PU.1 and bacterial metabolites regulate the human gene CAMP encoding antimicrobial peptide LL-37 in colon epithelial cells

Molecular Immunology

Volumn 45, Issue 15, 2008, Pages 3947-3955

  Termén, Stefan ^a,b   Tollin, Maria ^b   Rodriguez, Eduardo ^a   Sveinsdóttir, Sigrún H ^a   Jóhannesson, Bjarki ^a   Cederlund, Andreas ^b   Sjövall, Jan ^b   Agerberth, Birgitta ^b   Gudmundsson, Gudmundur H ^a  

^a UNIVERSITY OF ICELAND   (Iceland)

^b KAROLINSKA INSTITUTE   (Sweden)

Author keywords

Cathelicidin; Gene regulation; Host microbe crosstalk; Mucosal immunity; Nuclear receptors

Indexed keywords

BUTYRIC ACID; CATHELICIDIN ANTIMICROBIAL PEPTIDE LL 37; LITHOCHOLIC ACID; LUCIFERASE; TRANSCRIPTION FACTOR ETS; TRANSCRIPTION FACTOR PU 1; VITAMIN D;

ARTICLE; CAMP GENE; CELL STRAIN HT29; CHROMATIN IMMUNOPRECIPITATION; COLON MUCOSA; CONTROLLED STUDY; GENE; GENE CONTROL; GENE EXPRESSION; GENE INDUCTION; GENE INSERTION; GENETIC TRANSCRIPTION; HOMEOSTASIS; HOST RESISTANCE; HUMAN; HUMAN CELL; INNATE IMMUNITY; INTRON; METABOLITE; MOLECULAR INTERACTION; MUCOSAL IMMUNITY; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROMOTER REGION; REGULATORY SEQUENCE; REPORTER GENE;

ANTIMICROBIAL CATIONIC PEPTIDES; BASE SEQUENCE; BUTYRATES; CELL LINE; CHROMATIN IMMUNOPRECIPITATION; COLON; ENHANCER ELEMENTS, GENETIC; EPITHELIAL CELLS; GENE EXPRESSION REGULATION; HUMANS; INTRONS; LITHOCHOLIC ACID; MOLECULAR SEQUENCE DATA; PROMOTER REGIONS, GENETIC; PROTO-ONCOGENE PROTEINS; TRANS-ACTIVATORS;

BACTERIA (MICROORGANISMS); MAMMALIA;

EID: 49449112567     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2008.06.020     Document Type: Article

References (34)

1. Adachi R., Honma Y., Masuno H., Kawana K., Shimomura I., Yamada S., and Makishima M. Selective activation of vitamin D receptor by lithocholic acid acetate, a bile acid derivative. J. Lipid Res. 46 (2005) 46-57
2. Agerberth B., and Gudmundsson G.H. Host antimicrobial defence peptides in human disease. Curr. Top. Microbiol. Immunol. 306 (2006) 67-90
3. Agerberth B., Gunne H., Odeberg J., Kogner P., Boman H.G., and Gudmundsson G.H. FALL-39, a putative human peptide antibiotic, is cysteine-free and expressed in bone marrow and testis. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 195-199
4. Bals R., and Wilson J.M. Cathelicidins-a family of multifunctional antimicrobial peptides. Cell Mol. Life Sci. 60 (2003) 711-720
5. Davie J.R. Inhibition of histone deacetylase activity by butyrate. J. Nutr. 133 (2003) 2485S-2493S
6. Elloumi H.Z., and Holland S.M. Complex regulation of human cathelicidin gene expression: novel splice variants and 5′UTR negative regulatory element. Mol. Immunol. 45 (2008) 204-217
7. Fauci A.S. Infectious diseases: considerations for the 21st century. Clin. Infect. Dis. 32 (2001) 675-685
8. Friedman A.D. Transcriptional control of granulocyte and monocyte development. Oncogene 26 (2007) 6816-6828
9. Frohm M., Agerberth B., Ahangari G., Stahle-Backdahl M., Liden S., Wigzell H., and Gudmundsson G.H. The expression of the gene coding for the antibacterial peptide LL-37 is induced in human keratinocytes during inflammatory disorders. J. Biol. Chem. 272 (1997) 15258-15263
10. Gombart A.F., Borregaard N., and Koeffler H.P. 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 D3. FASEB J. 19 (2005) 1067-1077
11. Gudmundsson G.H., Agerberth B., Odeberg J., Bergman T., Olsson B., and Salcedo R. The human gene FALL39 and processing of the cathelin precursor to the antibacterial peptide LL-37 in granulocytes. Eur. J. Biochem. 238 (1996) 325-332
12. Gudmundsson G.H., Magnusson K.P., Chowdhary B.P., Johansson M., Andersson L., and Boman H.G. Structure of the gene for porcine peptide antibiotic PR-39, a cathelin gene family member: comparative mapping of the locus for the human peptide antibiotic FALL-39. Proc. Natl. Acad. Sci. U.S.A. 92 (1995) 7085-7089
13. Hase K., Eckmann L., Leopard J.D., Varki N., and Kagnoff M.F. Cell differentiation is a key determinant of cathelicidin LL-37/human cationic antimicrobial protein 18 expression by human colon epithelium. Infect. Immun. 70 (2002) 953-963
14. Hornef M.W., Normark B.H., Vandewalle A., and Normark S. Intracellular recognition of lipopolysaccharide by toll-like receptor 4 in intestinal epithelial cells. J. Exp. Med. 198 (2003) 1225-1235
15. Inagaki T., Moschetta A., Lee Y.K., Peng L., Zhao G., Downes M., Yu R.T., Shelton J.M., Richardson J.A., Repa J.J., Mangelsdorf D.J., and Kliewer S.A. Regulation of antibacterial defense in the small intestine by the nuclear bile acid receptor. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 3920-3925
16. Islam D., Bandholtz L., Nilsson J., Wigzell H., Christensson B., Agerberth B., and Gudmundsson G. Downregulation of bactericidal peptides in enteric infections: a novel immune escape mechanism with bacterial DNA as a potential regulator. Nat. Med. 7 (2001) 180-185
17. Kida Y., Shimizu T., and Kuwano K. Sodium butyrate up-regulates cathelicidin gene expression via activator protein-1 and histone acetylation at the promoter region in a human lung epithelial cell line, EBC-1. Mol. Immunol. 43 (2006) 1972-1981
18. Lennartsson A., Pieters K., Ullmark T., Vidovic K., and Gullberg U. AML-1, PU.1, and Sp3 regulate expression of human bactericidal/permeability-increasing protein. Biochem. Biophys. Res. Commun. 311 (2003) 853-863
19. Ley R.E., Peterson D.A., and Gordon J.I. Ecological and evolutionary forces shaping microbial diversity in the human intestine. Cell 124 (2006) 837-848
20. Ma Y., Su Q., and Tempst P. Differentiation-stimulated activity binds an ETS-like, essential regulatory element in the human promyelocytic defensin-1 promoter. J. Biol. Chem. 273 (1998) 8727-8740
21. Makishima M., Lu T.T., Xie W., Whitfield G.K., Domoto H., Evans R.M., Haussler M.R., and Mangelsdorf D.J. Vitamin D receptor as an intestinal bile acid sensor. Science 296 (2002) 1313-1316
22. Miranda M.B., Xu H., Torchia J.A., and Johnson D.E. Cytokine-induced myeloid differentiation is dependent on activation of the MEK/ERK pathway. Leuk. Res. 29 (2005) 1293-1306
23. Ogawa S., Lozach J., Benner C., Pascual G., Tangirala R.K., Westin S., Hoffmann A., Subramaniam S., David M., Rosenfeld M.G., and Glass C.K. Molecular determinants of crosstalk between nuclear receptors and toll-like receptors. Cell 122 (2005) 707-721
24. Ramanathan B., Minton J.E., Ross C.R., and Blecha F. PU.1-mediated transcriptional regulation of prophenin-2 in primary bone marrow cells. Gene 352 (2005) 1-9
25. Raqib R., Sarker P., Bergman P., Ara G., Lindh M., Sack D.A., Nasirul Islam K.M., Gudmundsson G.H., Andersson J., and Agerberth B. Improved outcome in shigellosis associated with butyrate induction of an endogenous peptide antibiotic. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 9178-9183
26. Sambrook J., and Russell D.W. Molecular Cloning-A Laboratory Manual (2001), Cold Spring Harbor Laboratory Press, Cold Spring Harbor
27. Schauber J., Svanholm C., Termen S., Iffland K., Menzel T., Scheppach W., Melcher R., Agerberth B., Luhrs H., and Gudmundsson G.H. Expression of the cathelicidin LL-37 is modulated by short chain fatty acids in colonocytes: relevance of signalling pathways. Gut 52 (2003) 735-741
28. Teng C.T. Factors regulating lactoferrin gene expression. Biochem. Cell Biol. 84 (2006) 263-267
29. Verbeek W., Lekstrom-Himes J., Park D.J., Dang P.M., Vuong P.T., Kawano S., Babior B.M., Xanthopoulos K., and Koeffler H.P. Myeloid transcription factor C/EBP epsilon is involved in the positive regulation of lactoferrin gene expression in neutrophils. Blood 94 (1999) 3141-3150
30. Wachtershauser A., and Stein J. Rationale for the luminal provision of butyrate in intestinal diseases. Eur. J. Nutr. 39 (2000) 164-171
31. Wang T.T., Nestel F.P., Bourdeau V., Nagai Y., Wang Q., Liao J., Tavera-Mendoza L., Lin R., Hanrahan J.H., Mader S., and White J.H. Cutting edge: 1, 25-dihydroxyvitamin D3 is a direct inducer of antimicrobial peptide gene expression. J. Immunol. 173 (2004) 2909-2912
32. Wehkamp J., Salzman N.H., Porter E., Nuding S., Weichenthal M., Petras R.E., Shen B., Schaeffeler E., Schwab M., Linzmeier R., Feathers R.W., Chu H., Lima Jr. H., Fellermann K., Ganz T., Stange E.F., and Bevins C.L. Reduced Paneth cell alpha-defensins in ileal Crohn's disease. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 18129-18134
33. Wu H., Ross C.R., and Blecha F. Characterization of an upstream open reading frame in the 5′ untranslated region of PR-39, a cathelicidin antimicrobial peptide. Mol. Immunol. 39 (2002) 9-18
34. Zasloff M. Antimicrobial peptides of multicellular organisms. Nature 415 (2002) 389-395