dürr, U. H. N., Sudheendra, U. S., & Ramamoorthy, A. (2006) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/j.bbamem.2006.03.030 · Cited by 1,049
Epithelial antimicrobial defence of the skin and intestine
Gallo, R. L., & Hooper, L. V. (2012) · Nature reviews. Immunology · doi:10.1038/nri3228 · Cited by 1,020
Gut Microbial Metabolites Fuel Host Antibody Responses
Kim, M., Qie, Y., Park, J., & Kim, C. H. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.07.001 · Cited by 893
“SCFAs support epithelial cell integrity, innate immune functions, and the generation of regulatory and effector T cells (Arpaia et al., 2013; Furusawa et al., 2013; Kim et al., 2013; Park et al., 2015; Sakata, 1987; Schauber et al., 2003).”
Background
The Human Microbiota in Health and Disease
Wang, B., Yao, M., Lv, L., Ling, Z., & Li, L. (2017) · Engineering · doi:10.1016/j.eng.2017.01.008 · Cited by 916
Probiotic bacteria and intestinal epithelial barrier function
Ohland, C., & MacNaughton, W. K. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00243.2009 · Cited by 832
An update on alternatives to antimicrobial growth promoters for broilers
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Neutrophil granules: a library of innate immunity proteins
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Systematic Review of Gut Microbiota and Major Depression
Cheung, S. G., Goldenthal, A. R., Uhlemann, A.-C., Mann, J. J., Miller, J. M., & Sublette, M. E. (2019) · Frontiers in Psychiatry · doi:10.3389/fpsyt.2019.00034 · Cited by 597
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Multiple roles of antimicrobial defensins, cathelicidins, and eosinophil-derived neurotoxin in host defense
Yang, D., Biragyn, A., Hoover, D. M., Lubkowski, J., & Oppenheim, J. J. (2004) · Annual Review of Immunology · doi:10.1146/annurev.immunol.22.012703.104603 · Cited by 572
The Front Line of Enteric Host Defense against Unwelcome Intrusion of Harmful Microorganisms: Mucins, Antimicrobial Peptides, and Microbiota
Liévin-Le Moal, V., & Servin, A. L. (2006) · Clinical Microbiology Reviews · doi:10.1128/cmr.19.2.315-337.2006 · Cited by 568
Antimicrobial peptides: General overview and clinical implications in human health and disease
Guaní-Guerra, E., Santos-Mendoza, T., Reyes, S. O. L., & Teran, L. M. (2010) · Clinical Immunology · doi:10.1016/j.clim.2009.12.004 · Cited by 571
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Zhao, Y., Chen, F., Wu, W. H., Sun, M., Bilotta, A. J., Yao, S., Xiao, Y., Huang, X., Eaves-Pyles, T. D., Golovko, G., et al. (2018) · Mucosal Immunology · doi:10.1038/mi.2017.118 · Cited by 536
Respiratory viral infection-induced microbiome alterations and secondary bacterial pneumonia.
Hanada, S., Pirzadeh, M., Carver, K. Y., & Deng, J. C. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.02640 · Cited by 495
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Wang, J., Ji, H., Wang, S., Liu, H., Zhang, W., Zhang, D., & Wang, Y. (2018) · Frontiers in Microbiology · doi:10.3389/fmicb.2018.01953 · Cited by 463
The Vitamin D–Antimicrobial Peptide Pathway and its Role in Protection Against Infection
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Singh, A. K., Cabral, C., Kumar, R., Ganguly, R., Rana, H. K., Gupta, A., Lauro, M. R., Carbone, C., Reis, F., & Pandey, A. K. (2019) · Nutrients · doi:10.3390/nu11092216 · Cited by 454
Surface components and metabolites of probiotics for regulation of intestinal epithelial barrier
Liu, Q., Yu, Z., Tian, F., Zhao, J., Zhang, H., Zhai, Q., & Chen, W. (2020) · Microbial Cell Factories · doi:10.1186/s12934-020-1289-4 · Cited by 456
The epigenetic effects of butyrate: potential therapeutic implications for clinical practice
Berni Canani, R., Di Costanzo, M., & Leone, L. (2012) · Clinical Epigenetics · doi:10.1186/1868-7083-4-4 · Cited by 431
Wound healing in the 21st century
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The Role of Cathelicidins in the Innate Host Defenses of Mammals
Zanetti, M. (2005) · Current Issues in Molecular Biology · doi:10.21775/cimb.007.179 · Cited by 414
Immune regulation by microbiome metabolites
Kim, C. H. (2018) · Immunology · doi:10.1111/imm.12930 · Cited by 375
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Haney, E. F., Straus, S. K., & Hancock, R. E. W. (2019) · Frontiers in Chemistry · doi:10.3389/fchem.2019.00043 · Cited by 376
Exploring the Human Microbiome: The Potential Future Role of Next-Generation Sequencing in Disease Diagnosis and Treatment
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Induction of cathelicidin in normal and CF bronchial epithelial cells by 1,25-dihydroxyvitamin D3
Yim, S., Dhawan, P., Ragunath, C., Christakos, S., & Diamond, G. (2007) · Journal of Cystic Fibrosis · doi:10.1016/j.jcf.2007.03.003 · Cited by 347
Intestinal epithelial vitamin D receptor deletion leads to defective autophagy in colitis
Wu, S., Zhang, Y., Lu, R., Xia, Y., Zhou, D., Petrof, E. O., Claud, E. C., Chen, D., Chang, E. B., Carmeliet, G., et al. (2014) · Gut · doi:10.1136/gutjnl-2014-307436 · Cited by 353
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Xu, J., Chen, H., & Li, S. (2017) · Medicinal Research Reviews · doi:10.1002/med.21431 · Cited by 346
EMA and EFSA Joint Scientific Opinion on measures to reduce the need to use antimicrobial agents in animal husbandry in the European Union, and the resulting impacts on food safety (RONAFA)
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Improved outcome in shigellosis associated with butyrate induction of an endogenous peptide antibiotic
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Untitled work
(2016) · PubMed · Cited by 287
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Alli, S. R., Gorbovskaya, I., Liu, J. C. W., Kolla, N. J., Brown, L., & Müller, D. J. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094494 · Cited by 202
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Timbermont, L., Lanckriet, A., Dewulf, J., Nollet, N., Schwarzer, K., Haesebrouck, F., Ducatelle, R., & Immerseel, F. V. (2010) · Avian Pathology · doi:10.1080/03079451003610586 · Cited by 201
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Sun, L., Zhang, X., Zhang, Y., Zheng, K., Xiang, Q., Chen, N., Chen, Z., Zhang, N., Zhu, J., & He, Q. (2019) · Frontiers in Cellular and Infection Microbiology · doi:10.3389/fcimb.2019.00099 · Cited by 186
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Self-citation
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Self-citation
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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

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

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